Tyrosine and serine phosphorylation of dystrophin and the 58-kDa protein in the postsynaptic membrane of Torpedo electric organ

Research output: Contribution to journalArticle

Abstract

Dystrophin associates with a 58-kDa and an 87-kDa protein in the postsynaptic membrane of the Torpedo electric organ. We have previously shown that the 87-kDa protein is a major phosphotyrosine-containing protein in these membranes. Immunoprecipitation of the 87-kDa protein from phosphorylated postsynaptic membranes results in coimmunoprecipitation of additional phosphoproteins. These phosphoproteins are identified as dystrophin and the 58-kDa protein. Monoclonal antibodies to dystrophin and the 58-kDa protein immunoprecipitate phosphorylated forms of these proteins from postsynaptic membranes phosphorylated in vitro. Phosphoamino acid analysis reveals that dystrophin and the 58-kDa protein are phosphorylated on serine and tyrosine residues. In addition, both dystrophin and the 58-kDa protein are shown to be phosphorylated on tyrosine residues in vivo. These results suggest that the synaptic function of dystrophin and its associated proteins, the 58-kDa and 87-kDa proteins, may be modulated by tyrosine and serine protein phosphorylation.

Original languageEnglish (US)
Pages (from-to)1947-1952
Number of pages6
JournalJournal of Neurochemistry
Volume62
Issue number5
StatePublished - May 1994

Fingerprint

Electric Organ
Torpedo
Dystrophin
Phosphorylation
Serine
Tyrosine
Membranes
Proteins
Phosphoproteins
Dystrophin-Associated Proteins
Membrane Proteins
Phosphoamino Acids
Phosphotyrosine
Immunoprecipitation
Monoclonal Antibodies

Keywords

  • Dystrophin
  • Phosphorylation
  • Postsynaptic membrane
  • Serine
  • Synaptic function
  • Torpedo electric organ
  • Tyrosine

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

@article{bf192c18bf0a4b3ea67413205bb38f72,
title = "Tyrosine and serine phosphorylation of dystrophin and the 58-kDa protein in the postsynaptic membrane of Torpedo electric organ",
abstract = "Dystrophin associates with a 58-kDa and an 87-kDa protein in the postsynaptic membrane of the Torpedo electric organ. We have previously shown that the 87-kDa protein is a major phosphotyrosine-containing protein in these membranes. Immunoprecipitation of the 87-kDa protein from phosphorylated postsynaptic membranes results in coimmunoprecipitation of additional phosphoproteins. These phosphoproteins are identified as dystrophin and the 58-kDa protein. Monoclonal antibodies to dystrophin and the 58-kDa protein immunoprecipitate phosphorylated forms of these proteins from postsynaptic membranes phosphorylated in vitro. Phosphoamino acid analysis reveals that dystrophin and the 58-kDa protein are phosphorylated on serine and tyrosine residues. In addition, both dystrophin and the 58-kDa protein are shown to be phosphorylated on tyrosine residues in vivo. These results suggest that the synaptic function of dystrophin and its associated proteins, the 58-kDa and 87-kDa proteins, may be modulated by tyrosine and serine protein phosphorylation.",
keywords = "Dystrophin, Phosphorylation, Postsynaptic membrane, Serine, Synaptic function, Torpedo electric organ, Tyrosine",
author = "Wagner, {Kathryn Rae} and Huganir, {Richard L}",
year = "1994",
month = "5",
language = "English (US)",
volume = "62",
pages = "1947--1952",
journal = "Journal of Neurochemistry",
issn = "0022-3042",
publisher = "Wiley-Blackwell",
number = "5",

}

TY - JOUR

T1 - Tyrosine and serine phosphorylation of dystrophin and the 58-kDa protein in the postsynaptic membrane of Torpedo electric organ

AU - Wagner, Kathryn Rae

AU - Huganir, Richard L

PY - 1994/5

Y1 - 1994/5

N2 - Dystrophin associates with a 58-kDa and an 87-kDa protein in the postsynaptic membrane of the Torpedo electric organ. We have previously shown that the 87-kDa protein is a major phosphotyrosine-containing protein in these membranes. Immunoprecipitation of the 87-kDa protein from phosphorylated postsynaptic membranes results in coimmunoprecipitation of additional phosphoproteins. These phosphoproteins are identified as dystrophin and the 58-kDa protein. Monoclonal antibodies to dystrophin and the 58-kDa protein immunoprecipitate phosphorylated forms of these proteins from postsynaptic membranes phosphorylated in vitro. Phosphoamino acid analysis reveals that dystrophin and the 58-kDa protein are phosphorylated on serine and tyrosine residues. In addition, both dystrophin and the 58-kDa protein are shown to be phosphorylated on tyrosine residues in vivo. These results suggest that the synaptic function of dystrophin and its associated proteins, the 58-kDa and 87-kDa proteins, may be modulated by tyrosine and serine protein phosphorylation.

AB - Dystrophin associates with a 58-kDa and an 87-kDa protein in the postsynaptic membrane of the Torpedo electric organ. We have previously shown that the 87-kDa protein is a major phosphotyrosine-containing protein in these membranes. Immunoprecipitation of the 87-kDa protein from phosphorylated postsynaptic membranes results in coimmunoprecipitation of additional phosphoproteins. These phosphoproteins are identified as dystrophin and the 58-kDa protein. Monoclonal antibodies to dystrophin and the 58-kDa protein immunoprecipitate phosphorylated forms of these proteins from postsynaptic membranes phosphorylated in vitro. Phosphoamino acid analysis reveals that dystrophin and the 58-kDa protein are phosphorylated on serine and tyrosine residues. In addition, both dystrophin and the 58-kDa protein are shown to be phosphorylated on tyrosine residues in vivo. These results suggest that the synaptic function of dystrophin and its associated proteins, the 58-kDa and 87-kDa proteins, may be modulated by tyrosine and serine protein phosphorylation.

KW - Dystrophin

KW - Phosphorylation

KW - Postsynaptic membrane

KW - Serine

KW - Synaptic function

KW - Torpedo electric organ

KW - Tyrosine

UR - http://www.scopus.com/inward/record.url?scp=0028261751&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028261751&partnerID=8YFLogxK

M3 - Article

VL - 62

SP - 1947

EP - 1952

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

SN - 0022-3042

IS - 5

ER -