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Inhibitory regulation of EGF receptor degradation by sorting nexin 5.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Liu H,Liu ZQ,Chen CX,Magill S,Jiang Y,Liu YJ

doi

10.1016/j.bbrc.2006.01.179

subject

Has Abstract

pub_date

2006-04-07 00:00:00

pages

537-46

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)00178-1

journal_volume

342

pub_type

杂志文章

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