PortalPublikationenTransient tyrosine phosphorylation of human ryanodine recept...

Transient tyrosine phosphorylation of human ryanodine receptor upon T cell stimulation.

Standard

Transient tyrosine phosphorylation of human ryanodine receptor upon T cell stimulation. / Guse, A H; Tsygankov, A Y; Weber, K; Mayr, Georg W.

in: J BIOL CHEM, Jahrgang 276, Nr. 37, 37, 2001, S. 34722-34727.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Guse, AH, Tsygankov, AY, Weber, K & Mayr, GW 2001, 'Transient tyrosine phosphorylation of human ryanodine receptor upon T cell stimulation.', J BIOL CHEM, Jg. 276, Nr. 37, 37, S. 34722-34727. <http://www.ncbi.nlm.nih.gov/pubmed/11466305?dopt=Citation>

APA

Guse, A. H., Tsygankov, A. Y., Weber, K., & Mayr, G. W. (2001). Transient tyrosine phosphorylation of human ryanodine receptor upon T cell stimulation. J BIOL CHEM, 276(37), 34722-34727. [37]. http://www.ncbi.nlm.nih.gov/pubmed/11466305?dopt=Citation

Vancouver

Guse AH, Tsygankov AY, Weber K, Mayr GW. Transient tyrosine phosphorylation of human ryanodine receptor upon T cell stimulation. J BIOL CHEM. 2001;276(37):34722-34727. 37.

Bibtex

@article{c0d06a2cd31f4d0fa75baa3d6a67544c,
title = "Transient tyrosine phosphorylation of human ryanodine receptor upon T cell stimulation.",
abstract = "The ryanodine receptor of Jurkat T lymphocytes was phosphorylated on tyrosine residues upon stimulation of the cells via the T cell receptor/CD3 complex. The tyrosine phosphorylation was transient, reaching a maximum at 2 min, and rapidly declined thereafter. In co-immunoprecipitates of the ryanodine receptor, the tyrosine kinases p56(lck) and p59(fyn) were detected. However, only p59(fyn) associated with the ryanodine receptor in a stimulation-dependent fashion. Both tyrosine kinases, recombinantly expressed as glutathione S-transferase (GST) fusion proteins, phosphorylated the immunoprecipitated ryanodine receptor in vitro. In permeabilized Jurkat T cells, GST-p59(fyn), but not GST-p56(lck), GST-Grb2, or GST alone, significantly and concentration-dependently enhanced Ca(2+) release by cyclic ADP-ribose. The tyrosine kinase inhibitor PP2 specifically blocked the effect of GST-p59(fyn). This indicates that intracellular Ca(2+) release via ryanodine receptors may be modulated by tyrosine phosphorylation during T cell activation.",
author = "Guse, {A H} and Tsygankov, {A Y} and K Weber and Mayr, {Georg W.}",
year = "2001",
language = "Deutsch",
volume = "276",
pages = "34722--34727",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "37",

}

RIS

TY - JOUR

T1 - Transient tyrosine phosphorylation of human ryanodine receptor upon T cell stimulation.

AU - Guse, A H

AU - Tsygankov, A Y

AU - Weber, K

AU - Mayr, Georg W.

PY - 2001

Y1 - 2001

N2 - The ryanodine receptor of Jurkat T lymphocytes was phosphorylated on tyrosine residues upon stimulation of the cells via the T cell receptor/CD3 complex. The tyrosine phosphorylation was transient, reaching a maximum at 2 min, and rapidly declined thereafter. In co-immunoprecipitates of the ryanodine receptor, the tyrosine kinases p56(lck) and p59(fyn) were detected. However, only p59(fyn) associated with the ryanodine receptor in a stimulation-dependent fashion. Both tyrosine kinases, recombinantly expressed as glutathione S-transferase (GST) fusion proteins, phosphorylated the immunoprecipitated ryanodine receptor in vitro. In permeabilized Jurkat T cells, GST-p59(fyn), but not GST-p56(lck), GST-Grb2, or GST alone, significantly and concentration-dependently enhanced Ca(2+) release by cyclic ADP-ribose. The tyrosine kinase inhibitor PP2 specifically blocked the effect of GST-p59(fyn). This indicates that intracellular Ca(2+) release via ryanodine receptors may be modulated by tyrosine phosphorylation during T cell activation.

AB - The ryanodine receptor of Jurkat T lymphocytes was phosphorylated on tyrosine residues upon stimulation of the cells via the T cell receptor/CD3 complex. The tyrosine phosphorylation was transient, reaching a maximum at 2 min, and rapidly declined thereafter. In co-immunoprecipitates of the ryanodine receptor, the tyrosine kinases p56(lck) and p59(fyn) were detected. However, only p59(fyn) associated with the ryanodine receptor in a stimulation-dependent fashion. Both tyrosine kinases, recombinantly expressed as glutathione S-transferase (GST) fusion proteins, phosphorylated the immunoprecipitated ryanodine receptor in vitro. In permeabilized Jurkat T cells, GST-p59(fyn), but not GST-p56(lck), GST-Grb2, or GST alone, significantly and concentration-dependently enhanced Ca(2+) release by cyclic ADP-ribose. The tyrosine kinase inhibitor PP2 specifically blocked the effect of GST-p59(fyn). This indicates that intracellular Ca(2+) release via ryanodine receptors may be modulated by tyrosine phosphorylation during T cell activation.

M3 - SCORING: Zeitschriftenaufsatz

VL - 276

SP - 34722

EP - 34727

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 37

M1 - 37

ER -