Dephosphorylation of cytoplasmic non-polysomal messenger ribonucleoproteins from cryptobiotic gastrulae of Artemia salina

Lauris Van Hove, Chris Thoen, Philip Cohen, Herman Slegers

    Research output: Contribution to journalArticle

    10 Citations (Scopus)

    Abstract

    Cytoplasmic non-polysomal mRNP from cryptobiotic gastrulae of the brine shrimp Artemia salina 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.

    Original languageEnglish
    Pages (from-to)1241-1250
    Number of pages10
    JournalBiochemical and Biophysical Research Communications
    Volume131
    Issue number3
    DOIs
    Publication statusPublished - 30 Sep 1985

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