Cloning and characterization of mammalian myosin regulatory light chain (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues

doi:10.1083/jcb.104.6.1505

This Article

	Full Text (PDF, 1623K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Taubman, M. B.
	Articles by Nadal-Ginard, B.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Taubman, M. B.
	Articles by Nadal-Ginard, B.


Social Bookmarking

	What's this?

ARTICLES

Cloning and characterization of mammalian myosin regulatory light chain (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues

MB Taubman, JW Grant and B Nadal-Ginard

The 20-kD regulatory light chain (RLC) plays a central role in the regulation of smooth muscle contraction. Little is known about the structure or expression of smooth muscle myosin light chain (MLC) genes. A cDNA library was constructed in the expression vector, lambda gt-11, with mRNA derived from cultured rat aortic smooth muscle cells. Using antibody generated against tracheal smooth muscle myosin, three cDNA clones encoding a RLC were isolated, one of which, SmRLC-2, represents a full-length transcript of the RLC mRNA. The derived amino acid sequence shows 94.2% homology with the chicken gizzard RLC, and 70 and 52% homology with the rat skeletal and cardiac muscle MLC-2 proteins, respectively. Thus, the gene encoding the putative smooth muscle RLC appears to have originated by duplication of the same ancestor that gave rise to the sarcomeric MLC-2 genes. Contrary to the stringent tissue-specific expression of sarcomeric MLC-2 genes, RNA blot hybridization and S1 nuclease mapping demonstrates that the putative smooth muscle RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues at significant levels. Primer extension analysis suggests that the same promoter region is used in these different tissues. Thus the putative smooth muscle RLC gene appears to be a gene that is constitutively expressed in a large variety of cells and has a differentiated function in smooth muscle.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Bajaj, G., Zhang, Y., Schimerlik, M. I., Hau, A. M., Yang, J., Filtz, T. M., Kioussi, C., Ishmael, J. E. (2009). N-Methyl-D-aspartate Receptor Subunits Are Non-myosin Targets of Myosin Regulatory Light Chain. J. Biol. Chem. 284: 1252-1266 [Abstract] [Full Text]
Eddinger, T. J., Meer, D. P. (2007). Myosin II isoforms in smooth muscle: heterogeneity and function. Am. J. Physiol. Cell Physiol. 293: C493-C508 [Abstract] [Full Text]
Royou, A., Sullivan, W., Karess, R. (2002). Cortical recruitment of nonmuscle myosin II in early syncytial Drosophila embryos: its role in nuclear axial expansion and its regulation by Cdc2 activity. JCB 158: 127-137 [Abstract] [Full Text]
Cavusoglu, E., Chen, I., Rappaport, J., Marmur, J. D. (2002). Inhibition of Tissue Factor Gene Induction and Activity Using a Hairpin Ribozyme. Circulation 105: 2282-2287 [Abstract] [Full Text]
Parisi, J. A., Eddinger, T. J. (2002). Smooth Muscle Myosin Heavy Chain Isoform Distribution in the Swine Stomach. J. Histochem. Cytochem. 50: 385-394 [Abstract] [Full Text]
Eddinger, T. J., Meer, D. P. (2001). Single rabbit stomach smooth muscle cell myosin heavy chain SMB expression and shortening velocity. Am. J. Physiol. Cell Physiol. 280: C309-C316 [Abstract] [Full Text]
Olsson, P.-A., Korhonen, L., Mercer, E. A., Lindholm, D. (1999). MIR Is a Novel ERM-like Protein That Interacts with Myosin Regulatory Light Chain and Inhibits Neurite Outgrowth. J. Biol. Chem. 274: 36288-36292 [Abstract] [Full Text]
Sakurada, K., Seto, M., Sasaki, Y. (1998). Dynamics of myosin light chain phosphorylation at Ser19 and Thr18/Ser19 in smooth muscle cells in culture. Am. J. Physiol. Cell Physiol. 274: C1563-C1572 [Abstract] [Full Text]
Yoshioka, K., Matsumura, F., Akedo, H., Itoh, K. (1998). Small GTP-binding Protein Rho Stimulates the Actomyosin System, Leading to Invasion of Tumor Cells. J. Biol. Chem. 273: 5146-5154 [Abstract] [Full Text]
Jordan, P., Karess, R. (1997). Myosin Light Chain-activating Phosphorylation Sites Are Required for Oogenesis in Drosophila. JCB 139: 1805-1819 [Abstract] [Full Text]
Samaha, F. F., Ip, H. S., Morrisey, E. E., Seltzer, J., Tang, Z., Solway, J., Parmacek, M. S. (1996). Developmental Pattern of Expression and Genomic Organization of the Calponin-h1 Gene. J. Biol. Chem. 271: 395-403 [Abstract] [Full Text]
Solway, J., Seltzer, J., Samaha, F. F., Kim, S., Alger, L. E., Niu, Q., Morrisey, E. E., Ip, H. S., Parmacek, M. S. (1995). Structure and Expression of a Smooth Muscle Cell-specific Gene, SM22[IMAGE]. J. Biol. Chem. 270: 13460-13469 [Abstract] [Full Text]
Shimizu, R. T., Blank, R. S., Jervis, R., Lawrenz-Smith, S. C., Owens, G. K. (1995). The Smooth Muscle alpha-Actin Gene Promoter Is Differentially Regulated in Smooth Muscle versus Non-smooth Muscle Cells. J. Biol. Chem. 270: 7631-7643 [Abstract] [Full Text]