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Dephosphorylation of cytoplasmic non-polysomal messenger ribonucleoproteins from cryptobiotic gastrulae of Artemia salina
Van Hove, L.; Thoen, C.; Cohen, P.; Slegers, H. (1985). Dephosphorylation of cytoplasmic non-polysomal messenger ribonucleoproteins from cryptobiotic gastrulae of Artemia salina. Biochem. Biophys. Res. Commun. 131(3): 1241-1250. dx.doi.org/10.1016/0006-291X(85)90224-4
In: Biochemical and Biophysical Research Communications. ACADEMIC PRESS INC ELSEVIER SCIENCE: San Diego etc.. ISSN 0006-291X, more
Peer reviewed article  

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  • Van Hove, L.
  • Thoen, C.
  • Cohen, P.
  • Slegers, H.

Abstract
    Cytoplasmic non-polysomal mRNP from cryptobiotic gastrulae of the brine shrimp Artemiasalina do not contain endogeneous protein phosphatase activity. However, both non-polysomal mRNP and purified mRNP proteins, phosphorylated by mRNP associated protein kinase, can be dephosphorylated by protein phosphatases purified from A. salina cytosol and rabbit skeletal muscle. The 38kDa and 23.5kDa poly(A) binding proteins (P38 and P23.5) and a 65kDa protein are the major substrates of each protein phosphatase used. The reversible phosphorylation-dephosphorylation of mRNP may be involved in the regulation of mRNP metabolism, by altering the poly(A) binding capacities of the mRNP proteins.

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