Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I
- PMID: 2405279
- DOI: 10.1038/343288a0
Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I
Abstract
In yeast, the cortical actin cytoskeleton seems to specify sites of growth of the cell surface. Because the actin-binding protein ABP1p is associated with the cortical cytoskeleton of Saccharomyces cerevisiae, it might be involved in the spatial organization of cell surface growth. ABP1p is localized to the cortical cytoskeleton and its overproduction causes assembly of the cortical actin cytoskeleton at inappropriate sites on the cell surface, resulting in delocalized surface growth. We have now cloned and sequenced the gene encoding ABP1p. ABP1p is a novel protein with a 50 amino-acid C-terminal domain that is very similar to the SH3 domain in the non-catalytic region of nonreceptor tyrosine kinases (including those encoded by the proto-oncogenes c-src and c-abl), in phospholipase C gamma and in alpha-spectrin. We also identified an SH3-related motif in the actin-binding tail domain of myosin-I. The identification of SH3 domains in a family of otherwise unrelated proteins that associate with the membrane cytoskeleton indicates that this domain might serve to bring together signal transduction proteins and their targets or regulators, or both, in the membrane cytoskeleton.
Similar articles
-
The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic context.Genetics. 2007 May;176(1):193-208. doi: 10.1534/genetics.106.070300. Epub 2007 Apr 3. Genetics. 2007. PMID: 17409071 Free PMC article.
-
Verprolin function in endocytosis and actin organization. Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain.FEBS J. 2007 Aug;274(16):4103-25. doi: 10.1111/j.1742-4658.2007.05936.x. Epub 2007 Jul 16. FEBS J. 2007. PMID: 17635585
-
Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton.Mol Biol Cell. 1997 Feb;8(2):367-85. doi: 10.1091/mbc.8.2.367. Mol Biol Cell. 1997. PMID: 9190214 Free PMC article.
-
Actin and actin-binding proteins in yeast.Cell Motil Cytoskeleton. 1990;15(1):7-11. doi: 10.1002/cm.970150103. Cell Motil Cytoskeleton. 1990. PMID: 2403847 Review. No abstract available.
-
SH3--an abundant protein domain in search of a function.FEBS Lett. 1992 Jul 27;307(1):55-61. doi: 10.1016/0014-5793(92)80901-r. FEBS Lett. 1992. PMID: 1639195 Review.
Cited by
-
Anti-Cdc25 antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein.Mol Cell Biol. 1992 Jun;12(6):2653-61. doi: 10.1128/mcb.12.6.2653-2661.1992. Mol Cell Biol. 1992. PMID: 1588963 Free PMC article.
-
Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3'-kinase activity with pp60v-src and alter cellular morphology.J Virol. 1992 Apr;66(4):1866-74. doi: 10.1128/JVI.66.4.1866-1874.1992. J Virol. 1992. PMID: 1312609 Free PMC article.
-
The spectrin skeleton: from red cells to brain.J Clin Invest. 1991 May;87(5):1483-9. doi: 10.1172/JCI115157. J Clin Invest. 1991. PMID: 1850755 Free PMC article. Review. No abstract available.
-
Site-directed mutagenesis of the yeast actin gene: a test for actin function in vivo.EMBO J. 1991 Dec;10(12):3951-8. doi: 10.1002/j.1460-2075.1991.tb04965.x. EMBO J. 1991. PMID: 1935913 Free PMC article.
-
Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains.Mol Cell Biol. 1994 Jul;14(7):4509-21. doi: 10.1128/mcb.14.7.4509-4521.1994. Mol Cell Biol. 1994. PMID: 7516469 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous
