G. Moorhead et al., THE MAJOR MYOSIN PHOSPHATASE IN SKELETAL-MUSCLE IS A COMPLEX BETWEEN THE BETA-ISOFORM OF PROTEIN PHOSPHATASE-1 AND THE MYPT2 GENE-PRODUCT, FEBS letters, 438(3), 1998, pp. 141-144
Myosin is dephosphorylated by distinct forms of protein phosphatase 1
(PP1) in smooth muscle and skeletal muscle that are composed of PPI co
mplexed to different regulatory subunits, The smooth muscle myosin pho
sphatase (smPP1M) has been characterised previously and is composed of
PP1 beta complexed to M-110 and M-21 subunits that enhance the dephos
phorylation of smooth muscle myosin, but not skeletal muscle myosin. I
n contrast, the regulatory subunit(s) of skeletal muscle myosin phosph
atase (skPP1M) greatly enhance(s) the dephosphorylation of skeletal mu
scle myosin. Here me identify a regulatory subunit of skPP1M as the pr
oduct of the MYPT2 gene, a protein whose sequence is 61% identical to
the M-110 subunit of smPP1M, Surprisingly, the M-21 subunit of smPP1M
appears to be produced from the same gene that encodes MYPT2. (C) 1998
Federation of European Biochemical Societies.