期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 8, 页码 E643-E652出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1216229110
关键词
endosome; protein crystallography; X-ray scattering; membrane trafficking
资金
- ACRF
- Australian Research Council [DP0878608, DP120103930]
- National Health and Medical Research Council (NHMRC) of Australia [566727, 10012610]
- Canadian Cancer Society
- Australian Research Council (ARC) [FT100100027]
- NHMRC [569601, 511042]
- Australian Research Council [DP0878608] Funding Source: Australian Research Council
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 architecture of the atypical FERM domain and the molecular basis for recognition of these essential sorting sequences. We further show that the PX-FERM proteins share a promiscuous ability to bind a wide array of putative cargo molecules, including receptor tyrosine kinases, and propose a model for their coordinated molecular interactions with membrane, cargo, and regulatory proteins.
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