Document Title

Myosin Light Chain Kinase (MLCK) Gene Disruption in Dictyostelium: A Role for MLCK-A in Cytokinesis and Evidence for Multiple MLCKs

Department/School

Biology

Abstract

We have created a strain of Dictyostelium that is deficient for the Ca2+/calmodulin-independent MLCK-A. This strain undergoes cytokinesis less efficiently than wild type, which results in an increased frequency of multinucleate cells when grown in suspension. The MLCK-A-cells are able, however, to undergo development and to cap crosslinked surface receptors, processes that require myosin heavy chain. Phosphorylated regulatory light chain (RLC) is still present in MLCK-A-cells, indicating that Dictyostelium has one or more additional protein kinases capable of phosphorylating RLC. Concanavalin A treatment was found to induce phosphorylation of essentially all of the RLC in wild-type cells, but RLC phosphorylation levels in MLCK-A-cells are unaffected by concanavalin A. Thus MLCK-A is regulated separately from the other MLCK(s) in the cell.

Document Type

Article

Publication Title

Proceedings of the National Academy of Sciences of the United States of America

Publication Date

10-29-1996

Volume

93

Issue

22

Pages

12321-12326

Digital Object Identifier (DOI)

10.1073/pnas.93.22.12321

PubMed ID (PMID)

8901579

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