Structural and functional analysis of mammalian sds22, a novel regulatory polypeptide of protein phosphatase 1
FP4 — Training and Mobility of Researchers
- Duration
- 1996-11-01 → 1997-10-31
- EU contribution
- —
- Participants
- 2
- Scheme
- RGI
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Project objective
During my stay in Belgium from July 1993 onwards, I have been able to clone the mammalian homolog of SDS22, which was previously identified in Schizosaccharomyces pombe as a positive regulator of protein phosphatase-1. Our results have furthermore shown a high structural conservation of SDS22, a broad subcellular and tissue distribution, and a physical association with the catalytic subunit of protein phosphatase-l. My future research in Rouen will mainly focus on the function and regulation of the phosphatase that contains SDS22 as a subunit. To this end, the latter phosphatase will be purified by affinity chromatography on SDS22 antibody-.Sepharose and its substrate speci- ficity will be studied. I will also investigate the potential role. Of phosphorylation of SDS22 by various protein kinases. Using recombinant SDS22, phosphorylation sites will be mapped and the interaction of SDS22 with the type-l catalytic subunit will be further analysed. Finally, the expected role of SDS22 in cell division and in the cell cycle will be investigated in fibroblasts and in Xenopus oocytes overexpressing SDS22.
Original text from CORDIS.
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