SNX-BAR proteins in phosphoinositide-mediated, tubular-based endosomal sorting

Jan R.T. van Weering, Paul Verkade, Peter J. Cullen*

*Corresponding author for this work

Research output: Contribution to journalReview articleAcademicpeer-review

Abstract

The endocytic network is morphologically characterized by a wide variety of membrane bound compartments that are able to undergo dynamic re-modeling through tubular and vesicular structures. The precise molecular mechanisms governing such re-modeling, and the events that co-ordinated this with the major role of endosomes, cargo sorting, remain unclear. That said, recent work on a protein family of sorting nexins (SNX) - especially a subfamily of SNX that contain a BAR domain (SNX-BARs) - has begun to shed some much needed light on these issues and in particular the process of tubular-based endosomal sorting. SNX-BARs are evolutionary conserved in endosomal protein complexes such as retromer, where they co-ordinate membrane deformation with cargo selection. Furthermore a central theme emerges of SNX-BARs linking the forming membrane carrier to cytoskeletal elements for transport through motor proteins such as dynein. By studying these SNX-BARs, we are gaining an increasingly detailed appreciation of the mechanistic basis of endosomal sorting and how this highly dynamic process functions in health and disease.

Original languageEnglish
Pages (from-to)371-380
Number of pages10
JournalSeminars in Cell and Developmental Biology
Volume21
Issue number4
DOIs
Publication statusPublished - Jun 2010

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