Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport.
Small ubiquitin related modifier 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.
Pichler
Andrea
A
Max Planck Institute for Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
Melchior
Frauke
F
D021581:Active Transport, Cell Nucleus; D000818:Animals; D019759:Carbon-Nitrogen Lyases / Q000378:metabolism; D020690:GTPase-Activating Proteins / Q000378:metabolism; D008025:Ligases / Q000378:metabolism; D025842:SUMO-1 Protein / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases; D000098843:Ubiquitin-Conjugating Enzyme UBC9
D020690:GTPase-Activating Proteins; D025842:SUMO-1 Protein; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases; D019759:Carbon-Nitrogen Lyases; C034300:isopeptidase; D008025:Ligases; D000098843:Ubiquitin-Conjugating Enzyme UBC9