The cytoskeleton-associated TCR ζ chain is constitutively phosphorylated in the absence of an active p56lck form

Steve Caplan, Osnat Almogi-Hazan, Anala Ezernitchi, Efrat Manaster, Aviv Gazit, Michal Baniyash

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The TCR recognizes peptide-MHC complexes and transmits activation signals leading to cellular responses. We have previously characterized two TCR populations expressed on the T cell surface; one is linked to the cytoskeleton via a detergent-insoluble cytoskeleton-associated ζ (cska-ζ) chain, while the other is detergent soluble and not linked to the cytoskeleton. The cska-ζ form displays unique properties: it is constitutively phosphorylated, does not undergo hyperphosphorylation upon TCR stimulation as opposed to its non-cytoskeleton-associated counterpart (non-cska-ζ) and it maintains a molecular mass of 16 kDa. It is well established that p56lck and possibly p59fyn are responsible for the generation of the 21/23-kDa phosphorylated detergent-soluble ζ form. We now demonstrate that the posphorylation of cska-ζ does not require the activity of p56lck. We also show that although Lck does not phosphorylate cska-ζ in vivo, it retains the capacity to phosphorylate cska-ζ in vitro. Moreover, differences in ζ-associated kinase activity were detected for non-cska-ζ and cska-ζ. Our results indicating that different kinases phosphorylate the two ζ forms are consistent with a growing consensus that each TCR form may regulate distinct cellular functions.

Original languageEnglish (US)
Pages (from-to)580-589
Number of pages10
JournalEuropean Journal of Immunology
Volume31
Issue number2
DOIs
StatePublished - Mar 3 2001

Fingerprint

Cytoskeleton
Detergents
Phosphotransferases
T-Lymphocytes
Peptides
Population

Keywords

  • Cytoskeleton
  • Signaling
  • T cell
  • TCR

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Cite this

The cytoskeleton-associated TCR ζ chain is constitutively phosphorylated in the absence of an active p56lck form. / Caplan, Steve; Almogi-Hazan, Osnat; Ezernitchi, Anala; Manaster, Efrat; Gazit, Aviv; Baniyash, Michal.

In: European Journal of Immunology, Vol. 31, No. 2, 03.03.2001, p. 580-589.

Research output: Contribution to journalArticle

Caplan, Steve ; Almogi-Hazan, Osnat ; Ezernitchi, Anala ; Manaster, Efrat ; Gazit, Aviv ; Baniyash, Michal. / The cytoskeleton-associated TCR ζ chain is constitutively phosphorylated in the absence of an active p56lck form. In: European Journal of Immunology. 2001 ; Vol. 31, No. 2. pp. 580-589.
@article{6da45616406944ab8b37e8a3b3d111f5,
title = "The cytoskeleton-associated TCR ζ chain is constitutively phosphorylated in the absence of an active p56lck form",
abstract = "The TCR recognizes peptide-MHC complexes and transmits activation signals leading to cellular responses. We have previously characterized two TCR populations expressed on the T cell surface; one is linked to the cytoskeleton via a detergent-insoluble cytoskeleton-associated ζ (cska-ζ) chain, while the other is detergent soluble and not linked to the cytoskeleton. The cska-ζ form displays unique properties: it is constitutively phosphorylated, does not undergo hyperphosphorylation upon TCR stimulation as opposed to its non-cytoskeleton-associated counterpart (non-cska-ζ) and it maintains a molecular mass of 16 kDa. It is well established that p56lck and possibly p59fyn are responsible for the generation of the 21/23-kDa phosphorylated detergent-soluble ζ form. We now demonstrate that the posphorylation of cska-ζ does not require the activity of p56lck. We also show that although Lck does not phosphorylate cska-ζ in vivo, it retains the capacity to phosphorylate cska-ζ in vitro. Moreover, differences in ζ-associated kinase activity were detected for non-cska-ζ and cska-ζ. Our results indicating that different kinases phosphorylate the two ζ forms are consistent with a growing consensus that each TCR form may regulate distinct cellular functions.",
keywords = "Cytoskeleton, Signaling, T cell, TCR",
author = "Steve Caplan and Osnat Almogi-Hazan and Anala Ezernitchi and Efrat Manaster and Aviv Gazit and Michal Baniyash",
year = "2001",
month = "3",
day = "3",
doi = "10.1002/1521-4141(200102)31:2<580::AID-IMMU580>3.0.CO;2-H",
language = "English (US)",
volume = "31",
pages = "580--589",
journal = "European Journal of Immunology",
issn = "0014-2980",
publisher = "Wiley-VCH Verlag",
number = "2",

}

TY - JOUR

T1 - The cytoskeleton-associated TCR ζ chain is constitutively phosphorylated in the absence of an active p56lck form

AU - Caplan, Steve

AU - Almogi-Hazan, Osnat

AU - Ezernitchi, Anala

AU - Manaster, Efrat

AU - Gazit, Aviv

AU - Baniyash, Michal

PY - 2001/3/3

Y1 - 2001/3/3

N2 - The TCR recognizes peptide-MHC complexes and transmits activation signals leading to cellular responses. We have previously characterized two TCR populations expressed on the T cell surface; one is linked to the cytoskeleton via a detergent-insoluble cytoskeleton-associated ζ (cska-ζ) chain, while the other is detergent soluble and not linked to the cytoskeleton. The cska-ζ form displays unique properties: it is constitutively phosphorylated, does not undergo hyperphosphorylation upon TCR stimulation as opposed to its non-cytoskeleton-associated counterpart (non-cska-ζ) and it maintains a molecular mass of 16 kDa. It is well established that p56lck and possibly p59fyn are responsible for the generation of the 21/23-kDa phosphorylated detergent-soluble ζ form. We now demonstrate that the posphorylation of cska-ζ does not require the activity of p56lck. We also show that although Lck does not phosphorylate cska-ζ in vivo, it retains the capacity to phosphorylate cska-ζ in vitro. Moreover, differences in ζ-associated kinase activity were detected for non-cska-ζ and cska-ζ. Our results indicating that different kinases phosphorylate the two ζ forms are consistent with a growing consensus that each TCR form may regulate distinct cellular functions.

AB - The TCR recognizes peptide-MHC complexes and transmits activation signals leading to cellular responses. We have previously characterized two TCR populations expressed on the T cell surface; one is linked to the cytoskeleton via a detergent-insoluble cytoskeleton-associated ζ (cska-ζ) chain, while the other is detergent soluble and not linked to the cytoskeleton. The cska-ζ form displays unique properties: it is constitutively phosphorylated, does not undergo hyperphosphorylation upon TCR stimulation as opposed to its non-cytoskeleton-associated counterpart (non-cska-ζ) and it maintains a molecular mass of 16 kDa. It is well established that p56lck and possibly p59fyn are responsible for the generation of the 21/23-kDa phosphorylated detergent-soluble ζ form. We now demonstrate that the posphorylation of cska-ζ does not require the activity of p56lck. We also show that although Lck does not phosphorylate cska-ζ in vivo, it retains the capacity to phosphorylate cska-ζ in vitro. Moreover, differences in ζ-associated kinase activity were detected for non-cska-ζ and cska-ζ. Our results indicating that different kinases phosphorylate the two ζ forms are consistent with a growing consensus that each TCR form may regulate distinct cellular functions.

KW - Cytoskeleton

KW - Signaling

KW - T cell

KW - TCR

UR - http://www.scopus.com/inward/record.url?scp=0035105239&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035105239&partnerID=8YFLogxK

U2 - 10.1002/1521-4141(200102)31:2<580::AID-IMMU580>3.0.CO;2-H

DO - 10.1002/1521-4141(200102)31:2<580::AID-IMMU580>3.0.CO;2-H

M3 - Article

C2 - 11180123

AN - SCOPUS:0035105239

VL - 31

SP - 580

EP - 589

JO - European Journal of Immunology

JF - European Journal of Immunology

SN - 0014-2980

IS - 2

ER -