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Localization of the small GTP-binding protein rab1p to early compartments of the secretory pathway
J. Saraste, U. Lahtinen, B. Goud
Journal of Cell Science 1995 108: 1541-1552;

Summary

We have studied the localization of the small GTPase rab1p in different cell types using polyclonal antibodies prepared against the rab1A isoform of the protein. Immunofluorescence microscopy of normal rat kidney (NRK) and mouse myeloma cells showed the association of the protein with the Golgi complex and peripheral sites where it colocalized with p58, a pre- and cis-Golgi marker protein. Rab1p and p58 also had similar distributions in membrane fractions derived from rat pancreas microsomes. Both were concentrated in two intermediate density subfractions between the rough endoplasmic reticulum and trans-Golgi, whereas rab6p, previously localized to middle and trans-Golgi, was enriched in the light density trans-Golgi fraction. Immunoperoxidase electron microscopy of NRK and myeloma cells revealed the association of rab1p with 1–2 cisternae, vacuolar, and tubulovesicular membranes in the cis-Golgi region. The rab1p-specific staining typically covered the entire lateral surface of the cisternae but, in weakly stained cells, local labeling between closely opposed membranes could also be seen. The rab1p-positive pre-Golgi compartment had a predominantly tubulovesicular appearance in NRK cells whereas in myeloma cells it consisted of vacuoles surrounded by rab1p-positive vesicles and tubules of heterogeneous size. In both cell types the rough ER cisternae and the nuclear envelope contained negligible labeling and no continuities between these and the rab1p-positive membranes were observed. In addition, in myeloma cells the smooth ER subcompartment, containing endogenous retrovirus particles, was devoid of rab1p-labeling. These results indicate that the pre-Golgi (intermediate) compartment consists of different membrane domains and its morphology can vary considerably between different cell types. Further, they suggest that the recruitment of rab1p to membranes occurs predominantly in a post-ER location and that the protein functions in targeting/fusion events within the pre- and cis-Golgi membranes.

REFERENCES

    1. Anthony C.,
    2. Cibert C.,
    3. Geraud G.,
    4. Santa Maria A.,
    5. Maro B.,
    6. Mayau V. and
    7. Goud B.
    (1992). The small GTP-binding protein rab6p is distributed from medial Golgi to the trans -Golgi network as determined by a confocal microscopic approach. J. Cell Sci 103, 785–796
    OpenUrlAbstract/FREE Full Text
    1. Bacon R.,
    2. Salminen A.,
    3. Ruohola H.,
    4. Novick P. and
    5. Ferro-Novick S.
    (1989). The GTP-binding protein YPT1 is required for transport in vitro: the Golgi apparatus is defective in YPT1 mutants. J. Cell Biol 109, 1015–1022
    OpenUrlAbstract/FREE Full Text
    1. Bailly E.,
    2. McCaffrey M.,
    3. Touchot N.,
    4. Zahraoui A.,
    5. Goud B. and
    6. Bornens M.
    (1991). Phosphorylation of two small GTP-binding proteins of the rab family by p34cdc2. Nature 350, 715–718
    OpenUrlCrossRefPubMed
    1. Baker D.,
    2. Wuestehube L.,
    3. Schekman R.,
    4. Botstein D. and
    5. Segev N.
    (1990). GTP-binding Ypt1 protein and Ca2+ function independently in a cell-free protein transport reaction. Proc. Nat. Acad. Sci. USA 87, 355–359
    OpenUrlAbstract/FREE Full Text
    1. Balch W. E.,
    2. McCaffery J. M.,
    3. Plutner H. and
    4. Farquhar M. G.
    (1994). Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell 76, 841–852
    OpenUrlCrossRefPubMedWeb of Science
    1. Barlowe C.,
    2. Orci L.,
    3. Yeung T.,
    4. Hosobuchi M.,
    5. Hamamoto S.,
    6. Salama N.,
    7. Rexach M.,
    8. Ravazzola M.,
    9. Amherdt M. and
    10. Schekman R.
    (1994). COPII: a membrane coat formed by sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895–907
    OpenUrlCrossRefPubMedWeb of Science
    1. Bennett M. K. and
    2. Scheller R. H.
    (1993). The molecular machinery for secretion is conserved from yeast to neurons. Proc. Nat. Acad. Sci. USA 90, 2559–2563
    OpenUrlAbstract/FREE Full Text
    1. Bonatti S. and
    2. Torrisi M.-R.
    (1993). The intermediate compartment betweenendoplasmic reticulum and Golgi complex in mammalian cells. Subcell. Biochem 21, 121–142
    OpenUrlPubMed
    1. Bourne H. R.
    (1988). Do GTPases direct membrane traffic in secretion?. Cell 53, 669–671
    OpenUrlCrossRefPubMedWeb of Science
    1. Brennwald P. and
    2. Novick P.
    (1993). Interactions of three domains distinquishing the ras-related GTP-binding proteins ypt1 and sec4. Nature 362, 560–563
    OpenUrlCrossRefPubMedWeb of Science
    1. Bucci C.,
    2. Parton. R. G.,
    3. Mather I. M.,
    4. Stunnenberg H.,
    5. Simons K.,
    6. Hoflack B. and
    7. Zerial M.
    (1992). The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70, 715–728
    OpenUrlCrossRefPubMedWeb of Science
    1. Chavrier P.,
    2. Parton R. G.,
    3. Hauri H.-P.,
    4. Simons K. and
    5. Zerial M.
    (1990). Localization of low molecular weight GTP-binding proteins to exotic and endocytic compartments. Cell 62, 317–329
    OpenUrlCrossRefPubMedWeb of Science
    1. Chavrier P.,
    2. Vingron M.,
    3. Sander C.,
    4. Simons K. and
    5. Zerial M.
    (1990). Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line. Mol. Cell. Biol 10, 6578–6585
    OpenUrlAbstract/FREE Full Text
    1. Cooper M. S.,
    2. Cornell-Bell A. H.,
    3. Chernjavsky A.,
    4. Dani J. W. and
    5. Smith S. J.
    (1990). Tubulovesicular processes emerge from trans-Golgi cisternae, extend along microtubules, and interlink adjacent trans-Golgi elements into a reticulum. Cell 61, 135–145
    OpenUrlCrossRefPubMedWeb of Science
    1. Cosson P. and
    2. Letourneur F.
    (1994). Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629–1631
    OpenUrlAbstract/FREE Full Text
    1. Davidson H. W. and
    2. Balch W. E.
    (1993). Differential inhibition of multiple vesicular transport steps between the endoplasmic reticulum and the trans-Golgi network. J. Biol. Chem 268, 4216–4226
    OpenUrlAbstract/FREE Full Text
    1. Deretic D. and
    2. Papermaster D. S.
    (1993). Rab6 is associated with a compartment that transports rhodopsin from the trans-Golgi to the site of rod outer disk formation in frog retinal photoreceptors. J. Cell Sci 106, 803–813
    OpenUrlAbstract/FREE Full Text
    1. Donaldson J. G.,
    2. Lippincott-Schwarz J.,
    3. Bloom G. S.,
    4. Kreis T. E. and
    5. Klausner R. D.
    (1990). Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J. Cell Biol 111, 2295–2306
    OpenUrlAbstract/FREE Full Text
    1. Duden R.,
    2. Griffiths G.,
    3. Frank R.,
    4. Argos P. and
    5. Kreis T. E.
    (1991). -COP, a 110 kd protein associated with non-clathrin coated vesicles and the Golgi complex, shows homology to -adaptin. Cell 64, 649–665
    OpenUrlCrossRefPubMedWeb of Science
    1. Dunn B.,
    2. Stearns T. and
    3. Botstein D.
    (1993). Specificity domains distinquish the ras-related GTPases ypt1 and sec4. Nature 362, 563–565
    OpenUrlCrossRefPubMedWeb of Science
    1. Ferro-Novick S. and
    2. Novick P.
    (1993). The role of GTP-binding proteins in transport along the exocytic pathway. Annu. Rev. Cell Biol 9, 575–599
    OpenUrlCrossRefWeb of Science
    1. Goud B.,
    2. Zahraoui A.,
    3. Tavitian A. and
    4. Saraste J.
    (1990). Small GTP-binding protein associated with Golgi cisternae. Nature 345, 553–556
    OpenUrlCrossRefPubMed
    1. Goud B. and
    2. McGaffrey M.
    (1991). Small GTP-binding proteins and their role in transport. Curr. Opin. Cell Biol 3, 626–633
    OpenUrlCrossRefPubMed
    1. Haubruck H.,
    2. Prange R.,
    3. Vorgias C. and
    4. Gallwitz D.
    (1989). The ras-related mouse ypt1 protein can functionally replace the YPT1 gene product in yeast. EMBO J 8, 1427–1432
    OpenUrlPubMedWeb of Science
    1. Hauri H.-P. and
    2. Schweizer A.
    (1992). The endoplasmic reticulum-Golgi intermediate compartment. Curr. Opin. Cell Biol 4, 600–608
    OpenUrlCrossRefPubMed
    1. Hendricks L. C.,
    2. McCaffery M.,
    3. Palade G. E. and
    4. Farquhar M. G.
    (1993). Disruption of endoplasmic reticulum to Golgi transport leads to the accumulation of large aggregates containing-COP in pancreatic acinar cells. Mol. Biol. Cell 4, 413–424
    OpenUrlAbstract/FREE Full Text
    1. Hendriks R. J. M. and
    2. Fuller S. D.
    (1994). Compartments of the early secretory pathway. Subcell. Biochem 22, 101–149
    OpenUrlCrossRefPubMed
    1. Hobman T. C.,
    2. Woodward L. and
    3. Farquhar M. G.
    (1992). The rubella virus E1 glyco-protein is arrested in a novel post-ER, pre-Golgi compartment. J. Cell Biol 118, 795–811
    OpenUrlAbstract/FREE Full Text
    1. Huber L. A.,
    2. Pimplikar S.,
    3. Parton R.,
    4. Virta H.,
    5. Zerial M. and
    6. Simons K.
    (1993). Rab8, a small GTPase involved in vesicular traffic between the TGN and the baso-lateral plasma membrane. J. Cell Biol 123, 34–45
    OpenUrl
    1. Huber L. A.,
    2. Ullrich O.,
    3. Takai Y.,
    4. Lutcke A.,
    5. Dupree P.,
    6. Olkkonen V.,
    7. Virta H.,
    8. de Hoop M. J.,
    9. Alexandrov K.,
    10. Peter M.,
    11. Zerial M. and
    12. Simons K.
    (1994). Mapping of ras-related GTP-binding proteins by GTP-overlay and 2D-gel analysis. Proc. Nat. Acad. Sci. USA 91, 7874–7878
    OpenUrlAbstract/FREE Full Text
    1. Krijnse-Locker J.,
    2. Ericsson M.,
    3. Rottier P. and
    4. Griffiths G.
    (1994). Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. J. Cell Biol 124, 55–70
    OpenUrlAbstract/FREE Full Text
    1. Kuismanen E. and
    2. Saraste J.
    (1989). Low temperature-induced transport blocks as tools to manipulate membrane traffic. Meth. Cell Biol 32, 257–274
    OpenUrlPubMedWeb of Science
    1. Lahtinen U.,
    2. Dahllof B. and
    3. Saraste J.
    (1992). Characterization of a 58 kDa cis-Golgi protein in pancreatic exocrine cells. J. Cell Sci 103, 321–333
    OpenUrlAbstract/FREE Full Text
    1. Lledo P.-M.,
    2. Vernier P.,
    3. Vincent J.-D.,
    4. Mason W.T. and
    5. Zorec R.
    (1993). Inhibition of rab3B expression attenuates Ca2+ -dependent exocytosis in rat anterior pituitary cells. Nature 364, 540–544
    OpenUrlCrossRefPubMedWeb of Science
    1. Lombardi D.,
    2. Soldati T.,
    3. Riederer M. A.,
    4. Goda Y.,
    5. Zerial M. and
    6. Pfeffer S. R.
    (1993). Rab9 functions in transport between late endosomes and the trans-Golgi network. EMBO J 12, 677–682
    OpenUrlPubMedWeb of Science
    1. Maridonneau-Parini I.,
    2. Yang C.,
    3. Bornens M. and
    4. Goud B.
    (1991). Increase in the expression of a family of small guanosine triphosphate-binding proteins, rab proteins, during induced phagocyte differentiation. J. Clin. Invest 87, 901–907
    OpenUrlCrossRefPubMedWeb of Science
    1. Martinez O.,
    2. Schmidt A.,
    3. Salamero J.,
    4. Hoflack B.,
    5. Roa M. and
    6. Goud B.
    (1994). The small GTP-binding protein rab6p functions in intra-Golgi transport. J. Cell Biol 127, 1575–1588
    OpenUrlAbstract/FREE Full Text
    1. Nuoffer C.,
    2. Davidson H. W.,
    3. Matteson J.,
    4. Meinkoth J. and
    5. Balch W. E.
    (1994). A GDP-bound form of rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments. J. Cell Biol 125, 225–237
    OpenUrlAbstract/FREE Full Text
    1. Oprins A.,
    2. Duden R.,
    3. Kreis T. E.,
    4. Geuze H. and
    5. Slot J. W.
    (1993). -COP localizes mainly to the cis-Golgi side in exocrine pancreas. J. Cell Biol 121, 49–59
    OpenUrlAbstract/FREE Full Text
    1. Ottosen P. D.,
    2. Courtoy P. J. and
    3. Farquhar M. G.
    (1980). Pathways followed by membrane recovered from the surface of plasma cells and myeloma cells. J. Exp. Med 152, 1–19
    OpenUrlAbstract/FREE Full Text
    1. Pelham H. R. B.
    (1989). Control of protein exit from the endoplasmic reticulum. Annu. Rev. Cell Biol 5, 1–23
    OpenUrlCrossRefWeb of Science
    1. Pepperkok R.,
    2. Scheel J.,
    3. Horstmann H.,
    4. Hauri H.-P.,
    5. Griffiths G. and
    6. Kreis T. E.
    (1993). -COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74, 71–82
    OpenUrlCrossRefPubMedWeb of Science
    1. Peränen J.
    (1992). Rapid affinity-purification and biotinylation of antibodies. Biotechniques 13, 546–.
    OpenUrlPubMedWeb of Science
    1. Peter F.,
    2. Plutner H.,
    3. Zhu H.,
    4. Kreis T. E. and
    5. Balch W. E.
    (1993). -COP is essential for transport of protein from the endoplasmic reticulum to the Golgi in vitro. J. Cell Biol 122, 1155–1167
    OpenUrlAbstract/FREE Full Text
    1. Pfeffer S.
    (1994). Rab GTPases: master regulators of membrane trafficking. Curr. Opin. Cell Biol 6, 522–526
    OpenUrlCrossRefPubMedWeb of Science
    1. Pind S. N.,
    2. Nuoffer C.,
    3. McCaffery M. J.,
    4. Plutner H.,
    5. Davidson H. W.,
    6. Farquhar M. G. and
    7. Balch W. E.
    (1994). Rab1 and Ca2+ are required for the fusion of carrier vesicles mediating endoplasmic reticulum to Golgi transport. J. Cell Biol 125, 239–252
    OpenUrlAbstract/FREE Full Text
    1. Plutner H.,
    2. Cox A. D.,
    3. Pind S.,
    4. Khosravi-Far R.,
    5. Bourne J. R.,
    6. Schwaninger R.,
    7. Der C. J. and
    8. Balch W. E.
    (1991). Rab1B regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. J. Cell Biol 115, 31–43
    OpenUrlAbstract/FREE Full Text
    1. Plutner H.,
    2. Davidson H. W.,
    3. Saraste J. and
    4. Balch W. E.
    (1992). Morphological analysis of protein transport from the ER to Golgi membranes in digitonin-permeabilized cells: role of the p58-containing compartment. J. Cell Biol 119, 1097–1116
    OpenUrlAbstract/FREE Full Text
    1. Pryer N. K.,
    2. Wuestehube L. J. and
    3. Schekman R.
    (1992). Vesicle-mediated protein sorting. Annu. Rev. Biochem 61, 471–516
    OpenUrlCrossRefPubMedWeb of Science
    1. Rexach M. F. and
    2. Schekman R.
    (1991). Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles. J. Cell Biol 114, 219–229
    OpenUrlAbstract/FREE Full Text
    1. Roth J.,
    2. Taatjes D. J.,
    3. Lucocq J. M.,
    4. Weinstein J. and
    5. Paulson J. C.
    (1985). Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell 43, 287–295
    OpenUrlCrossRefPubMedWeb of Science
    1. Rothman J. E. and
    2. Orci L.
    (1992). Molecular dissection of the secretory pathway. Nature 355, 409–415
    OpenUrlCrossRefPubMed
    1. Salama N.,
    2. Yeung T. and
    3. Schekman R. W.
    (1993). The sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. EMBO J 12, 4073–4082
    OpenUrlPubMedWeb of Science
    1. Salminen A. and
    2. Novick P.
    (1987). A ras-like protein is required for a post-Golgi event in yeast secretion. Cell 49, 527–538
    OpenUrlCrossRefPubMedWeb of Science
    1. Saraste J. and
    2. Kuismanen E.
    (1984). Pre-and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38, 535–549
    OpenUrlCrossRefPubMedWeb of Science
    1. Saraste J.,
    2. Palade G. E. and
    3. Farquhar M. G.
    (1986). Temperature-sensitive steps in the transport of secretory proteins through the Golgi complex in pancreatic exocrine cells. Proc. Nat. Acad. Sci. USA 83, 6425–6429
    OpenUrlAbstract/FREE Full Text
    1. Saraste J.,
    2. Palade G. E. and
    3. Farquhar M. G.
    (1987). Antibodies to rat pancreas Golgi subfractions: Identification of a 58-kD cis-Golgi protein. J. Cell Biol 105, 2021–2030
    OpenUrlAbstract/FREE Full Text
    1. Saraste J. and
    2. Svensson K.
    (1991). Distribution of the intermediate elements operating in ER to Golgi transport. J. Cell Sci 100, 415–430
    OpenUrlAbstract/FREE Full Text
    1. Saraste J. and
    2. Kuismanen E.
    (1992). Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex. Semin. Cell Biol 3, 343–355
    OpenUrlCrossRefPubMed
    1. Schwaninger R.,
    2. Plutner H.,
    3. Bokoch G. M. and
    4. Balch W. E.
    (1992). Multiple GTP-binding proteins regulate vesicular transport from the ER to Golgi membranes. J. Cell Biol 119, 1077–1096
    OpenUrlAbstract/FREE Full Text
    1. Segev N.,
    2. Mulholland J. and
    3. Botstein D.
    (1988). The yeast GTP-binding YPT1 protein and a mammalian counterpart are associated with the secretion machinery. Cell 52, 915–924
    OpenUrlCrossRefPubMedWeb of Science
    1. Segev N.
    (1991). Mediation of the attachment or fusion step in vesicular transport by the GTP-binding ypt1 protein. Science 252, 1553–1556
    OpenUrlAbstract/FREE Full Text
    1. Söllner T. and
    2. Rothman J. E.
    (1994). Neurotransmission: harnessing fusion machinery at the synapse. Trends Neurosci 17, 344–348
    OpenUrlCrossRefPubMedWeb of Science
    1. Søgaard M.,
    2. Tani K.,
    3. Ye R. R.,
    4. Geromanos S.,
    5. Tempst P.,
    6. Kirchhausen T.,
    7. Rothman J. E. and
    8. Söllner T.
    (1994). A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell 78, 937–948
    OpenUrlCrossRefPubMedWeb of Science
    1. Takatsuki A. and
    2. Tamura G.
    (1985). Brefeldin A, a specific inhibitor of intracellular translocation of vesicular stomatitis virus G-protein: Intracellular accumulation of high-mannose type G-protein and inhibition of its surface expression. Agric. Biol. Chem 49, 899–902
    OpenUrlCrossRefWeb of Science
    1. Tisdale E. J.,
    2. Bourne J. R.,
    3. Khosravi-Far R.,
    4. Der C. J. and
    5. Balch W. E.
    (1992). GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J. Cell Biol 119, 749–761
    OpenUrlAbstract/FREE Full Text
    1. Tixier-Vidal A.,
    2. Barret A.,
    3. Picart R.,
    4. Mayau V.,
    5. Vogt D.,
    6. Wiedenmann B. and
    7. Goud B.
    (1993). The small GTP-binding protein, Rab6p, is associated with both Golgi and post-Golgi synaptophysin-containing membranes during synaptogenesis of hypothalamic neurons in culture. J. Cell Sci 105, 935–947
    OpenUrlAbstract/FREE Full Text
    1. Touchot N.,
    2. Chardin P. and
    3. Tavitian A.
    (1987). Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat brain library. Proc. Nat. Acad. Sci. USA 84, 8210–8214
    OpenUrlAbstract/FREE Full Text
    1. van der Sluijs P.,
    2. Hull M.,
    3. Webster P.,
    4. Male P.,
    5. Goud B. and
    6. Mellman I.
    (1992). The small GTP-binding ptotein rab4 controls an early sorting event in the endocytic pathway. Cell 70, 729–740
    OpenUrlCrossRefPubMedWeb of Science
    1. Vielh E.,
    2. Touchot N.,
    3. Zahraoui A. and
    4. Tavitian A.
    (1989). Nucleotide sequence of a rat cDNA: Rab1B, encoding a Rab1-YPT related protein. Nucl. Acids Res 17, 1770–.
    OpenUrlFREE Full Text
    1. Warren G.
    (1987). Signals and salvage sequences. Nature 327, 17–18
    OpenUrlCrossRefPubMed
    1. Zahraoui A.,
    2. Touchot N.,
    3. Chardin P. and
    4. Tavitian A.
    (1989). The human rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. J. Biol. Chem 264, 12394–12401
    OpenUrlAbstract/FREE Full Text
    1. Zerial M. and
    2. Stenmark H.
    (1993). Rab GTPases in vesicular transport. Curr. Opin. Cell Biol 5, 613–620
    OpenUrlCrossRefPubMed
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Journal Articles
Localization of the small GTP-binding protein rab1p to early compartments of the secretory pathway
J. Saraste, U. Lahtinen, B. Goud
Journal of Cell Science 1995 108: 1541-1552;
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