Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments-Reference-Cited by-同舟云学术

Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments

Published:2020-02-15 Issue:4 Volume:31 Page:273-286
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Bradley Alexander O.¹,Vizcarra Christina L.¹,Bailey Hannah M.¹,Quinlan Margot E.¹²

Affiliation:

1. Department of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095

2. Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095

Abstract

The actin nucleators Cappuccino and Spire collaborate to build an actin mesh in oocytes. We resolve two questions regarding their mechanism of action: Spire binds both barbed and pointed ends of actin filaments; however, barbed-end binding is not necessary for oogenesis or synergistic actin assembly.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference49 articles.

1. Active Mechanics Reveal Molecular-Scale Force Kinetics in Living Oocytes

2. Active diffusion positions the nucleus in mouse oocytes

3. Spindle Positioning in Mouse Oocytes Relies on a Dynamic Meshwork of Actin Filaments

4. Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains

5. Analysis of the Function of Spire in Actin Assembly and Its Synergy with Formin and Profilin

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