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W. Dale Branton, Ph.D.
Associate Professor, Department of Neuroscience
branton@umn.edu |
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The Molecular Basis of Synaptic Transmission
Our laboratory is interested in cellular and molecular aspects
of physiological regulatory mechanisms. Research emphasizes synaptic
transmission and signaling mechanisms that involve calcium. Our
studies span a range of technical approaches in the tradition of
neuroscience. One line of research in the laboratory involves characterization
of unique biological toxins that may be useful in elucidating new
biological mechanisms. We have focused on a class of toxins that
either suppress or prolong synaptic transmission. They act by affecting
the function of calcium channels and perhaps by affecting other
types of ion channels as well. We have shown that these toxins are
small proteins that are palmitoylated on the hydroxyl side chain
of a C-terminal amino acid. This unique proteolipid structure has
special physical properties and we are intrigued by the similarity
between the palmitoylated C-terminal of these toxins and the acylated
C-terminal regions of biological regulatory proteins including small
GTP binding proteins. Other interests include molecular studies,
in collaboration with Robert F. Miller, of calcium channels in retina.
We have also been involved in studies of ADP-ribosyl cyclases and
hydrolases, enzymes that make and degrade cyclic ADP-ribose. Cyclic
ADP-ribose is a key regulator of intracellular calcium levels that
was discovered by a departmental colleague, Hon Cheung Lee.
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Selected Publications
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Munshi CB, Fryxell KB, Lee HC, Branton
WD
Large-scale production of human CD38 in yeast by fermentation.
Methods
Enzymol 1997;280:318-30 |
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Bodi, J., H. Nishio, Y. Zhou, W.D. Branton, T. Kimura
and S. Sakakibar
Synthesis of an O-Palmitoylated 44-residue peptide amide (PLTXII)
blocking presynaptic calcium channels in Drosophila.
Peptide
Res 1995;8(4):228-235 |
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Branton, W.D., Y. Zhou, C.G. Fields and G.B. Fields
Synthetic approaches for the structural characterization of a novel
family of proteolipid spider toxins.
In Peptides: Chemistry, Structure and Biology. 1995. Edited
by P.T.P. Kaumaya and R.S. Hodges. Leiden, the Netherlands:
Escom |
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Fryxell, K.B., K.J. O'Donoghue, R.M. Graeff, H.C. Lee
and W.D. Branton
Functional expression of soluble forms of human CD38 in E. coli and
pichia pastoris.
Protein
Expr Purif 1995;6:329-336 |
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