SUMO, ubiquitin's mysterious cousin.
Covalent modification of cellular proteins by the ubiquitin-like modifier SUMO regulates various cellular processes, such as nuclear transport, signal transduction, stress response and cell-cycle progression. But, in contrast to ubiquitylation, sumoylation does not tag proteins for degradation, but seems to enhance their stability or modulate their subcellular compartmentalization.
Müller
S
S
Max Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18a, 82152, Martinsried, Germany. stmuelle@biochem.mpg.de
Hoege
C
C
Pyrowolakis
G
G
Jentsch
S
S
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008025:Ligases / Q000378:metabolism; D008969:Molecular Sequence Data; D011506:Proteins / Q000378:metabolism; D025842:SUMO-1 Protein; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D044763:Ubiquitin-Conjugating Enzymes; D014452:Ubiquitins / Q000235:genetics / Q000378:metabolism*; D000098843:Ubiquitin-Conjugating Enzyme UBC9
D011506:Proteins; D025842:SUMO-1 Protein; D014452:Ubiquitins; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases; D000098843:Ubiquitin-Conjugating Enzyme UBC9