Skip to main content
Advertisement

Main menu

  • Home
  • Articles
    • Accepted manuscripts
    • Issue in progress
    • Latest complete issue
    • Issue archive
    • Archive by article type
    • Special issues
    • Subject collections
    • Cell Scientists to Watch
    • First Person
    • Sign up for alerts
  • About us
    • About JCS
    • Editors and Board
    • Editor biographies
    • Travelling Fellowships
    • Grants and funding
    • Journal Meetings
    • Workshops
    • The Company of Biologists
    • Journal news
  • For authors
    • Submit a manuscript
    • Aims and scope
    • Presubmission enquiries
    • Fast-track manuscripts
    • Article types
    • Manuscript preparation
    • Cover suggestions
    • Editorial process
    • Promoting your paper
    • Open Access
    • JCS Prize
    • Manuscript transfer network
    • Biology Open transfer
  • Journal info
    • Journal policies
    • Rights and permissions
    • Media policies
    • Reviewer guide
    • Sign up for alerts
  • Contacts
    • Contact JCS
    • Subscriptions
    • Advertising
    • Feedback
    • For library administrators
  • COB
    • About The Company of Biologists
    • Development
    • Journal of Cell Science
    • Journal of Experimental Biology
    • Disease Models & Mechanisms
    • Biology Open

User menu

  • Log in
  • Log out

Search

  • Advanced search
Journal of Cell Science
  • COB
    • About The Company of Biologists
    • Development
    • Journal of Cell Science
    • Journal of Experimental Biology
    • Disease Models & Mechanisms
    • Biology Open

supporting biologistsinspiring biology

Journal of Cell Science

  • Log in
Advanced search

RSS   Twitter  Facebook   YouTube  

  • Home
  • Articles
    • Accepted manuscripts
    • Issue in progress
    • Latest complete issue
    • Issue archive
    • Archive by article type
    • Special issues
    • Subject collections
    • Cell Scientists to Watch
    • First Person
    • Sign up for alerts
  • About us
    • About JCS
    • Editors and Board
    • Editor biographies
    • Travelling Fellowships
    • Grants and funding
    • Journal Meetings
    • Workshops
    • The Company of Biologists
    • Journal news
  • For authors
    • Submit a manuscript
    • Aims and scope
    • Presubmission enquiries
    • Fast-track manuscripts
    • Article types
    • Manuscript preparation
    • Cover suggestions
    • Editorial process
    • Promoting your paper
    • Open Access
    • JCS Prize
    • Manuscript transfer network
    • Biology Open transfer
  • Journal info
    • Journal policies
    • Rights and permissions
    • Media policies
    • Reviewer guide
    • Sign up for alerts
  • Contacts
    • Contact JCS
    • Subscriptions
    • Advertising
    • Feedback
    • For library administrators
Journal Articles
Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium
F. Rivero, R. Furukawa, M. Fechheimer, A.A. Noegel
Journal of Cell Science 1999 112: 2737-2751;
F. Rivero
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
R. Furukawa
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
M. Fechheimer
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
A.A. Noegel
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Info & metrics
  • PDF
Loading

Summary

The contribution of three actin cross-linking proteins, alpha-actinin (alphaA), gelation factor (ABP-120), and the 34 kDa actin-bundling protein to cellular functions has been studied in three single mutant (alphaA-, 120-, and 34-) and three double mutant (alphaA-/120-, 34-/alphaA-, 34-/120-) strains of Dictyostelium generated by homologous recombination. Strains alphaA-/120- and 34-/alphaA- exhibited a reduced rate of pinocytosis, grew to lower saturation densities, and produced small cells in shaking cultures. All strains grew normally in bacterial suspensions and on agar plates with a bacterial lawn. Slow growth under conditions of reduced temperature and increased osmolarity was observed in single mutants 34- and alphaA-, respectively, as well as in some of the double mutant strains. Motility, chemotaxis, and development were largely unaltered in 34-/alphaA- and 34-/120- cells. However, 34-/alphaA- cells showed enhanced aggregation when starved in suspension. Moreover, morphogenesis was impaired in both double mutant strains and fruiting bodies of aberrant morphology were observed. These defects were reverted by re-expression of one of the lacking cross-linking proteins. The additive and synthetic phenotypes of these mutations indicate that actin cross-linking proteins serve both unique and overlapping functions in the actin cytoskeleton.

  • © 1999 by Company of Biologists

REFERENCES

    1. Adachi H.,
    2. Hasebe T.,
    3. Yoshinaga K.,
    4. Ohta T. and
    5. Sutoh K.
    (1994). Isolation of Dictyostelium discoideum cytokinesis mutants by restriction enzyme-mediated integration of the blasticidin S resistance marker. Biochem. Biophys. Res. Commun 205, 1808–1814
    OpenUrlCrossRefPubMedWeb of Science
    1. Adams A. E. M.,
    2. Cooper J. A. and
    3. Drubin D. G.
    (1993). Unexpected combinations of null mutations in genes encoding the actin cytoskeleton are lethal in yeast. Mol. Biol. Cell 4, 459–468
    OpenUrlAbstract/FREE Full Text
    1. Adessi C.,
    2. Chapel A.,
    3. Vincon M.,
    4. Rabilloud T.,
    5. Klein G.,
    6. Satre M. and
    7. Garin J.
    (1995). Identification of major proteins associated with Dictyostelium discoideum endocytic vesicles. J. Cell Sci 108, 3331–3337
    OpenUrlAbstract/FREE Full Text
    1. Aizawa H.,
    2. Katadae M.,
    3. Maruya M.,
    4. Sameshima M.,
    5. Murakami-Mirofushi K. and
    6. Yahara I.
    (1998). Contraction of actin bundles inducedin Dictyostelium by overexpression of cofilin in response to hyperosmotic stress. Mol. Biol. Cell 9, 17–.
    OpenUrl
    1. Bartles J. R.,
    2. Zheng L. L.,
    3. Li A. L.,
    4. Wierda A. and
    5. Chen B.
    (1998). Small espin: a third actin-bundling protein and potential forked protein ortholog in brush border microvilli. J. Cell Biol 143, 107–119
    OpenUrlAbstract/FREE Full Text
    1. Bennett H. and
    2. Condeelis J.
    (1988). Isolation of an immunoreactive analogue of brain fodrin that is associated with the cell cortex of Dictyostelium amoebae. Cell Motil. Cytoskel 11, 303–317
    OpenUrlCrossRefPubMedWeb of Science
    1. Berthold J.,
    2. Stadler J.,
    3. Bozzaro S.,
    4. Fichtner B. and
    5. Gerisch G.
    (1985). Carbohydrate and other epitopes of the contact site A glycoprotein of Dictyostelium discoideum as characterized by monoclonal antibodies. Cell Differ 16, 187–202
    OpenUrlPubMedWeb of Science
    1. Beug H. and
    2. Gerisch G.
    (1972). A micromethod for routine measurement of cell agglutination and dissociation. J. Immunol. Meth 2, 49–57
    OpenUrlCrossRefPubMed
    1. Bonner J. T.
    (1947). Evidence for the formation of cell aggregates by chemotaxis in the development of the slime mold Dictyostelium discoideum. J. Exp. Zool 106, 1–26
    OpenUrlCrossRefPubMedWeb of Science
    1. Brier J.,
    2. Fechheimer M.,
    3. Swanson J. and
    4. Taylor D. L.
    (1983). Abundance, relative gelation activity, and distribution of the 95,000 dalton actin-binding protein from Dictyostelium discoideum. J. Cell Biol 97, 178–185
    OpenUrlAbstract/FREE Full Text
    1. Brink M.,
    2. Gerisch G.,
    3. Isenberg G.,
    4. Noegel A. A.,
    5. Segall J. E.,
    6. Wallraff E. and
    7. Schleicher M.
    (1990). A Dictyostelium mutant lacking an F-actin cross-linking protein, the 120 kD gelation factor. J. Cell Biol 111, 1477–1489
    OpenUrlAbstract/FREE Full Text
    1. Brookfield J. F. Y.
    (1997). Genetic redundancy. Advan. Genet 36, 137–155
    OpenUrlPubMedWeb of Science
    1. Caterina M. J.,
    2. Milne J. L. S. and
    3. Devreotes P. N.
    (1994). Mutation of the third intracellular loop of the cAMP receptor, cAR1, of Dictyostelium yields mutants impaired in multiple signaling pathways. J. Biol. Chem 269, 1523–1532
    OpenUrlAbstract/FREE Full Text
    1. Chen T.-L. L.,
    2. Kowalczyk P. A.,
    3. Ho G. and
    4. Chisholm R. L.
    (1995). Targeted disruption of the Dictyostelium myosin essential light chain gene produces cells defective in cytokinesis and morphogenesis. J. Cell Sci 108, 3207–3218
    OpenUrlAbstract/FREE Full Text
    1. Choi A. H. C. and
    2. Siu C. H.
    (1987). Filopodia are enriched in a cell cohesion molecule of Mr80,000 and participate in cell-cell contact formation in Dictyostelium discoideum. J. Cell Biol 104, 1375–1387
    OpenUrlAbstract/FREE Full Text
    1. Claviez M.,
    2. Pagh K.,
    3. Maruta H.,
    4. Baltes W.,
    5. Fisher P. and
    6. Gerisch G.
    (1982). Electron microscopic mapping of monoclonal antibodies on the tail region of Dictyostelium myosin. EMBO J 1, 1017–1022
    OpenUrlPubMedWeb of Science
    1. Condeelis J.,
    2. Salisbury J. and
    3. Fujiwara K.
    (1981). A new protein that gels F-actin in the cell cortex of Dictyostelium discoideum. Nature 292, 161–163
    OpenUrl
    1. Condeelis J. S. and
    2. Vahey M.
    (1982). A calcium and pH-regulated protein from Dictyostelium discoideum that cross-links filaments. J. Cell Biol 94, 466–471
    OpenUrlAbstract/FREE Full Text
    1. Cox D.,
    2. Condeelis J.,
    3. Wessels D.,
    4. Soll D.,
    5. Kern H. and
    6. Knecht D.
    (1992). Targeted disruption of the ABP-120 gene leads to cells with altered motility. J. Cell Biol 116, 943–955
    OpenUrlAbstract/FREE Full Text
    1. Cox D.,
    2. Wessels D.,
    3. Soll D.,
    4. Hartwig J. and
    5. Condeelis J.
    (1996). Re-expression of ABP-120 rescues cytoskeletal, motility, and phagocytosis defects of ABP-120- Dictyostelium mutants. Mol. Biol. Cell 7, 803–823
    OpenUrlAbstract/FREE Full Text
    1. Cubitt A. B.,
    2. Firtel R. A.,
    3. Fisher G.,
    4. Jaffe L. F. and
    5. Miller A.-L.
    (1995). Patterns of free calcium in multicellular stages of Dictyostelium expressing jellyfish apoaequorin. Development 121, 2291–2301
    OpenUrlAbstract
    1. de Hostos E. L.,
    2. Bradtke B.,
    3. Lottspeich F.,
    4. Guggenheim R. and
    5. Gerisch G.
    (1991). Coronin, an actin-binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G proteinsubunits. EMBO J 10, 4097–4104
    OpenUrlPubMedWeb of Science
    1. Doberstein S. K.,
    2. Baines I. C.,
    3. Wiegand G.,
    4. Korn E. D. and
    5. Pollard T. D.
    (1993). Inhibition of contractile vacuole function in vivo by antibodies against myosin I. Nature 365, 841–843
    OpenUrlCrossRefPubMedWeb of Science
    1. Early A. E.,
    2. Williams J. G.,
    3. Meyer H. E.,
    4. Por S. B.,
    5. Smith E.,
    6. Williams K. L. and
    7. Gooley A. A.
    (1988). Structural characterization of Dictyostelium discoideum prespore-specific gene D19 and of its product, cell surface glycoprotein PsA. Mol. Cell. Biol 8, 3458–3466
    OpenUrlAbstract/FREE Full Text
    1. Eichinger L.,
    2. Köppel B.,
    3. Noegel A. A.,
    4. Schleicher M.,
    5. Schliwa M.,
    6. Weijer C. J.,
    7. Witke W. and
    8. Janmey P. A.
    (1996). Mechanical perturbation elicits a phenotypic difference between Dictyostelium wild-type cells and cytoskeletal mutants. Biophys. J 70, 1054–1060
    OpenUrlPubMedWeb of Science
    1. Faix J.,
    2. Steinmetz M.,
    3. Boves H.,
    4. Kammerer R. A.,
    5. Lottspeich F.,
    6. Mintert U.,
    7. Murphy J.,
    8. Stock A.,
    9. Aebi U. and
    10. Gerisch G.
    (1996). Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail. Cell 86, 631–642
    OpenUrlCrossRefPubMedWeb of Science
    1. Fechheimer M. and
    2. Taylor D. L.
    (1984). Isolation and characterization of a 30,000-dalton calcium-sensitive actin cross-linking protein from Dictyostelium discoideum. J. Biol. Chem 259, 4514–4520
    OpenUrlAbstract/FREE Full Text
    1. Fechheimer M.
    (1987). The Dictyostelium discoideum 30,000 Dalton calcium-sensitive actin-bundling protein is selectively present in filopodia. J. Cell Biol 104, 1539–1551
    OpenUrlAbstract/FREE Full Text
    1. Fechheimer M.,
    2. Murdock D.,
    3. Carney M. and
    4. Glover C. V. C.
    (1991). Isolation and sequencing of cDNA clones encoding the Dictyostelium discoideum 30,000 dalton actin bundling protein. J. Biol. Chem 266, 2883–2889
    OpenUrlAbstract/FREE Full Text
    1. Fechheimer M.,
    2. Ingalls H. M.,
    3. Furukawa R. and
    4. Luna E. J.
    (1994). Association of the Dictyostelium 30,000 Mr actin bundling protein with contact regions. J. Cell Sci 107, 2393–2401
    OpenUrlAbstract/FREE Full Text
    1. Fisher P. R.,
    2. Merkl R. and
    3. Gerisch G.
    (1989). Quantitative analysis of cell motility and chemotaxis in Dictyostelium discoideum by using an image processing system and a novel chemotaxis chamber providing stationary chemical gradients. J. Cell Biol 108, 973–984
    OpenUrlAbstract/FREE Full Text
    1. Fisher P. R.,
    2. Noegel A. A.,
    3. Fechheimer M.,
    4. Rivero F.,
    5. Prassler J. and
    6. Gerisch G.
    (1997). Photosensory and thermosensory responses in Dictyostelium slugs are specifically impaired by absence of the F-actin cross-linking gelation factor (ABP-120). Curr. Biol 7, 889–892
    OpenUrlCrossRefPubMed
    1. Fucini P.,
    2. Renner C.,
    3. Herberhold C.,
    4. Noegel A. A. and
    5. Holak T.
    (1997). The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold. Nature Struct. Biol 4, 223–230
    OpenUrlCrossRefPubMedWeb of Science
    1. Fukui Y.
    (1993). Toward a new concept of cell motility: Cytoskeletal dynamics in amoeboid movement and cell division. Int. Rev. Cytol 144, 85–127
    OpenUrlPubMedWeb of Science
    1. Furukawa R.,
    2. Butz S.,
    3. Fleischmann E. and
    4. Fechheimer M.
    (1992). The Dictyostelium discoideum 30,000 dalton protein contributes to phagocytosis. Protoplasma 169, 18–27
    OpenUrlCrossRef
    1. Furukawa R. and
    2. Fechheimer M.
    (1997). The structure, function, and assembly of actin filament bundles. Int. Rev. Cytol 175, 29–90
    OpenUrlCrossRefPubMedWeb of Science
    1. Gao E. N.,
    2. Shier P. and
    3. Siu C. H.
    (1992). Purification and partial characterization of a cell adhesion molecule (GP 150) involved in postaggregation stage cell-cell binding in Dictyostelium discoideum. J. Biol. Chem 267, 9409–9415
    OpenUrlAbstract/FREE Full Text
    1. Gottlieb T. A.,
    2. Ivanov I. E.,
    3. Adesnik M. and
    4. Sabatini D. D.
    (1993). Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J. Cell Biol 120, 695–710
    OpenUrlAbstract/FREE Full Text
    1. Guarente L.
    (1993). Synthetic enhancement in gene interaction: a genetic tool come of age. Trends Genet 9, 362–366
    OpenUrlCrossRefPubMedWeb of Science
    1. Hacker U.,
    2. Albrecht R. and
    3. Maniak M.
    (1997). Fluid-phase uptake by macropinocytosis in Dictyostelium. J. Cell Sci 110, 105–112
    OpenUrlAbstract/FREE Full Text
    1. Haugwitz M.,
    2. Noegel A. A.,
    3. Karakesisoglou J. and
    4. Schleicher M.
    (1994). Dictyostelium amebas that lack G-actin sequestering profilins show defects in F-actin content, cytokinesis, and development. Cell 79, 303–314
    OpenUrlCrossRefPubMedWeb of Science
    1. Hellewell S. B. and
    2. Taylor D. L.
    (1979). The contractile basis of amoeboid movement. VI. The solation contraction coupling hypothesis. J. Cell Biol 83, 633–648
    OpenUrlAbstract/FREE Full Text
    1. Jung G.,
    2. Wu X. and
    3. Hammer J. A. III.
    (1996). Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions. J. Cell Biol 133, 305–323
    OpenUrlAbstract/FREE Full Text
    1. Knecht D. A. and
    2. Loomis W. F.
    (1987). Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium discoideum. Science 236, 1081–1086
    OpenUrlAbstract/FREE Full Text
    1. Knecht D. A. and
    2. Shelden E.
    (1995). 3-dimensional localization of wild-type and myosin II mutant cells during morphogenesis of Dictyostelium. Dev. Biol 170, 434–444
    OpenUrlCrossRefPubMed
    1. Kuwayama H.,
    2. Ecke M.,
    3. Gerisch G. and
    4. Van Haastert P. J. M.
    (1996). Protection against osmotic-stress by cGMP mediated phosphorylation. Science 271, 207–209
    OpenUrlAbstract
    1. Kubler G. and
    2. Riezman H.
    (1993). Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J 12, 2855–2862
    OpenUrlPubMedWeb of Science
    1. Laemmli U. K.
    (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680–685
    OpenUrlCrossRefPubMedWeb of Science
    1. Lichtscheidl I. K. and
    2. Foissner I.
    (1996). Video microscopy of dynamic plant cell organelles- principles of the technique and practical application. J. Microsc 181, 117–128
    OpenUrlCrossRefWeb of Science
    1. Luna E. J.,
    2. Wuestehube L. J.,
    3. Ingalls H. M. and
    4. Chia C. P.
    (1990). The Dictyostelium discoideum plasma membrane: a model system for the study of actin-membrane interactions. Advan. Cell Biol 3, 1–34
    OpenUrl
    1. Matsudaira P.
    (1991). Modular organization of actin crosslinking proteins. Trends Biochem. Sci 16, 87–92
    OpenUrlCrossRefPubMedWeb of Science
    1. Mulholland J.,
    2. Wesp A.,
    3. Riezman H. and
    4. Botstein D.
    (1997). Yeast actin cytoskeleton mutants accumulate a new class of Golgi-derived secretory vesicle. Mol. Biol. Cell 8, 1481–1499
    OpenUrlAbstract/FREE Full Text
    1. Muller K. and
    2. Gerisch G.
    (1978). A specific glycoprotein as the target site of adhesion blocking Fab in aggregating Dictyostelium cells. Nature 274, 445–449
    OpenUrlCrossRefPubMedWeb of Science
    1. Newell P. C.,
    2. Telser A. and
    3. Sussmann M.
    (1969). Alternative developmental pathways determined by environmental conditions in the cellular slime mold Dictyostelium discoideum. J. Bacteriol 100, 763–768
    OpenUrlAbstract/FREE Full Text
    1. Niewöhner J.,
    2. Weber I.,
    3. Maniak M.,
    4. Muller-Taubenberger A. and
    5. Gerisch G.
    (1997). Talin-null cells of Dictyostelium are strongly defective in adhesion to particle and substrate surfaces and slightly impaired in cytokinesis. J. Cell Biol 138, 349–361
    OpenUrlAbstract/FREE Full Text
    1. Noegel A. A.,
    2. Metz B. A. and
    3. Williams K. L.
    (1985). Developmentally regulated transcription of Dictyostelium discoideum plasmid Ddp1. EMBO J 4, 3797–3803
    OpenUrlPubMedWeb of Science
    1. Noegel A. A.,
    2. Gerisch G.,
    3. Stadler J. and
    4. Westphal M.
    (1986). Complete sequence and transcript of a cell adhesion protein from aggregating Dictyostelium cells. EMBO J 5, 1473–1476
    OpenUrlPubMedWeb of Science
    1. Noegel A. A.,
    2. Witke W. and
    3. Schleicher M.
    (1987). Calcium-sensitive non-muscle alpha-actinin contains EF-hand structures and highly conserved regions. FEBS Lett 221, 391–396
    OpenUrlCrossRefPubMedWeb of Science
    1. Noegel A. A.,
    2. Rapp S.,
    3. Lottspeich F.,
    4. Schleicher M. and
    5. Stewart M.
    (1989). The Dictyostelium gelation factor shares a putative actin-binding site with alpha-actinin and dystrophin and also has a rod domain containing six 100 residue motifs that appear to have a cross-conformation. J. Cell Biol 108, 607–618
    OpenUrlAbstract/FREE Full Text
    1. Noegel A. A. and
    2. Luna E. J.
    (1995). The Dictyostelium cytoskeleton. Experientia 51, 1135–1143
    OpenUrlCrossRefPubMedWeb of Science
    1. Novak K. D.,
    2. Peterson M. D.,
    3. Reedy M. C. and
    4. Titus M. A.
    (1995). Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis. J. Cell Biol 131, 1205–1221
    OpenUrlAbstract/FREE Full Text
    1. Novak K. D. and
    2. Titus M. A.
    (1997). Myosin I overexpression impairs cell migration. J. Cell Biol 136, 633–647
    OpenUrlAbstract/FREE Full Text
    1. Nowak M. A.,
    2. Boerlizst M. C.,
    3. Cooke J. and
    4. Smith J. M.
    (1997). Evolution of genetic redundancy. Nature 388, 167–171
    OpenUrlCrossRefPubMedWeb of Science
    1. Oliver S. G.,
    2. van der Aart Q. J.,
    3. Agostoni-Carbone M. L.,
    4. Aigle M.,
    5. Alberghina L.,
    6. Alexandraki D.,
    7. Antoine G.,
    8. Anwar R.,
    9. Ballesta J. P.,
    10. Benit P. and
    11. et al.
    (1992). The complete DNA sequence of yeast chromosome III. Nature 357, 38–46
    OpenUrlCrossRefPubMed
    1. Otto J. J.
    (1994). Actin-bundling proteins. Curr. Opin. Cell Biol 6, 105–109
    OpenUrlCrossRefPubMedWeb of Science
    1. Pinson K. I.,
    2. Dunbar L.,
    3. Samuelson L. and
    4. Gumucio D. L.
    (1998). Targeted disruption of the mouse villin gene does not impair the morphogenesis of microvilli. Dev. Dynam 211, 109–121
    OpenUrlCrossRefPubMedWeb of Science
    1. Prassler J.,
    2. Stocker S.,
    3. Marriott G.,
    4. Heidecker M.,
    5. Kellermann J. and
    6. Gerisch G.
    (1997). Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes. Mol. Biol. Cell 8, 83–95
    OpenUrlAbstract/FREE Full Text
    1. Rivero F.,
    2. Furukawa R.,
    3. Noegel A. A. and
    4. Fechheimer M.
    (1996). Dictyostelium discoideum cells lacking the 34,000 dalton actin binding protein can grow, locomote, and develop, but exhibit defects in regulation of cell structure and movement: a case of partial redundancy. J. Cell Biol 135, 965–980
    OpenUrlAbstract/FREE Full Text
    1. Rivero F.,
    2. Köppel B.,
    3. Peracino B.,
    4. Bozzaro S.,
    5. Siegert F.,
    6. Weijer C. J.,
    7. Schleicher M.,
    8. Albrecht R. and
    9. Noegel A. A.
    (1996). The role of the cortical cytoskeleton: F-actin cross-linking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J. Cell Sci 109, 2679–2691
    OpenUrlAbstract/FREE Full Text
    1. Schleicher M.,
    2. Noegel A. A.,
    3. Schwarz T.,
    4. Wallraff E.,
    5. Brink M.,
    6. Faix J.,
    7. Gerisch G. and
    8. Isenberg G.
    (1988). A Dictyostelium mutant with severe defects in alpha-actinin: its characterization using cDNA probes and monoclonal antibodies. J. Cell Sci 90, 59–71
    OpenUrlAbstract/FREE Full Text
    1. Schleicher M.,
    2. Andre B.,
    3. Andreoli C.,
    4. Eichinger L.,
    5. Haugwitz M.,
    6. Hofmann A.,
    7. Karakesisoglu J.,
    8. Stöckelhuber M. and
    9. Noegel A. A.
    (1995). Structure/function studies on cytoskeletal proteins in Dictyostelium amoebae as a paradigm. FEBS Lett 369, 38–42
    OpenUrlCrossRefPubMedWeb of Science
    1. Shelden E. and
    2. Knecht D. A.
    (1995). Mutants lacking myosin II cannot resist forces generated during multicellular morphogenesis. J. Cell Sci 108, 1105–1115
    OpenUrlAbstract/FREE Full Text
    1. Steck T. L.,
    2. Chiaraviglio L. and
    3. Meredith S.
    (1997). Osmotic homeostasis in Dictyosteliumdiscoideum: Excretion of amino acids and ingested solutes. J. Euk. Microbiol 44, 503–510
    OpenUrlPubMed
    1. Swanson J. A.,
    2. Yirinec B. D. and
    3. Silverstein S. C.
    (1985). Phorbol esters and horse radish peroxidase stimulate pinocytosis and redirect the flow of pinocytosed fluid in macrophages. J. Cell Biol 100, 851–859
    OpenUrlAbstract/FREE Full Text
    1. Tautz D.
    (1992). Redundancies, development, and the flow of information. BioEssays 14, 263–266
    OpenUrlCrossRefPubMedWeb of Science
    1. Temesvari L. A.,
    2. Bush J. M.,
    3. Peterson M. D.,
    4. Novak K. D.,
    5. Titus M. A. and
    6. Cardelli J. A.
    (1996). Examination of the endosomal and lysosomal pathways in Dictyostelium discoideum myosin I mutants. J. Cell Sci 109, 663–673
    OpenUrlAbstract/FREE Full Text
    1. Thomas J. H.
    (1993). Thinking about genetic redundancy. Trends Genet 9, 395–399
    OpenUrlCrossRefPubMedWeb of Science
    1. Tilney L. G.,
    2. Tilney M. S. and
    3. Guild G. M.
    (1995). F-Actin bundles in Drosophila bristles I. Two filament cross-links are involved in bundling. J. Cell Biol 130, 629–638
    OpenUrlAbstract/FREE Full Text
    1. Tilney L. G.,
    2. Connelly P. S.,
    3. Vranich K. A.,
    4. Shaw M. K. and
    5. Guild G. M.
    (1998). Why are two different cross-linkers necessary for actin bundle formation in vivo and what does each cross-link contribute. J. Cell Biol 143, 121–133
    OpenUrlAbstract/FREE Full Text
    1. Towbin H.,
    2. Staehelin T. and
    3. Gordon J.
    (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Nat. Acad. Sci. USA 76, 4350–4354
    OpenUrlAbstract/FREE Full Text
    1. Wallraff E.,
    2. Schleicher M.,
    3. Modersitzki M.,
    4. Rieger D.,
    5. Isenberg G. and
    6. Gerisch G.
    (1986). Selection of Dictyostelium mutants defective in cytoskeletal proteins: the use of an antibody that binds to the ends of-actinin rods. EMBO J 5, 61–67
    OpenUrlPubMed
    1. Way M.,
    2. Pope B. and
    3. Weeds A. G.
    (1992). Evidence for functional homology in the F-actin binding domains of gelsolin andactinin: implications for the requirements of severing and capping. J. Cell Biol 119, 835–842
    OpenUrlAbstract/FREE Full Text
    1. Weiner O. H.,
    2. Murphy J.,
    3. Griffiths G.,
    4. Schleicher M. and
    5. Noegel A. A.
    (1993). The actin-binding protein comitin (p24) is a component of the Golgi apparatus. J. Cell Biol 123, 23–34
    OpenUrlAbstract/FREE Full Text
    1. Williams K. L. and
    2. Newell P. C.
    (1976). A genetic study in the cellular slime mold Dictyostelium discoideum using complementation analysis. Genetics 82, 287–307
    OpenUrlAbstract/FREE Full Text
    1. Witke W.,
    2. Schleicher M. and
    3. Noegel A. A.
    (1992). Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell 68, 53–62
    OpenUrlCrossRefPubMedWeb of Science
    1. Witke W.,
    2. Hofmann A.,
    3. K⁁ppel B.,
    4. Schleicher M. and
    5. Noegel A. A.
    (1993). The Ca2+-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis. J. Cell Biol 121, 599–606
    OpenUrlAbstract/FREE Full Text
    1. Wong E. F.,
    2. Brar S. K.,
    3. Sesaki H.,
    4. Yang C. Z. and
    5. Siu C. H.
    (1996). Molecular cloning and characterization of DdCAD-1, a Ca2+-dependent cell-cell adhesion molecule, in Dictyostelium discoideum. J. Biol. Chem 271, 16399–16408
    OpenUrlAbstract/FREE Full Text
    1. Xu X. S.,
    2. Kuspa A.,
    3. Fuller D.,
    4. Loomis W. F. and
    5. Knecht D. A.
    (1996). Cell-cell adhesion prevents mutant cells lacking myosin II from penetrating aggregation streams of Dictyostelium. Dev. Biol 175, 218–226
    OpenUrlCrossRefPubMedWeb of Science
    1. Yumura S.,
    2. Furuya K. and
    3. Takeuchi I.
    (1996). Intracellular free calcium responses during chemotaxis of Dictyostelium cells. J. Cell Sci 109, 2673–2678
    OpenUrlAbstract/FREE Full Text
Previous ArticleNext Article
Back to top
Previous ArticleNext Article

This Issue

 Download PDF

Email

Thank you for your interest in spreading the word on Journal of Cell Science.

NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.

Enter multiple addresses on separate lines or separate them with commas.
Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium
(Your Name) has sent you a message from Journal of Cell Science
(Your Name) thought you would like to see the Journal of Cell Science web site.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Journal Articles
Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium
F. Rivero, R. Furukawa, M. Fechheimer, A.A. Noegel
Journal of Cell Science 1999 112: 2737-2751;
del.icio.us logo Digg logo Reddit logo Twitter logo CiteULike logo Facebook logo Google logo Mendeley logo
Citation Tools
Journal Articles
Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium
F. Rivero, R. Furukawa, M. Fechheimer, A.A. Noegel
Journal of Cell Science 1999 112: 2737-2751;

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
Alerts

Please log in to add an alert for this article.

Sign in to email alerts with your email address

Article navigation

  • Top
  • Article
  • Info & metrics
  • PDF

Related articles

Cited by...

More in this TOC section

  • Involvement of actin filaments and integrins in the binding step in collagen phagocytosis by human fibroblasts
  • University administration
  • Integrin cytoplasmic domain-binding proteins
Show more Journal Articles

Similar articles

Other journals from The Company of Biologists

Development

Journal of Experimental Biology

Disease Models & Mechanisms

Biology Open

Advertisement

Follow us on Instagram

Cell science is bursting with beautiful images and over on Instagram, we’re showing them off! Find both JCS and FocalPlane on Instagram for stories and techniques across cell biology.


An interview with Derek Walsh

Professor Derek Walsh is the guest editor of our new special issue Cell Biology of Host-Pathogen Interactions. In an interview, Derek tells us about his work in the field of DNA viruses, the impact of the pandemic on virology and what his role as Guest Editor taught him.


How to improve your scientific writing

"If you are a scientist and you want to succeed, you must become a writer."

How do scientists become master storytellers? We called on our journal Editors, proofreaders and contributors to our community sites for their advice on how to improve your scientific writing.


Meet the preLighters: Jennifer Ann Black

Following the theme of our latest special issue, postdoc Jennifer Ann Black studies replication stress and genome plasticity in Leishmania in Professor Luiz Tosi’s lab in Sao Paolo. We caught up with Jenn (virtually) to hear about her relocation to Brazil mid-pandemic, her research on parasites and what she enjoys about ‘preLighting’.

In our special issue, Chandrakar et al. and Rosazza et al. present their latest work on Leishmania.


Mole – The Corona Files

“There are millions of people around the world who continue to believe that the Terrible Pandemic is a hoax.”

Mole continues to offer his wise words to researchers on how to manage during the COVID-19 pandemic.


JCS and COVID-19

For more information on measures Journal of Cell Science is taking to support the community during the COVID-19 pandemic, please see here.

If you have any questions or concerns, please do not hestiate to contact the Editorial Office.

Articles

  • Accepted manuscripts
  • Issue in progress
  • Latest complete issue
  • Issue archive
  • Archive by article type
  • Special issues
  • Subject collections
  • Interviews
  • Sign up for alerts

About us

  • About Journal of Cell Science
  • Editors and Board
  • Editor biographies
  • Travelling Fellowships
  • Grants and funding
  • Journal Meetings
  • Workshops
  • The Company of Biologists

For Authors

  • Submit a manuscript
  • Aims and scope
  • Presubmission enquiries
  • Fast-track manuscripts
  • Article types
  • Manuscript preparation
  • Cover suggestions
  • Editorial process
  • Promoting your paper
  • Open Access
  • JCS Prize
  • Manuscript transfer network
  • Biology Open transfer

Journal Info

  • Journal policies
  • Rights and permissions
  • Media policies
  • Reviewer guide
  • Sign up for alerts

Contacts

  • Contact JCS
  • Subscriptions
  • Advertising
  • Feedback

Twitter   YouTube   LinkedIn

© 2021   The Company of Biologists Ltd   Registered Charity 277992