PIAS4 SUMOylates VHL with SUMO1

Stable Identifier
R-HSA-4551721
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

PIAS4 SUMOylates VHL at lysine-159, lysine-171, and lysine-196 with SUMO1 (Cai et al. 2010, Cai and Robertson 2010, Chien et al. 2013). SUMOylation facilitates the oligomerization of VHL, abolishes the inhibitory function of VHL on HIF1A, and abolishes the tumor suppressor function of VHL by inactivating the ubiquitinylation activity of VHL.

Literature References
PubMed ID Title Journal Year
20844582 Ubiquitin/SUMO modification regulates VHL protein stability and nucleocytoplasmic localization

Cai, Q, Robertson, ES

PLoS ONE 2010
20300531 Hypoxia inactivates the VHL tumor suppressor through PIASy-mediated SUMO modification

Cai, Q, Verma, SC, Kumar, P, Ma, M, Robertson, ES

PLoS ONE 2010
24002598 PIAS4 is an activator of hypoxia signalling via VHL suppression during growth of pancreatic cancer cells

Chien, W, Lee, KL, Ding, LW, Wuensche, P, Kato, H, Doan, NB, Poellinger, L, Said, JW, Koeffler, HP

Br. J. Cancer 2013
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
SUMO transferase activity of PIAS4 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created