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Identification and characterization of a cDNA encoding mouse CAP: a homolog of the yeast adenylyl cyclase associated protein
A.B. Vojtek, J.A. Cooper
Journal of Cell Science 1993 105: 777-785;

Summary

CAP, an adenylyl cyclase associated protein, is present in Saccharomyces cerevisiae and Schizosaccharomyces pombe. In both organisms, CAP is bifunctional: the N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to respond appropriately to upstream regulatory signals, such as RAS in S. cerevisiae; the C-terminal domain is required for cellular morphogenesis. Here, we describe the isolation of a cDNA encoding a CAP homolog from a higher eukaryote. The mouse CAP cDNA contains an open reading frame capable of encoding a 474 amino acid protein. The protein encoded by the mouse CAP cDNA shows extensive homology to the yeast CAP proteins, particularly in the central poly-proline rich region and in the C-terminal domain. By northern analysis, the CAP message appears to be ubiquitous, but not uniform. By indirect immunofluorescence, ectopically expressed mouse CAP protein is found in the cytoplasm of fibroblasts and, in migrating cells, at the leading edge. Expression of the mouse CAP cDNA in S. cerevisiae complements defects associated with loss of the yeast CAP carboxy-terminal domain. Hence, the function of the CAP carboxy-terminal domain has been conserved from yeast to mouse.

REFERENCES

    1. Archer B.,
    2. Ozcelik T.,
    3. Jahn R.,
    4. Francke U. and
    5. Sudhof T.
    (1990). Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2. J. Biol. Chem 265, 17267–17273
    OpenUrlAbstract/FREE Full Text
    1. Ballester R.,
    2. Michaeli T.,
    3. Ferguson K.,
    4. Xu H.,
    5. McCormick F. and
    6. Wigler M.
    (1989). Genetic analysis of mammalian GAP expressed in yeast. Cell 59, 681–686
    OpenUrlCrossRefPubMedWeb of Science
    1. Benezra R.,
    2. Davis R.,
    3. Lockson D.,
    4. Turner D. and
    5. Weintraub H.
    (1990). The protein Id: a negative regulator of helix-loop-helix DNA binding proteins. Cell 61, 49–59
    OpenUrlCrossRefPubMedWeb of Science
    1. Busch S. and
    2. Sassone-Corsi P.
    (1990). Dimers, leucine zippers and DNA-binding domains. Trends Genet 6, 36–40
    OpenUrlCrossRefPubMedWeb of Science
    1. Buss F.,
    2. Temm-Grove C.,
    3. Henning S. and
    4. Jockusch B.
    (1992). Distribution of profilin in fibroblasts correlates with the presence of highly dynamic actin filaments. Cell Motil. Cytoskel 22, 51–61
    OpenUrlCrossRefPubMedWeb of Science
    1. Chomczynski P. and
    2. Sacchi N.
    (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem 162, 156–159
    OpenUrlCrossRefPubMedWeb of Science
    1. Cohen C. and
    2. Parry D.
    (1986). Alpha-helical coiled-coils: a widespread motif in proteins. Trends Biochem. Sci 11, 245–248
    OpenUrlCrossRefWeb of Science
    1. Elferink L.,
    2. Trimble W. and
    3. Scheller R.
    (1989). Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem 264, 11061–11064
    OpenUrlAbstract/FREE Full Text
    1. Evan G.,
    2. Lewis G.,
    3. Ramsay G. and
    4. Bishop J.
    (1985). Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol 5, 3610–3616
    OpenUrlAbstract/FREE Full Text
    1. Fedor-Chaiken M.,
    2. Deschenes R. and
    3. Broach J.
    (1990). SRV2, a gene required for RAS activation of adenylate cyclase in yeast. Cell 61, 329–340
    OpenUrlCrossRefPubMedWeb of Science
    1. Field J.,
    2. Vojtek A.,
    3. Ballester R.,
    4. Bolger G.,
    5. Colicelli J.,
    6. Ferguson K.,
    7. Gerst J.,
    8. Kataoka T.,
    9. Michaeli T.,
    10. Powers S.,
    11. Riggs M.,
    12. Rodgers L.,
    13. Wieland I.,
    14. Wheland B. and
    15. Wigler M.
    (1990). Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase associated protein. Cell 61, 319–327
    OpenUrlCrossRefPubMedWeb of Science
    1. Fukai Y.,
    2. Kozasa T.,
    3. Kaziro Y.,
    4. Takeda T. and
    5. Yamamoto M.
    (1986). Role of a ras homolog in the life cycle of Schizosaccharomycespombe. Cell 44, 329–336
    OpenUrlCrossRefPubMedWeb of Science
    1. Gerst J.,
    2. Ferguson K.,
    3. Vojtek A.,
    4. Wigler M. and
    5. Field J.
    (1991). CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex. Mol. Cell. Biol 11, 1248–1257
    OpenUrlAbstract/FREE Full Text
    1. Gerst J.,
    2. Rodgers L.,
    3. Riggs M. and
    4. Wigler M.
    (1992). SNC1, a yeast homolog of the synaptic vesicle associated membrane protein/synaptobrevin gene family: genetic interactions with RAS and CAP genes. Proc. Nat. Acad. Sci. USA 89, 4338–4342
    OpenUrlAbstract/FREE Full Text
    1. Gieselman R. and
    2. Mann K.
    (1992). ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase associated protein from yeast. FEBS Lett 298, 149–153
    OpenUrlCrossRefPubMedWeb of Science
    1. Goldschmidt-Clermont P.,
    2. Kim J.,
    3. Machesky L.,
    4. Rhee S. and
    5. Pollard T.
    (1991). Regulation of phospholipase C by profilin and tyrosine phosphorylation. Science 251, 1231–1233
    OpenUrlAbstract/FREE Full Text
    1. Goldschmidt-Clermont P.,
    2. Machesky L.,
    3. Baldassare J. and
    4. Pollard T.
    (1990). The actin binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science 247, 1575–1578
    OpenUrlAbstract/FREE Full Text
    1. Hartwig H.,
    2. Chambers K.,
    3. Hopcia K. and
    4. Kwiatkowski D.
    (1989). Association of profilin with filament-free regions of human leukocyte and platelet membranes and reversible membrane binding during platelet activation. J. Cell Biol 109, 1571–1579
    OpenUrlAbstract/FREE Full Text
    1. Kawamukai M.,
    2. Gerst J.,
    3. Field J.,
    4. Riggs M.,
    5. Rodgers L.,
    6. Wigler M. and
    7. Young D.
    (1992). Genetic and biochemical analysis of the adenylyl cyclase associated protein, cap, in S. pombe. Mol. Biol. Cell 3, 167–180
    OpenUrlAbstract/FREE Full Text
    1. Lassing I. and
    2. Lindberg U.
    (1985). Specific interaction betweenphosphatidylinositol-4,5-bisphosphate and profilactin. Nature 314, 472–474
    OpenUrlCrossRefPubMedWeb of Science
    1. Lassing I. and
    2. Lindberg U.
    (1988). Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex. J. Cell. Biochem 37, 255–267
    OpenUrlCrossRefPubMedWeb of Science
    1. Matviw H.,
    2. Yu G. and
    3. Young D.
    (1992). Identification of a human cDNA encoding a protein that is structurally and functionally related to the yeast adenylyl cyclase associated CAP proteins. Mol. Cell. Biol 12, 5033–5040
    OpenUrlAbstract/FREE Full Text
    1. Pollard T. and
    2. Cooper J.
    (1986). Actin and actin binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem 55, 987–1035
    OpenUrlCrossRefPubMedWeb of Science
    1. Roth M.,
    2. Zahler A. and
    3. Stolk J.
    (1991). A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. J. Cell Biol 115, 587–596
    OpenUrlAbstract/FREE Full Text
    1. Toda T.,
    2. Uno I.,
    3. Ishikawa T.,
    4. Powers S.,
    5. Kataoka T.,
    6. Broek D.,
    7. Cameron S.,
    8. Broach J.,
    9. Matsumoto K. and
    10. Wigler M.
    (1985). In yeast, RAS proteins are controlling elements of adenylate cyclase. Cell 40, 27–36
    OpenUrlCrossRefPubMedWeb of Science
    1. Vojtek A.,
    2. Haarer B.,
    3. Field J.,
    4. Gerst J.,
    5. Pollard T.,
    6. Brown S. and
    7. Wigler M.
    (1991). Evidence for a functional link between profilin and CAP is the yeast S. cerevisiae. Cell 66, 497–505
    OpenUrlCrossRefPubMedWeb of Science
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Journal Articles
Identification and characterization of a cDNA encoding mouse CAP: a homolog of the yeast adenylyl cyclase associated protein
A.B. Vojtek, J.A. Cooper
Journal of Cell Science 1993 105: 777-785;
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