Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation.
作者： Lene Melsæther Grøvdal , Espen Stang , Alexander Sorkin , Inger Helene Madshus
DOI: 10.1016/J.YEXCR.2004.07.003
关键词:
摘要: Mutation of the binding site for Cbl (Tyr1045) in EGF receptor (EGFR) results impaired ubiquitination but does not affect EGFR internalization. However, Y1045F mutation resulted strongly decreased degradation EGFR, as well efficient recycling to plasma membrane. Significantly, more wild-type than was found localizing multivesicular late endosomes. Ubiquitination HeLa cells inhibited both upon overexpressing N-terminal part and a double mutant Grb2 incapable interacting with thereby being indirectly recruiting EGFR. Collectively, these data suggest that resulting from direct pTyr1045 is critical lysosomal sorting contrast Grb2-mediated
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