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PI(3,5)P2 controls endosomal branched actin dynamics by regulating cortactin–actin interactions

Hong, Nan Hyung, Qi, Aidong, Weaver, Alissa M.·2015·Journal of Cell Biology
DOI 10.1083/jcb.201412127PMC PMC4555817
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Abstract

Branched actin critically contributes to membrane trafficking by regulating membrane curvature, dynamics, fission, and transport. However, how actin dynamics are controlled at membranes is poorly understood. Here, we identify the branched actin regulator cortactin as a direct binding partner of phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) and demonstrate that their interaction promotes turnover of late endosomal actin. In vitro biochemical studies indicated that cortactin binds PI(3,5)P2 via its actin filament-binding region. Furthermore, PI(3,5)P2 competed with actin filaments for binding to cortactin, thereby antagonizing cortactin activity. These findings suggest that PI(3,5)P2 formation on endosomes may remove cortactin from endosome-associated branched actin. Indeed, inhibition of PI(3,5)P2 production led to cortactin accumulation and actin stabilization on Rab7+ endosomes. Conversely, inhibition of Arp2/3 complex activity greatly reduced cortactin localization to late endosomes. Knockdown of cortactin reversed PI(3,5)P2-inhibitor–induced actin accumulation and stabilization on endosomes. These data suggest a model in which PI(3,5)P2 binding removes cortactin from late endosomal branched actin networks and thereby promotes net actin turnover.

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Metadata

Authors
Hong, N. H., Qi, A., & Weaver, A. M.
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2015-08-31
Volume
210
Issue
5
Pages
753-769
ISSN
  • 0021-9525
  • 1540-8140
DOI
10.1083/jcb.201412127
PMC
PMC4555817
Cited by
89
References
4
Language
en

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