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Post-translational modifications of Annexin A2 are linked to its association with perinuclear nonpolysomal mRNP complexes.

FEBS Open Bio. 2017; 
Aukrust Ingvild,Rosenberg Linn Andersen,Ankerud Mia Madeleine,Bertelsen Vibeke,Holl?s Hanne,Saraste Jaakko,Grindheim Ann Kari,Vedeler
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Recombinant Proteins Biosciences, San Jose, CA, USA; 1 : 1000 dilution), tubulin (A01410-40; Genscript, Piscat- away, NJ, USA; 1 Get A Quote

摘要

Various post-translational modifications (PTMs) regulate the localisation and function of the multifunctional protein Annexin A2 (AnxA2). In addition to its various tasks as a cytoskeletal- and membrane-associated protein, AnxA2 can function as a -acting protein binding to -acting sequences of specific mRNAs. In the present study, we have examined the role of Ser25 phosphorylation in subcellular localisation of AnxA2 and its interaction with mRNP complexes. Subcellular fractionation and confocal microscopy of rat neuroendocrine PC12 cells showed that Ser25-phosphorylated AnxA2 (pSer25AnxA2) is absent from the nucleus and mainly localised to the perinuclear region, evidently associating with both membranes... More

关键词

Annexin A2,Ser phosphorylation,mRNP complexes,post‐translational modification,sumoylation,ubiquitina