Ubiquitination of Rac1 by inhibitors of apoptosis (IAPs).
Ubiquitination of proteins has emerged as a vital posttranslational modification at the crux of numerous signalling pathways, regulating them in various ways. Most members of the small GTPase family including Ras and Rho proteins are regulated by GEFs, GAPs, and RhoGDIs that modulate their cycling between the active and inactive states. Ubiquitination has added another layer to the regulation of small GTPases. Recently, we have uncovered that inhibitors of apoptosis (IAPs) function as direct E3 ubiquitin ligases for Rho GTPase Rac1 and target it for proteasomal degradation. Here, we describe in vitro and in vivo ubiquitination assays for detecting the conjugation of ubiquitin to Rac1 by XIAP and cIAP1.
Cell Death Signaling Group, Institute for Biochemie II, Goethe University Medical School, Goethe University, Frankfurt, Germany.
Tripat Kaur
TK
Oberoi-Khanuja
Krishnaraj
K
Rajalingam
D057809:HEK293 Cells; D006367:HeLa Cells; D006639:Histidine / Q000737:chemistry; D006801:Humans; D009571:Nitrilotriacetic Acid / Q000031:analogs & derivatives / Q000737:chemistry; D009942:Organometallic Compounds / Q000737:chemistry; D011485:Protein Binding; D054875:Ubiquitination; D051636:X-Linked Inhibitor of Apoptosis Protein / Q000378:metabolism*; D020830:rac1 GTP-Binding Protein / Q000378:metabolism*
D009942:Organometallic Compounds; D051636:X-Linked Inhibitor of Apoptosis Protein; C088321:nickel nitrilotriacetic acid; D006639:Histidine; D020830:rac1 GTP-Binding Protein; D009571:Nitrilotriacetic Acid