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Gene Review

ABP1  -  Abp1p

Saccharomyces cerevisiae S288c

Synonyms: Actin-binding protein, YCR088W, YCR88W
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Disease relevance of ABP1


High impact information on ABP1


Biological context of ABP1


Anatomical context of ABP1


Associations of ABP1 with chemical compounds


Physical interactions of ABP1


Regulatory relationships of ABP1

  • YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed [17].
  • In the years following its discovery, profilin's role in vivo progressed from that of a simple actin-binding protein which inhibits actin polymerization, to one which, as an important regulator of the cytoskeleton, can even promote actin polymerization under the appropriate circumstances [18].

Other interactions of ABP1

  • Direct regulation of Arp2/3 complex activity and function by the actin binding protein coronin [19].
  • First, since mutations in pairs of actin-binding protein genes cause inviability, the actin cytoskeleton of yeast does not contain a high degree of redundancy [20].
  • Abp1 null mutations, like rvs167 mutations, result in defects in sporulation and reduced viability under certain suboptimal growth conditions [6].
  • Double mutants lacking fimbrin and either Abp1p or capping protein show negative synthetic effects on growth, in the most extreme case resulting in lethality [20].
  • The apparent redundancy between Sla1p and Abp1p resides in the C-terminal repeat region of Sla1p [21].

Analytical, diagnostic and therapeutic context of ABP1


  1. Hepatitis B virus core protein interacts with the C-terminal region of actin-binding protein. Huang, C.J., Chen, Y.H., Ting, L.P. J. Biomed. Sci. (2000) [Pubmed]
  2. Distribution of actin-binding protein and myosin in polymorphonuclear leukocytes during locomotion and phagocytosis. Valerius, N.H., Stendahl, O., Hartwig, J.H., Stossel, T.P. Cell (1981) [Pubmed]
  3. Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I. Drubin, D.G., Mulholland, J., Zhu, Z.M., Botstein, D. Nature (1990) [Pubmed]
  4. Mapping actin surfaces required for functional interactions in vivo. Holtzman, D.A., Wertman, K.F., Drubin, D.G. J. Cell Biol. (1994) [Pubmed]
  5. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. Holtzman, D.A., Yang, S., Drubin, D.G. J. Cell Biol. (1993) [Pubmed]
  6. Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton. Lila, T., Drubin, D.G. Mol. Biol. Cell (1997) [Pubmed]
  7. End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Wesp, A., Hicke, L., Palecek, J., Lombardi, R., Aust, T., Munn, A.L., Riezman, H. Mol. Biol. Cell (1997) [Pubmed]
  8. Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions. Quintero-Monzon, O., Rodal, A.A., Strokopytov, B., Almo, S.C., Goode, B.L. Mol. Biol. Cell (2005) [Pubmed]
  9. The phosphoinositide phosphatase Sjl2 is recruited to cortical actin patches in the control of vesicle formation and fission during endocytosis. Stefan, C.J., Padilla, S.M., Audhya, A., Emr, S.D. Mol. Cell. Biol. (2005) [Pubmed]
  10. Abp1 regulates pseudopodium number in chemotaxing Dictyostelium cells. Wang, Y., O'Halloran, T.J. J. Cell. Sci. (2006) [Pubmed]
  11. Coupling actin dynamics and membrane dynamics during endocytosis. Schafer, D.A. Curr. Opin. Cell Biol. (2002) [Pubmed]
  12. Distribution of actin-binding protein and myosin in macrophages during spreading and phagocytosis. Stendahl, O.I., Hartwig, J.H., Brotschi, E.A., Stossel, T.P. J. Cell Biol. (1980) [Pubmed]
  13. Interaptin, an actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments. Rivero, F., Kuspa, A., Brokamp, R., Matzner, M., Noegel, A.A. J. Cell Biol. (1998) [Pubmed]
  14. Cofilin is an essential component of the yeast cortical cytoskeleton. Moon, A.L., Janmey, P.A., Louie, K.A., Drubin, D.G. J. Cell Biol. (1993) [Pubmed]
  15. The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. McCann, R.O., Craig, S.W. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  16. A conserved proline-rich region of the Saccharomyces cerevisiae cyclase-associated protein binds SH3 domains and modulates cytoskeletal localization. Freeman, N.L., Lila, T., Mintzer, K.A., Chen, Z., Pahk, A.J., Ren, R., Drubin, D.G., Field, J. Mol. Cell. Biol. (1996) [Pubmed]
  17. YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed. Sattlegger, E., Swanson, M.J., Ashcraft, E.A., Jennings, J.L., Fekete, R.A., Link, A.J., Hinnebusch, A.G. J. Biol. Chem. (2004) [Pubmed]
  18. Profilin: at the crossroads of signal transduction and the actin cytoskeleton. Sohn, R.H., Goldschmidt-Clermont, P.J. Bioessays (1994) [Pubmed]
  19. Direct regulation of Arp2/3 complex activity and function by the actin binding protein coronin. Humphries, C.L., Balcer, H.I., D'Agostino, J.L., Winsor, B., Drubin, D.G., Barnes, G., Andrews, B.J., Goode, B.L. J. Cell Biol. (2002) [Pubmed]
  20. Unexpected combinations of null mutations in genes encoding the actin cytoskeleton are lethal in yeast. Adams, A.E., Cooper, J.A., Drubin, D.G. Mol. Biol. Cell (1993) [Pubmed]
  21. Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology. Ayscough, K.R., Eby, J.J., Lila, T., Dewar, H., Kozminski, K.G., Drubin, D.G. Mol. Biol. Cell (1999) [Pubmed]
  22. Salmonella effectors translocated across the vacuolar membrane interact with the actin cytoskeleton. Miao, E.A., Brittnacher, M., Haraga, A., Jeng, R.L., Welch, M.D., Miller, S.I. Mol. Microbiol. (2003) [Pubmed]
  23. The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis. Rath, A., Davidson, A.R. Protein Sci. (2000) [Pubmed]
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