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Ubiquitin‐Related Modifier SUMO1 and Nucleocytoplasmic Transport
Author(s) -
Pichler Andrea,
Melchior Frauke
Publication year - 2002
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2002.30601.x
Subject(s) - sumo protein , ubiquitin , sumo enzymes , microbiology and biotechnology , biology , nuclear transport , ubiquitins , transport protein , protein degradation , nuclear protein , intracellular , ubiquitin ligase , biochemistry , cell nucleus , nucleus , gene , transcription factor
S mall u biquitin related mo difier SUMO‐1 and its homologs can be conjugated to a large number of cellular proteins. This involves an enzymatic cascade that resembles ubiquitination, and the modification can be reverted by isopeptidases. SUMOylation does not lead to degradation but instead appears to regulate protein/protein interactions, intracellular localization and protects some modified targets from ubiquitin‐dependent degradation. Data collected for more than 30 different target proteins point to two cellular processes, nucleocytoplasmic transport and intranuclear targeting, in which SUMO plays an active role. Here we will focus on links between SUMO and nuclear transport.