Hypoxia inactivates the VHL tumor suppressor through PIASy-mediated SUMO modification.
Cai
Qiliang
Q
Department of Microbiology, Abramson Comprehensive Cancer Center, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, United States of America.
Verma
Suhbash C
SC
Kumar
Pankaj
P
Ma
Michelle
M
Robertson
Erle S
ES
D001665:Binding Sites; D002460:Cell Line; D045744:Cell Line, Tumor; D006801:Humans; D000860:Hypoxia; D051795:Hypoxia-Inducible Factor 1, alpha Subunit / Q000378:metabolism; D008239:Lysine / Q000737:chemistry; D008954:Models, Biological; D000075223:Poly-ADP-Ribose Binding Proteins; D050828:Protein Inhibitors of Activated STAT / Q000235:genetics*; D020033:Protein Isoforms; D017434:Protein Structure, Tertiary; D034741:RNA, Small Interfering / Q000378:metabolism; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D015854:Up-Regulation; D051794:Von Hippel-Lindau Tumor Suppressor Protein / Q000235:genetics*
D051795:Hypoxia-Inducible Factor 1, alpha Subunit; C485891:PIAS4 protein, human; D000075223:Poly-ADP-Ribose Binding Proteins; D050828:Protein Inhibitors of Activated STAT; D020033:Protein Isoforms; D034741:RNA, Small Interfering; D025841:Small Ubiquitin-Related Modifier Proteins; D051794:Von Hippel-Lindau Tumor Suppressor Protein; C497446:VHL protein, human; D008239:Lysine