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Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M
Author(s) -
Chen Yu Hua,
Chen Mao Xiang,
Alessi Dario R.,
Campbell David G.,
Shanahan Catherine,
Cohen Philip,
Cohen Patricia T.W.
Publication year - 1994
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 - 10.1016/0014-5793(94)01231-8
Subject(s) - protein subunit , leucine zipper , myosin light chain phosphatase , complementary dna , microbiology and biotechnology , ankyrin , biology , molecular cloning , biochemistry , myosin , peptide sequence , chemistry , gene
The structures of the M 110 and M 21 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 M 110 subunit from rat aorta contains seven ankyrin repeats, while the C‐terminus of the M 21 subunit from chicken gizzard contains a leucine zipper motif. The M 110 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 M 21 subunit.