|Whitcomb, Elizabeth -|
|Lefeuvre, Aurelie -|
|Taylor, Allen -|
Submitted to: Journal of Federation of American Societies for Experimental Biology
Publication Type: Abstract Only
Publication Acceptance Date: February 13, 2013
Publication Date: April 9, 2013
Citation: Whitcomb, E.A., Lefeuvre, A., Taylor, A. 2013. The Ubiquitin Conjugating Enzyme UbcH7, controls cell migration. Journal of Federation of American Societies for Experimental Biology. 27:785.4. Technical Abstract: Post translational modification by ubiquitination can target proteins for degradation, allow the interaction of proteins to form complexes or direct relocalization of proteins to different subcellular compartments. As such, ubiquitin controls a variety of essential cellular processes. Previously we demonstrated that the ubiquitin conjugating enzyme, UbcH7 controls both the entry into and progression through S phase of the cell cycle (Whitcomb et. al 2009 Mol. Biol. Cell v20:1–9). In our search for cell cycle regulatory proteins which might be involved in the UbcH7-mediated control of the cell cycle, we discovered that UbcH7 affects the level of the cyclin dependent kinase inhibitor, p27, but does not affect the similarly regulated cyclin dependent kinase, p21. Interestingly, depletion of UbcH7 affects p27 levels primarily in the cytosol. While nuclear p27 controls the G1 to S transition of the cell cycle through inhibition of the cyclin dependent kinases, cytosolic p27 plays a role in cell migration. Thus, we asked whether manipulation of UbcH7 also affected cell migration and find that depletion of UbcH7 inhibits cell migration. These results suggest that UbcH7 might be an attractive drug target as it plays roles in controlling both the cell cycle and cell migration.