Reactome | PIAS4 SUMOylates VHL with SUMO1

PIAS4 SUMOylates VHL with SUMO1

Stable Identifier

R-HSA-4551721

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

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