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

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 a...

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Bibliographic Details
Published in:FEBS letters 2002-04, Vol.516 (1), p.58-62
Main Authors: Steimle, Paul A, Licate, Lucila, Côté, Graham P, Egelhoff, Thomas T
Format: Article
Language:English
Subjects:
Actin
Actins - metabolism
Animals
Binding Sites
Calcium-Calmodulin-Dependent Protein Kinases - chemistry
Calcium-Calmodulin-Dependent Protein Kinases - metabolism
Cell Polarity
Chemotaxis
Dictyostelium - cytology
Dictyostelium - enzymology
Dictyostelium - genetics
Dictyostelium - physiology
In Vitro Techniques
Myosin
Myosin Type II - metabolism
Phosphorylation
Protein Structure, Tertiary
Protozoan Proteins
Pseudopodia - enzymology
Pseudopodia - physiology
Rabbits
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)02494-8