Ubiquitinated annexin A2 is enriched in the cytoskeleton fraction
- 7 December 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (1) , 203-206
- https://doi.org/10.1016/j.febslet.2004.11.076
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.Keywords
This publication has 30 references indexed in Scilit:
- Specificity of the Interaction between Ubiquitin-associated Domains and UbiquitinJournal of Biological Chemistry, 2004
- A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machineryProceedings of the National Academy of Sciences, 2003
- Non-traditional Functions of Ubiquitin and Ubiquitin-binding ProteinsJournal of Biological Chemistry, 2003
- Modulating signaling events in smooth muscle: cleavage of annexin 2 abolishes its binding to lipid raftsThe FASEB Journal, 2002
- Nitration of Annexin II TetramerBiochemistry, 2001
- Recognition of the polyubiquitin proteolytic signalThe EMBO Journal, 2000
- Mapping of a regulatory important site for protein kinase C phosphorylation in the N-terminal domain of annexin IIBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1996
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970