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J. Biol. Chem., Vol. 276, Issue 4, 2898-2904, January 26, 2001
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From the The Dictyostelium class I myosins,
MyoA, -B, -C, and -D, participate in plasma membrane-based
cellular processes such as pseudopod extension and
macropinocytosis. Given the existence of a high affinity
membrane-binding site in the C-terminal tail domain of these motor
proteins and their localized site of action at the cortical
membrane-cytoskeleton, it was of interest to determine whether each
myosin I was directly associated with the plasma membrane. The membrane
association of a myosin I heavy chain kinase that regulates the
activity of one of the class I myosins, MyoD was also examined.
Cellular fractionation experiments revealed that the majority of the
Dicyostelium MyoA, -B, -C and -D heavy chains and the
kinase are cytosolic. However, a small, but significant, fraction
(appr. 7. -15%) of each myosin I and the kinase was associated with
the plasma membrane. The level of plasma membrane-associated MyoB, but
neither that of MyoC nor MyoD, increases up to 2-fold in highly motile,
streaming cells. These results indicate that Dictyostelium
specifically recruits myoB to the plasma membrane during directed
cell migration, consistent with its known role in pseudopod formation.
Recruitment of a Specific Amoeboid Myosin I Isoform to the
Plasma Membrane in Chemotactic Dictyostelium
Cells*
§,
,**
Department of Cell Biology, Duke University
Medical Center, Durham, North Carolina 27710, the ¶ Department of
Biochemistry, Queens University, Kingston, Ontario, K7L 3N6 Canada, and
the ** Department of Genetics, Cell Biology and Development, University
of Minnesota, Minneapolis, Minnesota 55455
*
This work was supported by Canadian Institutes of Health
Research Grant MOP-8603 (to G. P. C.) and National
Institutes of Health Grant GM-46486 (to M. A. T.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Dept. of Pharmacology, University of Texas
Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75235-9041.
To whom all correspondence should be addressed: Depts. of
Genetics, Cell Biology and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church St., SE., Minneapolis, MN 55455. Tel.:
612-625-8498; Fax: 612-624-8118; E-mail:
titus@lenti.med.umn.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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