Myosin Is, which constitute a ubiquitous monomeric subclass of myosins with
actin-based motor properties, are associated with plasma membrane and intr
acellular vesicles. Myosin Is have been proposed as key players for membran
e trafficking in endocytosis or exocytosis. In the present paper we provide
biochemical and immunoelectron microscopic evidence indicating that a pool
of myosin I alpha (MMI alpha) is associated with endosomes and lysosomes.
We show that the overproduction of MMI alpha or the production of nonfuncti
onal truncated MMI alpha affects the distribution of the endocytic compartm
ents. We also show that truncated brush border myosin I proteins, myosin Is
that share 78% homology with MMI alpha, promote the dissociation of MMIa!
from vesicular membranes derived from endocytic compartments. The analysis
at the ultrastructural level of cells producing these brush border myosin I
truncated proteins shows that the delivery of the fluid phase markers from
endosomes to lysosomes is impaired. MMI alpha might therefore be involved
in membrane trafficking occurring between endosomes and lysosomes.