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J. Biol. Chem., Vol. 276, Issue 18, 15458-15465, May 4, 2001
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From the Department of Physiology, University of Wisconsin,
Madison, Wisconsin 53706
Assembly of the plasma membrane proteins syntaxin
1A and SNAP-25 with the vesicle protein synaptobrevin
is a critical step in neuronal exocytosis. Syntaxin is anchored
to the inner face of presynaptic plasma membrane via a single
C-terminal membrane-spanning domain. Here we report that this
transmembrane domain plays a critical role in a wide range of syntaxin
protein-protein interactions. Truncations or deletions of the
membrane-spanning domain reduce synaptotagmin,
The Transmembrane Domain of Syntaxin 1A Is Critical for
Cytoplasmic Domain Protein-Protein Interactions*
/
-SNAP, and
synaptobrevin binding. In contrast, deletion of the transmembrane
domain potentiates SNAP-25 and rbSec1A/nsec-1/munc18 binding. Normal
partner protein binding activity of the isolated cytoplasmic domain
could be "rescued" by fusion to the transmembrane segments of
synaptobrevin and to a lesser extent, synaptotagmin. However,
efficient rescue was not achieved by replacing deleted transmembrane
segments with corresponding lengths of other hydrophobic amino acids.
Mutations reported to diminish the dimerization of the transmembrane
domain of syntaxin did not impair the interaction of full-length
syntaxin with other proteins. Finally, we observed that membrane
insertion and wild-type interactions with interacting proteins are not
correlated. We conclude that the transmembrane domain, via a
length-dependent and sequence-specific mechanism, affects
the ability of the cytoplasmic domain to engage other proteins.
*
This study was supported by Grant GM 56827-01 from the
National Institutes of Health, Grant 9750326N from the American Heart Association, and the Milwaukee Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
A Pew Scholar in the Biomedical Sciences. To whom correspondence
should be addressed: Dept. of Physiology, SMI 129, University of
Wisconsin, 1300 University Ave., Madison, WI 53706. Tel.: 608-263-1762; Fax: (608) 265-5512; E-mail: chapman@physiology.wisc.edu.
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