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The Journal of Neuroscience, March 15, 1999, 19(6):1998-2007
Metabolic Stabilization of Muscle Nicotinic Acetylcholine
Receptor by Rapsyn
Zuo-Zhong
Wang1,
Askale
Mathias1,
Medha
Gautam2, and
Zach W.
Hall1
1 Laboratory of Cell Biology, National Institute of
Mental Health, National Institutes of Health, Bethesda, Maryland 20892, and 2 Department of Pharmacological and Physiological
Science, St. Louis University Medical School, St. Louis, Missouri
63104
Although the metabolic half-life of muscle endplate acetylcholine
receptor (AChR) changes during development and after denervation in the
adult, little is known about the molecular mechanisms that influence
receptor stability. We have investigated the effect on AChR turnover of
its interaction with rapsyn, a 43 kDa peripheral membrane protein that
is closely associated with the AChR in muscle cells and is required for
its clustering at endplates. Both in transfected COS cells and in
cultured myotubes from rapsyn-negative and rapsyn-positive mice, we
have found that the presence of rapsyn slows the turnover of AChRs by
as much as twofold. The effect was similar for both embryonic
( 2   ) and adult (2 ) AChRs and for AChRs whose subunit lacked a putative tyrosine
phosphorylation site. Neither colchicine nor cytochalasin D altered
AChR turnover or prevented the rapsyn effect. Mutant rapsyn proteins
whose N-terminal myristoylation signal was eliminated, or whose C
terminus or zinc-finger domains were deleted, failed to change the rate
of receptor turnover. Each of these mutations affects the association
of the AChR with rapsyn, suggesting that AChR stability is altered by
interaction between the two proteins. Our results suggest that, in
addition to its role in AChR clustering, rapsyn also functions to
metabolically stabilize the AChR.
Key words:
nicotinic receptors; rapsyn; 43 kDa protein; receptor
turnover; acetylcholine; neuromuscular junction; endplate; myotubes
Copyright © 1999 Society for Neuroscience 0270-6474/99/1961998-10$05.00/0
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