Lamellipodial localization of Dictyostelium myosin heavy chain kinase A is mediated via F-actin binding by the coiled-coil domain

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) modulates myosin II filament assembly in the amoeba Dictyostelium discoideum. MHCK A localization in vivo is dynamically regulated during chemotaxis, phagocytosis, and other polarized cell motility events, with preferential recruitment into anterior filamentous actin (F-actin)-rich structures. The current work reveals that an amino-terminal segment of MHCK A, previously identified as forming a coiled-coil, mediates anterior localization. MHCK A co-sediments with F-actin, and deletion of the amino-terminal domain eliminated actin binding. These results indicate that the anterior localization of MHCK A is mediated via direct binding to F-actin, and reveal the presence of an actin-binding function not previously detected by primary sequence evaluation of the coiled-coil domain.

Additional Information

FEBS Letters, April 10, 516:58-62
Language: English
Date: 2002
Myosin, Actin, Phosphorylation, Chemotaxis

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