The 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin

Research output: Contribution to journalArticle

Abstract

Postsynaptic peripheral membrane proteins at the neuromuscular junction have been proposed to participate in the immobilization of the nicotinic acetylcholine receptor at the synapse. An 87 kd cytoplasmic peripheral membrane protein has been demonstrated to colocalize with the nicotinic acetylcholine receptor in the Torpedo electric organ and at the mammalian neuromuscular junction. We have cloned the cDNA encoding the 87K protein from Torpedo electric organ, and the predicted protein sequence is homologous to the C-terminal domains of dystrophin, the protein product of the Duchenne muscular dystrophy gene. The 87K protein displays a restricted pattern of expression detected only in electric organ, brain, and skeletal muscle. Analysis of the in vitro and in vivo phosphorylation of the 87K protein indicates that it is multiply phosphorylated on serine, threonine, and tyrosine residues. The 87K protein is in a complex with other proteins associated with the post-synaptic membrane, including dystrophin and a 58 kd protein. These results suggest that the 87K protein is involved in the formation and stability of synapses and is regulated by protein phosphorylation.

Original languageEnglish (US)
Pages (from-to)511-522
Number of pages12
JournalNeuron
Volume10
Issue number3
DOIs
StatePublished - 1993

Fingerprint

Torpedo
Dystrophin
Protein-Tyrosine Kinases
Membrane Proteins
Electric Organ
Proteins
Neuromuscular Junction
Nicotinic Receptors
Synapses
Phosphorylation
Synaptic Membranes
Duchenne Muscular Dystrophy
Threonine
Sequence Homology
Immobilization
Serine
Tyrosine
Skeletal Muscle
Complementary DNA
Cell Membrane

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

The 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin. / Wagner, Kathryn Rae; Cohen, Jonathan B.; Huganir, Richard L.

In: Neuron, Vol. 10, No. 3, 1993, p. 511-522.

Research output: Contribution to journalArticle

@article{e993cc10fed248c285964360af506164,
title = "The 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin",
abstract = "Postsynaptic peripheral membrane proteins at the neuromuscular junction have been proposed to participate in the immobilization of the nicotinic acetylcholine receptor at the synapse. An 87 kd cytoplasmic peripheral membrane protein has been demonstrated to colocalize with the nicotinic acetylcholine receptor in the Torpedo electric organ and at the mammalian neuromuscular junction. We have cloned the cDNA encoding the 87K protein from Torpedo electric organ, and the predicted protein sequence is homologous to the C-terminal domains of dystrophin, the protein product of the Duchenne muscular dystrophy gene. The 87K protein displays a restricted pattern of expression detected only in electric organ, brain, and skeletal muscle. Analysis of the in vitro and in vivo phosphorylation of the 87K protein indicates that it is multiply phosphorylated on serine, threonine, and tyrosine residues. The 87K protein is in a complex with other proteins associated with the post-synaptic membrane, including dystrophin and a 58 kd protein. These results suggest that the 87K protein is involved in the formation and stability of synapses and is regulated by protein phosphorylation.",
author = "Wagner, {Kathryn Rae} and Cohen, {Jonathan B.} and Huganir, {Richard L}",
year = "1993",
doi = "10.1016/0896-6273(93)90338-R",
language = "English (US)",
volume = "10",
pages = "511--522",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - The 87K postsynaptic membrane protein from torpedo is a protein-tyrosine kinase substrate homologous to dystrophin

AU - Wagner, Kathryn Rae

AU - Cohen, Jonathan B.

AU - Huganir, Richard L

PY - 1993

Y1 - 1993

N2 - Postsynaptic peripheral membrane proteins at the neuromuscular junction have been proposed to participate in the immobilization of the nicotinic acetylcholine receptor at the synapse. An 87 kd cytoplasmic peripheral membrane protein has been demonstrated to colocalize with the nicotinic acetylcholine receptor in the Torpedo electric organ and at the mammalian neuromuscular junction. We have cloned the cDNA encoding the 87K protein from Torpedo electric organ, and the predicted protein sequence is homologous to the C-terminal domains of dystrophin, the protein product of the Duchenne muscular dystrophy gene. The 87K protein displays a restricted pattern of expression detected only in electric organ, brain, and skeletal muscle. Analysis of the in vitro and in vivo phosphorylation of the 87K protein indicates that it is multiply phosphorylated on serine, threonine, and tyrosine residues. The 87K protein is in a complex with other proteins associated with the post-synaptic membrane, including dystrophin and a 58 kd protein. These results suggest that the 87K protein is involved in the formation and stability of synapses and is regulated by protein phosphorylation.

AB - Postsynaptic peripheral membrane proteins at the neuromuscular junction have been proposed to participate in the immobilization of the nicotinic acetylcholine receptor at the synapse. An 87 kd cytoplasmic peripheral membrane protein has been demonstrated to colocalize with the nicotinic acetylcholine receptor in the Torpedo electric organ and at the mammalian neuromuscular junction. We have cloned the cDNA encoding the 87K protein from Torpedo electric organ, and the predicted protein sequence is homologous to the C-terminal domains of dystrophin, the protein product of the Duchenne muscular dystrophy gene. The 87K protein displays a restricted pattern of expression detected only in electric organ, brain, and skeletal muscle. Analysis of the in vitro and in vivo phosphorylation of the 87K protein indicates that it is multiply phosphorylated on serine, threonine, and tyrosine residues. The 87K protein is in a complex with other proteins associated with the post-synaptic membrane, including dystrophin and a 58 kd protein. These results suggest that the 87K protein is involved in the formation and stability of synapses and is regulated by protein phosphorylation.

UR - http://www.scopus.com/inward/record.url?scp=0027481757&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027481757&partnerID=8YFLogxK

U2 - 10.1016/0896-6273(93)90338-R

DO - 10.1016/0896-6273(93)90338-R

M3 - Article

C2 - 8461138

AN - SCOPUS:0027481757

VL - 10

SP - 511

EP - 522

JO - Neuron

JF - Neuron

SN - 0896-6273

IS - 3

ER -