Ubiquitination of the ubiquitin-binding machinery: how early ESCRT components are controlled
Author(s) -
Barbara Korbei
Publication year - 2022
Publication title -
essays in biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.351
H-Index - 66
eISSN - 1744-1358
pISSN - 0071-1365
DOI - 10.1042/ebc20210042
Subject(s) - ubiquitin , microbiology and biotechnology , escrt , lysosome , autophagy , function (biology) , protein targeting , vacuole , ubiquitin ligase , ubiquitin conjugating enzyme , translation (biology) , chemistry , biology , biochemistry , receptor , membrane protein , endosome , membrane , messenger rna , gene , enzyme , apoptosis , cytoplasm
To be able to quickly and accurately respond to the environment, cells need to tightly control the amount and localization of plasma membrane proteins. The post-translation modification by the protein modifier ubiquitin is the key signal for guiding membrane-associated cargo to the lysosome/vacuole for their degradation. The machinery responsible for such sorting contains several subunits that function as ubiquitin receptors, many of which are themselves subjected to ubiquitination. This review will focus on what is currently known about the modulation of the machinery itself by ubiquitination and how this might affect its function with a special emphasis on current findings from the plant field.
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