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Inhibitory regulation of EGF receptor degradation by sorting nexin 5.

Authors: Liu, Hao  Liu, Zu-Qiang  Chen, Carol X-Q  Magill, Stephen  Jiang, Yu  Liu, Yong-Jian 
Citation: Liu H, etal., Biochem Biophys Res Commun. 2006 Apr 7;342(2):537-46. doi: 10.1016/j.bbrc.2006.01.179. Epub 2006 Feb 9.
Pubmed: (View Article at PubMed) PMID:16487940
DOI: Full-text: DOI:10.1016/j.bbrc.2006.01.179

Endosomal trafficking of EGF receptor (EGFR) upon stimulation is a highly regulated process during receptor-mediated signaling. Recently, the sorting nexin (SNX) family has emerged as an important regulator in the membrane trafficking of EGFR. Here, we report the identification of a novel interaction between two members of the family, SNX1 and SNX5, which is mediated by the newly defined BAR domain of both SNXs. We have also shown that the PX domain of SNX5 binds specifically to PtdIns other than to PtdIns(3)P. Furthermore, the BAR domain but not the PX domain of SNX5 is sufficient for its subcellular membrane association. Functionally, overexpression of SNX5 inhibits the degradation of EGFR. This process appears to be independent of its interaction with SNX1. However, overexpression of SNX1 is able to attenuate the effect of SNX5 on EGFR degradation, suggesting the two proteins may play antagonistic roles in regulating endosomal trafficking of the receptor.

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RGD Object Information
RGD ID: 13508623
Created: 2018-03-05
Species: All species
Last Modified: 2018-03-05
Status: ACTIVE



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