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Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins.

Proc Natl Acad Sci U S A.. 2013-02;  110(8):E643 - 52
Ghai R, Bugarcic A, Liu H, Norwood SJ, Skeldal S, Coulson EJ, Li SS, Teasdale RD, Collins BM. Institute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD 4072, Australia.
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摘要

Transit of proteins through the endosomal organelle following endocytosis is critical for regulating the homeostasis of cell-surface proteins and controlling signal transduction pathways. However, the mechanisms that control these membrane-transport processes are poorly understood. The Phox-homology (PX) domain-containing proteins sorting nexin (SNX) 17, SNX27, and SNX31 have emerged recently as key regulators of endosomal recycling and bind conserved Asn-Pro-Xaa-Tyr-sorting signals in transmembrane cargos via an atypical band, 4.1/ezrin/radixin/moesin (FERM) domain. Here we present the crystal structure of the SNX17 FERM domain bound to the sorting motif of the P-selectin adhesion protein, revealing both the a... More

关键词

endosome;protein crystallography;X-ray scattering;membrane trafficking