| Autor: |
Lauvrak, Silje U., Hollås, Hanne, Døskeland, Anne P., Aukrust, Ingvild, Flatmark, Torgeir, Vedeler, Anni |
| Předmět: |
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| Zdroj: |
FEBS Letters; Jan2005, Vol. 579 Issue 1, p203-206, 4p |
| Abstrakt: |
Abstract: 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. [Copyright &y& Elsevier] |
| Databáze: |
Complementary Index |
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