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PPP1R6, a novel member of the family of glycogen‐targetting subunits of protein phosphatase 1
Author(s) -
Armstrong Christopher G,
Browne Gareth J,
Cohen Philip,
Cohen Patricia T.W
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01385-9
Subject(s) - protein subunit , glycogen , skeletal muscle , glycogen debranching enzyme , glycogen synthase , biology , allosteric regulation , phosphatase , protein phosphatase 2 , biochemistry , protein phosphatase 1 , glycogen branching enzyme , microbiology and biotechnology , enzyme , gene , anatomy
A complementary DNA encoding a novel human protein phosphatase 1 (PP1) glycogen‐targetting subunit of molecular mass 33 kDa has been sequenced. PPP1R6 is 31% identical to the glycogen‐targetting subunit (G L ) of PP1 from rat liver, 28% identical to the N‐terminal region of the glycogen‐targetting subunit (G M ) from human skeletal muscle and 27% identical to glycogen‐targetting subunit PPP1R5. Unlike human PPP1R5 and its murine homologue PTG, whose mRNAs are most abundant in skeletal muscle, heart and liver, PPP1R6 is present at similar levels in a wide variety of tissues. The PPP1R6 is associated with glycogen in muscle but is not subject to the same modes of covalent and allosteric regulation as G M and G L .