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Do unconventional myosins exert functions in dynamics of membrane compartments?
Author(s) -
Coudrier Evelyne,
Durrbach Antoine,
Louvard Daniel
Publication year - 1992
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 - 10.1016/0014-5793(92)80907-x
Subject(s) - microbiology and biotechnology , myosin , actin , intracellular , vesicle , biology , biophysics , vesicular transport protein , membrane , chemistry , biochemistry
Unconventional myosins have now been identified in amoeba as well as in higher eucaryotic cells. Their cellular localization, their ability to bind membrane vesicles and their ability to produce in vitro movement suggest that they can generate forces on the plasma membrane relative to actin filaments as well as on membrane compartments relative to actin. Genetic approaches and biochemical analysis of cells over‐producing nonfunctional domains of unconventional myosins have provided direct evidence for a role of unconventional myosins in movement of intracellular vesicles and have allowed us to formulate hypotheses about the possible mechanisms by which unconventional myosins could participate in the intracellular transport of membrane proteins and secretary proteins.