SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis.

SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Research Abstract Details 

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SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Abstract Text:

Multiple modes of endocytosis require actin-dependent remodeling of the plasma membrane; however, neither the factors linking these processes nor their mechanisms of action are understood. The sorting nexin, SNX9, localizes to clathrin-coated pits where it interacts with dynamin and functions in clathrin-mediated endocytosis. Here, we demonstrate that SNX9 also localizes to actin-rich structures implicated in fluid-phase uptake, including tubular membranes containing GPI-anchored proteins and dorsal membrane ruffles. Moreover, we show that SNX9 is critical for dorsal ruffle formation and for clathrin-independent, actin-dependent fluid-phase endocytosis. In vitro, SNX9 directly associates with N-WASP, an Arp2/3 complex activator, and stimulates N-WASP/Arp2/3-mediated actin assembly. SNX9-stimulated actin polymerization is greatly enhanced by PI(4,5)P(2)-containing liposomes, due in part to PI(4,5)P(2)-induced SNX9 oligomerization. These results suggest a mechanism for the spatial and temporal regulation of N-WASP-dependent actin assembly and implicate SNX9 in directly coupling actin dynamics to membrane remodeling during multiple modes of endocytosis.

SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Publishing Authors By Initials

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, tertiary: protein interaction domains and motifs: src homology domains research

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SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Developmental cell

VOLUME: 13

Page Numbers: 43-56

Journal Abbreviation: Dev. Cell

ISSN: 1534-5807

DAY: 3

MONTH: Jul

YEAR: 2007

SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101120028

SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Keywords Mesh Terms:

KEYWORDS: src Homology Domains

MESH TERMS: physiology

Chemical & Substance for Abstract: SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Information

Substance Name: phosphatidylinositol phosphate, PtdIns(4

Registry Number: 0

Grant and Affiliation Information for SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis.

AFFILIATION: Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. yarar@scripps.edu

Country: United States

AGENCY: United States NIMH

GRANT: MH61345

ACRONYM: MH

MEDLINETA: Dev Cell

REFSOURCE: Dev Cell. 2007 Jul;13(1):3-4

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