Myosin heavy chain kinase A from Dictyostelium possesses a novel actin binding domain that cross-links actin filaments

UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
Paul A. Steimle, Assistant Professor (Creator)
The University of North Carolina at Greensboro (UNCG )
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Abstract: Myosin heavy-chain kinase A (MHCK A) catalyses the disassembly of myosin II filaments in Dictyostelium cells via myosin II heavy-chain phosphorylation. MHCK A possesses a ‘coiled-coil’-enriched domain that mediates the oligomerization, cellular localization and actin-binding activities of the kinase. F-actin (filamentous actin) binding by the coiled-coil domain leads to a 40-fold increase in MHCK A activity. In the present study we examined the actin-binding characteristics of the coiled-coil domain as a means of identifying mechanisms by which MHCK A-mediated disassembly of myosin II filaments can be regulated in the cell.

Additional Information

Biochemical Journal. April 15, 395(2):373-382
Language: English
Date: 2006
actin-binding domain, cross-linking, Dictyostelium, filamentous actin (F-actin), myosin II, myosin heavy-chain kinase (MHCK)

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