Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function.

Abstract:

:Internalization of membrane proteins has been studied for more than three decades without solving all the underlying mechanisms. Our knowledge of the clathrin-coated endocytosis is sufficient to understand the basic principles. However, more detailed insight is required to recognize why different proteins enter clathrin-coated pits with different rates and affinities. In addition to clathrin coat components, several adapter systems and even more accessory proteins have been described to preselect membrane proteins before they can enter cells. Recent experimental data have identified the ubiquitin-proteasome system as a regulatory system both in endocytic and lysosomal membrane traffic. This system is well-known for its basic regulatory function in protein degradation, and controls a magnitude of key events. In this review, we will discuss the complexity and implications of this mechanism for membrane trafficking with emphasis on the growth hormone receptor.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Strous GJ,Gent J

doi

10.1016/s0014-5793(02)03187-3

keywords:

subject

Has Abstract

pub_date

2002-10-02 00:00:00

pages

102-9

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014579302031873

journal_volume

529

pub_type

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