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The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
It has been proposed that the carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein. This protein has been purified from tissues and named telokin (Ito, M., Dabrowska, R., Guerriero, V., Jr., and Hartshorne, D. J. (1989) J. Biol. Chem. 264, 13971-139...
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Published in: | The Journal of biological chemistry 1991-12, Vol.266 (35), p.23945-23952 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | It has been proposed that the carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent
protein. This protein has been purified from tissues and named telokin (Ito, M., Dabrowska, R., Guerriero, V., Jr., and Hartshorne,
D. J. (1989) J. Biol. Chem. 264, 13971-13974). In this study we have isolated and characterized cDNA and genomic clones encoding
telokin. Analysis of a genomic DNA clone suggests that the mRNA encoding telokin arises from a promoter which appears to be
located within an intron of the smooth muscle myosin light chain kinase (MLCK) gene. This intron interrupts exons encoding
the calmodulin binding domain of the kinase. The amino acid sequence deduced from the cDNA predicts that telokin is identical
to the carboxyl-terminal 155 residues of the smooth muscle MLCK. Unlike the smooth muscle MLCK which is expressed in both
smooth and non-muscle tissues, telokin is expressed in some smooth muscle tissues but has not been detected in aortic smooth
muscle or in any non-muscle tissues. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/s0021-9258(18)54376-3 |