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SNX9 - a prelude to vesicle release
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
2009 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 122, no 1, 5-11 p.Article in journal (Refereed) Published
Abstract [en]

The sorting nexin SNX9 has, in the past few years, been singled out as an important protein that participates in fundamental cellular activities. SNX9 binds strongly to dynamin and is partly responsible for the recruitment of this GTPase to sites of endocytosis. SNX9 also has a high capacity for modulation of the membrane and might therefore participate in the formation of the narrow neck of endocytic vesicles before scission occurs. Once assembled on the membrane, SNX9 stimulates the GTPase activity of dynamin to facilitate the scission reaction. It has also become clear that SNX9 has the ability to activate the actin regulator N-WASP in a membrane-dependent manner to coordinate actin polymerization with vesicle release. In this Commentary, we summarize several aspects of SNX9 structure and function in the context of membrane remodeling, discuss its interplay with various interaction partners and present a model of how SNX9 might work in endocytosis.

Place, publisher, year, edition, pages
2009. Vol. 122, no 1, 5-11 p.
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-36427DOI: 10.1242/jcs.037135ISI: 000261780200002PubMedID: 19092055OAI: oai:DiVA.org:umu-36427DiVA: diva2:354142
Available from: 2010-09-30 Created: 2010-09-30 Last updated: 2017-12-12Bibliographically approved

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