Ubiquitinated annexin A2 is enriched in the cytoskeleton fraction.
Annexin A2 is a multifunctional protein and its cellular functions are regulated by post-translational modifications and ligand binding. When purified from porcine intestinal mucosa and transformed mouse Krebs II cells, SDS-PAGE revealed high-molecular-mass forms in addition to the 36 kDa protomer. These forms were identified as poly-/multi-ubiquitin conjugates of annexin A2, and ubiquitination represents a novel post-translational modification of this protein. Subcellular fractionation of mouse Krebs II cells revealed an enrichment of annexin A2-ubiquitin conjugates in the Triton X-100 resistant cytoskeleton fraction, suggesting that ubiquitinated annexin A2 may have a role associated with its function as an actin-binding protein.
Lauvrak
Silje U
SU
Department of Biomedicine, University of Bergen, Jonas Lies vei 91, N-5009 Bergen, Norway.
Hollås
Hanne
H
Døskeland
Anne P
AP
Aukrust
Ingvild
I
Flatmark
Torgeir
T
Vedeler
Anni
A
D000818:Animals; D017306:Annexin A2 / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism*; D002461:Cell Line, Transformed; D003599:Cytoskeleton / Q000737:chemistry* / Q000378:metabolism; D007413:Intestinal Mucosa / Q000737:chemistry / Q000378:metabolism; D051379:Mice; D011499:Protein Processing, Post-Translational; D013552:Swine; D014452:Ubiquitins / Q000378:metabolism* / Q000502:physiology
D017306:Annexin A2; D014452:Ubiquitins