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Truncated Brush Border Myosin I Affects Membrane Traffic in Polarized Epithelial Cells
Author(s) -
Durrbach A.,
Raposo G.,
Tenza D.,
Louvard D.,
Coudrier E.
Publication year - 2000
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2000.010506.x
Subject(s) - endocytosis , endocytic cycle , microbiology and biotechnology , endosome , biology , myosin , actin , epithelial polarity , apical membrane , brush border , exocytosis , cell polarity , cell membrane , biophysics , membrane , cell , biochemistry , vesicle , intracellular
We investigate, in this study, the potential involvement of an acto‐myosin‐driven mechanism in endocytosis of polarized cells. We observed that depolymerization of actin filaments using latrunculin A decreases the rate of transferrin recycling to the basolateral plasma membrane of Caco‐2 cells, and increases its delivery to the apical plasma membrane. To analyze whether a myosin was involved in endocytosis, we produced, in this polarized cell line, truncated, non‐functional, brush border, myosin I proteins (BBMI) that we have previously demonstrated to have a dominant negative effect on endocytosis of unpolarized cells. These non‐functional proteins affect the rate of transferrin recycling and the rate of transepithelial transport of dipeptidyl‐peptidase IV from the basolateral plasma membrane to the apical plasma membrane. They modify the distribution of internalized endocytic tracers in apical multivesicular endosomes that are accessible to fluid phase tracers internalized from apical and basolateral plasma membrane domains. Altogether, these observations suggest that an acto‐myosin‐driven mechanism is involved in the trafficking of basolaterally internalized molecules to the apical plasma membrane.