Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-01

AUTHORS

D G Drubin, J Mulholland, Z M Zhu, D Botstein

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. More... »

PAGES

288

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/343288a0

DOI

http://dx.doi.org/10.1038/343288a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027562049

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2405279


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