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J Biol Chem, Vol. 274, Issue 28, 19771-19777, July 9, 1999
From the Graduate Program in Neuroscience, Department of
Psychiatry, University of British Columbia, Vancouver,
British Columbia V6T 1Z3, Canada
We have identified a novel protein (BERP) that is
a specific partner for the tail domain of myosin V. Class V myosins are a family of molecular motors thought to interact via their unique C-terminal tails with specific proteins for the targeted transport of
organelles. BERP is highly expressed in brain and contains an
N-terminal RING finger, followed by a B-box
zinc finger, a coiled-coil (RBCC domain), and a
unique C-terminal
Cloning and Characterization of a Novel RING Finger Protein That
Interacts with Class V Myosins
-propeller domain. A yeast two-hybrid screening
indicated that the C-terminal -propeller domain mediates binding to
the tail of the class V myosin myr6 (myosin Vb). This interaction was
confirmed by immunoprecipitation, which also demonstrated that BERP
could associate with myosin Va, the product of the dilute
gene. Like myosin Va, BERP is expressed in a punctate pattern in the
cytoplasm as well as in the neurites and growth cones of PC12 cells. We
also found that the RBCC domain of BERP is involved in protein
dimerization. Stable expression of a mutant form of BERP lacking the
myosin-binding domain but containing the dimerization domain resulted
in defective PC12 cell spreading and prevented neurite outgrowth in
response to nerve growth factor. Our studies present a novel
interaction for the -propeller domain and provide evidence for a
role for BERP in myosin V-mediated cargo transport.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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