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J. Biol. Chem., Vol. 269, Issue 48, 30132-30139, 12, 1994
PS McPherson, K Takei, SL Schmid and P De Camilli
Three major rat brain proteins were recently found to bind the SH3 domains
of Grb2: synapsin I, dynamin, and a novel 145-kDa protein (p145)
(McPherson, P. S., Czernik, A. J., Chilcote, T. J., Onofri, F., Benfenati,
F., Greengard, P., Schlessinger, J., and De Camilli, P. (1994) Proc. Natl.
Acad. Sci. U.S.A. 91, 6486-6490). We have now used antibodies raised
against p145 which had been purified by Grb2 affinity chromatography and
SDS-polyacrylamide gel electrophoresis to characterize this protein. p145
is neuron-specific and co-distributes with dynamin in subcellular fractions
of rat brain. Both proteins are partially recovered in soluble and
particulate fractions. By immunofluorescence, p145 is closely co-localized
with dynamin, which we show here to be highly concentrated in nerve
terminals. In contrast to synapsin I, which is highly enriched in a
purified synaptic vesicle fraction, both p145 and dynamin are de-enriched
in this fraction. However, both proteins are found on membranes which are
immunoisolated with antibodies directed against the synaptic vesicle
membrane protein synaptophysin, suggesting that dynamin and p145 are
localized in part on organelles which represent intermediate stages in the
reformation of synapatic vesicles during recycling. Finally, we have
determined that p145, like dynamin, is a phosphoprotein which undergoes
dephosphorylation in response to nerve terminal depolarization. These
findings suggest that p145 participates with dynamin in synaptic vesicle
endocytosis and recycling.
p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
Department of Cell Biology, Howard Hughes Medical Research Institute, Yale University School of Medicine, New Haven, Connecticut 06510.
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