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Ubiquitinated annexin A2 is enriched in the cytoskeleton fraction
Author(s) -
Lauvrak Silje U.,
Hollås Hanne,
Døskeland Anne P.,
Aukrust Ingvild,
Flatmark Torgeir,
Vedeler Anni
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.076
Subject(s) - annexin a2 , ubiquitin , annexin , cytoskeleton , cell fractionation , microbiology and biotechnology , biochemistry , biology , chemistry , cell , enzyme , gene
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.