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Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function
Author(s) -
Strous Ger J,
Gent Jürgen
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03187-3
Subject(s) - endocytic cycle , endocytosis , clathrin , internalization , microbiology and biotechnology , ubiquitin , receptor mediated endocytosis , signal transducing adaptor protein , function (biology) , biology , membrane protein , receptor , membrane , biochemistry , signal transduction , gene
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.