Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-57456
Nat Cell Biol 2020 Jul 01;227:803-814. doi: 10.1038/s41556-020-0531-y.
Show Gene links Show Anatomy links

SPIN90 associates with mDia1 and the Arp2/3 complex to regulate cortical actin organization.

Cao L , Yonis A , Vaghela M , Barriga EH , Chugh P , Smith MB , Maufront J , Lavoie G , Méant A , Ferber E , Bovellan M , Alberts A , Bertin A , Mayor R , Paluch EK , Roux PP , Jégou A , Romet-Lemonne G , Charras G .


???displayArticle.abstract???
Cell shape is controlled by the submembranous cortex, an actomyosin network mainly generated by two actin nucleators: the Arp2/3 complex and the formin mDia1. Changes in relative nucleator activity may alter cortical organization, mechanics and cell shape. Here we investigate how nucleation-promoting factors mediate interactions between nucleators. In vitro, the nucleation-promoting factor SPIN90 promotes formation of unbranched filaments by Arp2/3, a process thought to provide the initial filament for generation of dendritic networks. Paradoxically, in cells, SPIN90 appears to favour a formin-dominated cortex. Our in vitro experiments reveal that this feature stems mainly from two mechanisms: efficient recruitment of mDia1 to SPIN90-Arp2/3 nucleated filaments and formation of a ternary SPIN90-Arp2/3-mDia1 complex that greatly enhances filament nucleation. Both mechanisms yield rapidly elongating filaments with mDia1 at their barbed ends and SPIN90-Arp2/3 at their pointed ends. Thus, in networks, SPIN90 lowers branching densities and increases the proportion of long filaments elongated by mDia1.

???displayArticle.pubmedLink??? 32572169
???displayArticle.link??? Nat Cell Biol
???displayArticle.grants??? [+]

Species referenced: Xenopus laevis
Genes referenced: fmn1

References [+] :
Acharya, Mammalian Diaphanous 1 Mediates a Pathway for E-cadherin to Stabilize Epithelial Barriers through Junctional Contractility. 2017, Pubmed