Biology Reference
In-Depth Information
12
Dynamin and Cytoskeletal-
dependent Membrane Processes
James D. Orth, Noah W. Gray, Heather M. Thompson
and
Mark A. McNiven
The mechanochemical GTPase dynamin functions to mediate vesicle
formation from several cellular compartments, including the plasma
membrane, endosomes and Golgi complex. Dynamin is a multidomain
protein that interacts with lipids and numerous additional proteins, including
actin-associated proteins such as cortactin. Thus, dynamin is likely to
participate in many cell functions that require actin-based membrane
dynamics. Indeed, multiple recent observations support the premise that
dynamin functions at the interface between cell membranes and the
cytoskeleton during membrane ru
ing, vesicle tra
cking, cytokinesis and
synaptogenesis. This chapter summarizes our recent findings supporting these
new roles for dynamin and proposes future directions that should provide
insight into the molecular basis of membrane dynamics.
Introduction
An overview of dynamin
Dynamin is a large, 100-kDa GTPase that was first discovered as a
microtubule-associated protein from bovine brain (Shpetner and Vallee,
1989). Upon cloning,
it was realized that dynamin was the mammalian
