WTIP impairs AKT phosphorylation and activation leading to enhanced expression and transcriptional activity of FOXO1 which further increases p21Cip1 and p27Kip1 and decreases cyclin D1 which consequently results in cell cycle arrest.
The findings suggest that the UBA2-WTIP fusion is an oncogenic fusion gene as well as a promising therapeutic target for the treatment of acute myeloid leukemia.
We show that all three mammalian Ajuba family proteins - AJUBA LIMD1 and WTIP - exhibit tension-dependent localization to adherens junctions and that both LATS family proteins LATS1 and LATS2 exhibit an overlapping tension-dependent junctional localization
Wtip regulates the stable formation of cell adhesions to both extracellular matrix and neighboring cells and suggest that Wtip is necessary for normal glomerular filtration barrier function
Full-length Ror2 recruits Wtip to the cell membrane a mutant involved in human disease fails to do so. Both genes and proteins show overlapping expression in the mouse embryo.
WTIP is a member of the Ajuba family of LIM-domain containing proteins. Ajuba LIM proteins co-repress E-cadherin expression through interaction with the SNAG domain of Snail/Slug and promote epithelial to mesenchymal differentiation in a Xenopus model.
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