Anillin Puts RhoA in Touch with PIP2

Edwin Munro

doi:10.1016/j.devcel.2019.05.042

Anillin Puts RhoA in Touch with PIP2

Dev Cell. 2019 Jun 17;49(6):819-820. doi: 10.1016/j.devcel.2019.05.042.

Author

Edwin Munro¹

Affiliation

¹ Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA. Electronic address: emunro@uchicago.edu.

PMID: 31211987
DOI: 10.1016/j.devcel.2019.05.042

Abstract

In this issue of Developmental Cell, Budnar and colleagues report how the scaffolding protein anillin uses cycles of transient binding interactions to enhance the residence time and signaling output of active RhoA to control actomyosin contractility at epithelial junctions and during cell division.

Publication types

Comment

MeSH terms

Actomyosin
Contractile Proteins*
Kinetics
Touch*
rhoA GTP-Binding Protein

Substances

Contractile Proteins
anillin
Actomyosin
rhoA GTP-Binding Protein