Ubiquitinated annexin A2 is enriched in the cytoskeleton fraction

• Published in: FEBS letters Vol. 579; no. 1; pp. 203 - 206
• Main Authors: Lauvrak, Silje U., Hollås, Hanne, Døskeland, Anne P., Aukrust, Ingvild, Flatmark, Torgeir, Vedeler, Anni
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 03.01.2005
• Subjects: Animals; Annexin A2; Annexin A2 - analysis; Annexin A2 - isolation & purification; Annexin A2 - metabolism; anxA2; Cell Line, Transformed; coupling of ubiquitin conjugation to ER degradation; CUE; Cytoskeleton; Cytoskeleton - chemistry; Cytoskeleton - metabolism; ECL; enhanced chemiluminescence; horseradish peroxidase; HRP; Intestinal Mucosa - chemistry; Intestinal Mucosa - metabolism; Mice; Post-translational modification; Protein Processing, Post-Translational; Swine; UBA; Ubiquitin; ubiquitin-associated; ubiquitin-interacting motif; Ubiquitins - metabolism; Ubiquitins - physiology; UIM; Ubiquitin; Post-translational modification; CUE; UBA; anxA2; HRP; UIM; Cytoskeleton; Annexin A2; Ub; ECL
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2004.11.076

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.