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 Lettjournal_title
FEBS lettersauthors
Strous GJ,Gent Jdoi
10.1016/s0014-5793(02)03187-3keywords:
subject
Has Abstractpub_date
2002-10-02 00:00:00pages
102-9issue
1eissn
0014-5793issn
1873-3468pii
S0014579302031873journal_volume
529pub_type
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