The 21- and 23-kD forms of TCRζ are generated by specific ITAM phosphorylations

Nicolai S.C. Van Oers; Brett Tohlen; Bernard Malissen; Carolyn R. Moomaw; Steve Afendis; Clive A. Slaughter

doi:10.1038/79774

The 21- and 23-kD forms of TCRζ are generated by specific ITAM phosphorylations

Nicolai S.C. Van Oers, Brett Tohlen, Bernard Malissen, Carolyn R. Moomaw, Steve Afendis, Clive A. Slaughter

Research output: Contribution to journal › Article › peer-review

83 Scopus citations

Abstract

The T cell receptor (TCR) ζ subunit contains three immunoreceptor tyrosine-based activation motifs (ITAMs) that translate effective extracellular ligand binding into intracellular signals by becoming phosphorylated into 21- and 23-kD forms. We report here that the 21-kD form of TCRζ is generated by phosphorylation of the tyrosines in the second and third ITAMs, whereas the 23-kD form is formed by the additional phosphorylation of the membrane-proximal ITAM tyrosines. The stable formation of the 21- and 23-kD species requires the binding of the tandem SH2 domains of ZAP-70. We also report that TCR-mediated signaling processes can proceed independently of either the 21- or 23-kD species of TCRζ.

Original language	English (US)
Pages (from-to)	322-328
Number of pages	7
Journal	Nature Immunology
Volume	1
Issue number	4
DOIs	https://doi.org/10.1038/79774
State	Published - Oct 2000
Externally published	Yes

ASJC Scopus subject areas

Immunology and Allergy
Immunology

Access to Document

10.1038/79774

Cite this

@article{d522c65f758a4df8804036bd2b2d85cb,

title = "The 21- and 23-kD forms of TCRζ are generated by specific ITAM phosphorylations",

abstract = "The T cell receptor (TCR) ζ subunit contains three immunoreceptor tyrosine-based activation motifs (ITAMs) that translate effective extracellular ligand binding into intracellular signals by becoming phosphorylated into 21- and 23-kD forms. We report here that the 21-kD form of TCRζ is generated by phosphorylation of the tyrosines in the second and third ITAMs, whereas the 23-kD form is formed by the additional phosphorylation of the membrane-proximal ITAM tyrosines. The stable formation of the 21- and 23-kD species requires the binding of the tandem SH2 domains of ZAP-70. We also report that TCR-mediated signaling processes can proceed independently of either the 21- or 23-kD species of TCRζ.",

author = "{Van Oers}, {Nicolai S.C.} and Brett Tohlen and Bernard Malissen and Moomaw, {Carolyn R.} and Steve Afendis and Slaughter, {Clive A.}",

note = "Funding Information: Acknowledgments We thank J. Ritter for generation of mice; ˙H. Nikaidoh and staff from the Children{\textquoteright}s Medical Center of Dallas;A.Weiss, D. Kioussis and M. Cobb for discussions; D. Kioussis for VA-CD2 transgenic constructs.This work was supported in part by a grant from the NIH (RO1 AI42953 to N. S. C.V. O.) and the Howard Hughes Medical Institute (C.A. S).",

year = "2000",

month = oct,

doi = "10.1038/79774",

language = "English (US)",

volume = "1",

pages = "322--328",

journal = "Nature Immunology",

issn = "1529-2908",

publisher = "Nature Publishing Group",

number = "4",

}

TY - JOUR

T1 - The 21- and 23-kD forms of TCRζ are generated by specific ITAM phosphorylations

AU - Van Oers, Nicolai S.C.

AU - Tohlen, Brett

AU - Malissen, Bernard

AU - Moomaw, Carolyn R.

AU - Afendis, Steve

AU - Slaughter, Clive A.

N1 - Funding Information: Acknowledgments We thank J. Ritter for generation of mice; ˙H. Nikaidoh and staff from the Children’s Medical Center of Dallas;A.Weiss, D. Kioussis and M. Cobb for discussions; D. Kioussis for VA-CD2 transgenic constructs.This work was supported in part by a grant from the NIH (RO1 AI42953 to N. S. C.V. O.) and the Howard Hughes Medical Institute (C.A. S).

PY - 2000/10

Y1 - 2000/10

N2 - The T cell receptor (TCR) ζ subunit contains three immunoreceptor tyrosine-based activation motifs (ITAMs) that translate effective extracellular ligand binding into intracellular signals by becoming phosphorylated into 21- and 23-kD forms. We report here that the 21-kD form of TCRζ is generated by phosphorylation of the tyrosines in the second and third ITAMs, whereas the 23-kD form is formed by the additional phosphorylation of the membrane-proximal ITAM tyrosines. The stable formation of the 21- and 23-kD species requires the binding of the tandem SH2 domains of ZAP-70. We also report that TCR-mediated signaling processes can proceed independently of either the 21- or 23-kD species of TCRζ.

AB - The T cell receptor (TCR) ζ subunit contains three immunoreceptor tyrosine-based activation motifs (ITAMs) that translate effective extracellular ligand binding into intracellular signals by becoming phosphorylated into 21- and 23-kD forms. We report here that the 21-kD form of TCRζ is generated by phosphorylation of the tyrosines in the second and third ITAMs, whereas the 23-kD form is formed by the additional phosphorylation of the membrane-proximal ITAM tyrosines. The stable formation of the 21- and 23-kD species requires the binding of the tandem SH2 domains of ZAP-70. We also report that TCR-mediated signaling processes can proceed independently of either the 21- or 23-kD species of TCRζ.

UR - http://www.scopus.com/inward/record.url?scp=0034305516&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034305516&partnerID=8YFLogxK

U2 - 10.1038/79774

DO - 10.1038/79774

M3 - Article

C2 - 11017104

AN - SCOPUS:0034305516

SN - 1529-2908

VL - 1

SP - 322

EP - 328

JO - Nature Immunology

JF - Nature Immunology

IS - 4

ER -

The 21- and 23-kD forms of TCRζ are generated by specific ITAM phosphorylations

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this