DMCA
Metabolic stabilization of muscle nicotinic acetylcholine receptor by rapsyn (1999)
| Venue: | J Neurosci |
| Citations: | 8 - 0 self |
BibTeX
@ARTICLE{Wang99metabolicstabilization,
author = {Zuo-zhong Wang and Askale Mathias and Medha Gautam and Zach W. Hall},
title = {Metabolic stabilization of muscle nicotinic acetylcholine receptor by rapsyn},
journal = {J Neurosci},
year = {1999},
pages = {1998--2007}
}
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Abstract
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
Keyphrases
muscle nicotinic acetylcholine receptor metabolic stabilization achr turnover kda peripheral membrane protein receptor stability muscle endplate acetylcholine receptor putative tyrosine phosphorylation site co cell mutant rapsyn rapsyn effect molecular mechanism metabolic half-life muscle cell cultured myotubes rapsyn-positive mouse
