CaltechAUTHORS
  A Caltech Library Service

Phosphorylation of smooth muscle myosin by type II Ca^(2+)/calmodulin-dependent protein kinase.

Edelman, Arthur M. and Lin, Wei-Hsung and Osterhout, Donna J. and Bennett, Mark K. and Kennedy, Mary B. and Krebs, Edwin G. (1990) Phosphorylation of smooth muscle myosin by type II Ca^(2+)/calmodulin-dependent protein kinase. Molecular and cellular biochemistry, 97 (1). pp. 87-98. ISSN 0300-8177. http://resolver.caltech.edu/CaltechAUTHORS:20120424-154231046

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:20120424-154231046

Abstract

Brain type II Ca^(2+)/calmodulin-dependent protein kinase was found to phosphorylate smooth muscle myosin, incorporating maximally ~ 2 mol of phosphoryl per mol of myosin, exclusively on the 20,000 dalton light chain subunit. After maximal phosphorylation of myosin or the isolated 20,000 dalton light chain subunit by myosin light chain kinase, the addition of type II Ca^(2+)/calmodulin-dependent protein kinase led to no further incorporation indicating the two kinases phosphorylated a common site. This conclusion was supported by two dimensional mapping of tryptic digests of myosin phosphorylated by the two kinases. By phosphoamino acid analysis the phosphorylated residue was identified as a serine. The phosphorylation by type II Ca^(2+)/calmodulin-dependent protein kinase of myosin resulted in enhancement of its actin-activated Mg^(2+)-ATPase activity. Taken together, these data strongly support the conclusion that type II Ca^(2+)/calmodulin-dependent protein kinase phosphorylates the same amino acid residue on the 20,000 dalton light chain subunit of smooth muscle myosin as is phosphorylated by myosin light chain kinase and suggest an alternative mechanism for the regulation of actin-myosin interaction.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1007/BF00231704DOIUNSPECIFIED
http://www.springerlink.com/content/v850th4503931117/PublisherUNSPECIFIED
Additional Information:© 1990 Kluwer Academic Publisher. Received 19 October 1989; accepted 26 January 1990. We are grateful to Rob Saeli, Floyd Kennedy and Barbara Flug for technical assistance, Tecla Atkinson for illustrations, and Gerry Richtand for typing the manuscript. We also wish to thank Karen Polak for performing some of the phosphorylations of myosin. This work has been partially supported by GM 07145 and NS 24738 and by BNS 8617110 (NSF).
Funders:
Funding AgencyGrant Number
NSFGM 07145
NSFNS 24738
NSF8617110
Subject Keywords:myosin; calcium; calmodulin; type II kinase
Record Number:CaltechAUTHORS:20120424-154231046
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20120424-154231046
Official Citation:Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinase Arthur M. Edelman, Wei-Hsung Lin, Donna J. Osterhout, Mark K. Bennett and Mary B. Kennedy, et al.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:30336
Collection:CaltechAUTHORS
Deposited By: Melanie Stefan
Deposited On:25 Apr 2012 20:02
Last Modified:25 Apr 2012 20:02

Repository Staff Only: item control page