Recruitment of a Specific Amoeboid Myosin I Isoform to the Plasma Membrane in Chemotactic Dictyostelium Cells

Shunji Senda, Sheu Fen Lee, Graham P. Côté, Margaret A Titus

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2898-2904
Number of pages7
JournalJournal of Biological Chemistry
Volume276
Issue number4
DOIs
StatePublished - Jan 26 2001

Bibliographical note

Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.

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