Ubiquitinated annexin A2 is enriched in the cytoskeleton fraction |
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Authors: | Lauvrak Silje U Hollås Hanne Døskeland Anne P Aukrust Ingvild Flatmark Torgeir Vedeler Anni |
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Affiliation: | Department of Biomedicine, University of Bergen, Jonas Lies vei 91, N-5009 Bergen, Norway. |
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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. |
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Keywords: | anxA2, annexin A2 CUE, coupling of ubiquitin conjugation to ER degradation ECL, enhanced chemiluminescence HRP, horseradish peroxidase Ub, ubiquitin UBA, ubiquitin-associated UIM, ubiquitin-interacting motif |
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