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Lamellipodial localization of Dictyostelium myosin heavy chain kinase A is mediated via F‐actin binding by the coiled‐coil domain
Author(s) -
Steimle Paul A,
Licate Lucila,
Côté Graham P,
Egelhoff Thomas T
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02494-8
Subject(s) - myosin , dictyostelium , coiled coil , actin , dictyostelium discoideum , myosin light chain kinase , microbiology and biotechnology , pseudopodia , actin binding protein , biology , actin remodeling , chemotaxis , cytoskeleton , actin cytoskeleton , biochemistry , receptor , cell , gene
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.