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The proline‐rich domain of fission yeast WASp (Wsp1p) interacts with actin filaments and inhibits actin polymerization.

Authors :
Rosenbloom, Aaron D.
Pollard, Thomas D.
Source :
FEBS Letters. Mar2023, Vol. 597 Issue 5, p672-681. 10p.
Publication Year :
2023

Abstract

Members of the Wiskott–Aldrich Syndrome protein (WASp) family activate Arp2/3 complex (actin‐related proteins 2 and 3 complex) to form actin filament branches. The proline‐rich domain (PRD) of WASp contributes to branching nucleation, and the PRD of budding yeast Las17 binds actin filaments [Urbanek AN et al. (2013) Curr Biol 23, 196–203]. Biochemical assays showed the recombinant PRD of fission yeast Schizosaccharomyces pombe Wsp1p binds actin filaments with micromolar affinity. Recombinant PRDs of both Wsp1p and Las17p slowed the elongation of actin filaments by Mg‐ATP‐actin monomers by half and slowed the spontaneous polymerization of Mg‐ATP‐actin monomers modestly. The affinity of PRDs of WASp‐family proteins for actin filaments is high enough to contribute to the reported stimulation of actin filament branching by Arp2/3 complex. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00145793
Volume :
597
Issue :
5
Database :
Academic Search Index
Journal :
FEBS Letters
Publication Type :
Academic Journal
Accession number :
162380777
Full Text :
https://doi.org/10.1002/1873-3468.14571