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SCP1 encodes an actin-bundling protein in yeast.

Authors
  • Winder, Steven J
  • Jess, Thomas
  • Ayscough, Kathryn R
Type
Published Article
Journal
Biochemical Journal
Publisher
Portland Press
Publication Date
Oct 15, 2003
Volume
375
Issue
Pt 2
Pages
287–295
Identifiers
PMID: 12868959
Source
Medline
License
Unknown

Abstract

The association of F-actin (filamentous actin) with a large number of binding proteins is essential for cellular function. Actin-binding proteins control the dynamics of actin filaments, nucleate new filaments and facilitate formation of higher-order structures such as actin bundles. The yeast gene SCP1 encodes a small protein with significant homology to mammalian SM22/transgelin. We have investigated the role of Scp1p in budding yeast to probe the fundamental role of this family of proteins. Here, we demonstrate that Scp1p binds to F-actin and induces the formation of tight F-actin bundles in vitro. Deletion of SCP1 in yeast lacking the actin-bundling protein, fimbrin (Sac6p), exacerbates the disrupted actin phenotype and enhances latrunculin-A sensitivity. Furthermore, Scp1p co-localizes with actin in cortical patches and its localization is lost in the presence of latrunculin-A. Our data support a role for Scp1p in bundling actin filaments and, in concert with Sac6p, acting as a second actin-bundling activity crucial to the stability of the yeast actin cytoskeleton.

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