ArticleThe Journal of cell biology1993
Clustering of the acetylcholine receptor by the 43-kD protein: involvement of the zinc finger domain.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 45 citations in OpenAlex.
- Protein networking: nicotinic acetylcholine receptors and their protein-protein-associations.Molecular and cellular biochemistry · 2024Review
- Rapsyn carboxyl terminal domains mediate muscle specific kinase-induced phosphorylation of the muscle acetylcholine receptor.Neuroscience · 2008Article
- The Zebrafish motility mutant twitch once reveals new roles for rapsyn in synaptic function.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
- The actin-driven movement and formation of acetylcholine receptor clusters.The Journal of cell biology · 2000Article
- Metabolic stabilization of muscle nicotinic acetylcholine receptor by rapsyn.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- Identification of DNA recognition sequences and protein interaction domains of the multiple-Zn-finger protein Roaz.Molecular and cellular biology · 1998Article
- Mechanism of nicotinic acetylcholine receptor cluster formation by rapsyn.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- To muster a cluster: anchoring neurotransmitter receptors at synapses.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Laminin and alpha-dystroglycan mediate acetylcholine receptor aggregation via a MuSK-independent pathway.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole.Molecular biology of the cell · 1997Article
- Chick ciliary ganglion neurons contain transcripts coding for acetylcholine receptor-associated protein at synapses (rapsyn).The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997Article
- Zinc-binding and protein-protein interactions mediated by the polyomavirus large T antigen zinc finger.Journal of virology · 1995Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A postsynaptic membrane-associated protein of M(r) 43,000 (43-kD protein) is involved in clustering of the nicotinic acetylcholine receptor (AChR) at the neuromuscular junction. Previous studies have shown that recombinant mouse 43-kD protein forms membrane-associated clusters when expressed in Xenopus oocytes. Coexpression with the AChR results in colocalization of the receptor with the 43-kD protein clusters (Froehner, S. C., C. W. Luetje, P. B. Scotland, and J. Patrick, 1990. Neuron. 5:403-410). To understand the mechanism of this clustering, we have studied the role of the carboxy-terminal region of the 43-kD protein. The amino acid sequence of this region predicts two tandem zinc finger structures followed by a serine phosphorylation site. Both Torpedo 43-kD protein and the carboxy-terminal region of the mouse 43-kD protein bind radioisotopic zinc. Mutation of two histidine residues in this predicted domain greatly attenuates zinc binding, lending support to the proposal that this region forms zinc fingers. When expressed in oocytes, the ability of this mutant 43-kD protein to form clusters is greatly reduced. Its ability to interact with AChR, however, is retained. In contrast, a mutation that eliminates the potential serine phosphorylation site has no effect on clustering of the 43-kD protein or on interaction with the AChR. These findings suggest that protein interactions via the zinc finger domain of the 43-kD protein may be important for AChR clustering at the synapse.
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