Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M.
The structures of the M110 and M21 regulatory subunits of protein phosphatase-1M, the major enzyme which dephosphorylates myosin in smooth muscle, have been deduced from cloned cDNAs. The N-terminus of the M110 subunit from rat aorta contains seven ankyrin repeats, while the C-terminus of the M21 subunit from chicken gizzard contains a leucine zipper motif. The M110 subunit is expressed in two different forms which differ in their C-terminal sequences. One of these is highly homologous to the whole of the M21 subunit.
Chen
Y H
YH
Department of Biochemistry, University of Dundee, Scotland, UK.
Chen
M X
MX
Alessi
D R
DR
Campbell
D G
DG
Shanahan
C
C
Cohen
P
P
Cohen
P T
PT
D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta; D002645:Chickens; D003001:Cloning, Molecular; D018076:DNA, Complementary; D005895:Gizzard, Avian; D016350:Leucine Zippers / Q000235:genetics; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000235:genetics*; D051381:Rats; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D010749:Phosphoprotein Phosphatases