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J. Biol. Chem., Vol. 275, Issue 41, 31986-31995, October 13, 2000
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From the Department of Anatomy and Neurobiology and
¶ Department of Pediatrics, Washington University Medical
School, St. Louis, Missouri 63110
We describe a novel protein, Syne-1, that is
associated with nuclear envelopes in skeletal, cardiac, and smooth
muscle cells. Syne-1 contains multiple spectrin repeats similar to
those found in dystrophin and utrophin, as well as a domain homologous
to the carboxyl-terminal of Klarsicht, a protein associated with nuclei
and required for a subset of nuclear migrations in
Drosophila. In adult skeletal muscle fibers, levels of
Syne-1 are highest in the nuclei that lie beneath the postsynaptic
membrane at the neuromuscular junction. These nuclei are
transcriptionally specialized, expressing genes for synaptic components
at higher levels than extrasynaptic nuclei in the same cytoplasm.
Syne-1 is the first protein found to be selectively associated with
synaptic nuclei. Syne-1 becomes concentrated in synaptic nuclei
postnatally. It remains synaptically enriched following denervation or
degeneration/regeneration, and is also present at high levels in the
central nuclei of dystrophic myotubes. The location and structure of
Syne-1 suggest that it may participate in the migration of myonuclei in
myotubes and/or their anchoring at the postsynaptic apparatus. Finally,
we identify a homologous gene, syne-2, that is expressed in
an overlapping but distinct pattern.
Syne-1, A Dystrophin- and Klarsicht-related Protein
Associated with Synaptic Nuclei at the Neuromuscular Junction*
§,,¶, and
*
This work was supported by grants from National Institutes
of Health (to J. R. S.), Muscular Dystrophy
Association (to J. R. S. and R. M. G.), and
the McDonnell Center for Cellular Neurosciences at Washington
University (to E. D. A.).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.
Contributed equally to the results of this work.
§
Present address: ICOS Corp., 22021 20th Ave., S.E., Bothwell, WA 98021.
To whom correspondence should be addressed: Dept. of Anatomy
and Neurobiology, Washington University Medical School, 660 S. Euclid
Ave., St. Louis, MO 63110. Tel.: 314-362-2507; Fax: 314-747-1150; E-mail: sanesj@pcg.wustl.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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