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

作者：van Weering Jan R T; Verkade Paul; Cullen Peter J^*

来源：Seminars in Cell & Developmental Biology, 2010, 21(4): 371-380.

DOI：10.1016/j.semcdb.2009.11.009

• Sorting nexin
• Endosome
• Phosphoinositide
• Dynein
• Retromer
• Endocytosis

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) - as 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.

• 出版日期2010-6