P56(LCK) INTERACTS VIA ITS SRC HOMOLOGY-2 DOMAIN WITH THE ZAP-70 KINASE

被引:163
作者
DUPLAY, P
THOME, M
HERVE, F
ACUTO, O
机构
[1] Laboratory of Molecular Immunology, Department of lmmunologly, Institut Pasteur, Paris, 75724
关键词
D O I
10.1084/jem.179.4.1163
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
p56kk, a member of the src family of protein tyrosine kinases, is an essential component in T cell receptor (TCR) signal transduction. p56lck contains a src homology 2 (SH2) domain found in a number of proteins involved in intracellular signaling. SH2 domains have been implicated in protein-protein interactions by binding to sequences in target proteins containing phosphorylated tyrosine. Using an in vitro assay, we have studied specific binding of tyrosine-phosphorylated proteins to a recombinant p56lck SH2 domain. In nonactivated Jurkat cells, two tyrosine-phosphorylated proteins were detected. Stimulation with anti-CD3 monoclonal antibodies induced the binding of seven additional tyrosine-phosphorylated proteins to the SH2 domain of p56lck. We have identified the zeta-associated tyrosine kinase, ZAP-70, as one of these proteins. Evidence suggests that binding of ZAP-70 to p56lck SH2 is direct and not mediated by zeta. The significance of this interaction was further investigated in vivo. p56lck could be coprecipitated with the zeta/ZAP-70 complex and conversely, ZAP-70 was detected in p56lck immunoprecipitates of activated Jurkat cells. The physical association of p56lck and ZAP-70 during activation supports the recently proposed functional cooperation of these two tyrosine kinases in TCR signaling.
引用
收藏
页码:1163 / 1172
页数:10
相关论文
共 62 条
[1]   ENHANCEMENT OF T-CELL RESPONSIVENESS BY THE LYMPHOCYTE-SPECIFIC TYROSINE PROTEIN-KINASE P56LCK [J].
ABRAHAM, N ;
MICELI, MC ;
PARNES, JR ;
VEILLETTE, A .
NATURE, 1991, 350 (6313) :62-66
[3]   DEFECTIVE T-CELL RECEPTOR SIGNALING IN MICE LACKING THE THYMIC ISOFORM OF P59(FYN) [J].
APPLEBY, MW ;
GROSS, JA ;
COOKE, MP ;
LEVIN, SD ;
QIAN, X ;
PERLMUTTER, RM .
CELL, 1992, 70 (05) :751-763
[4]   ALTERED TYROSINE-527 PHOSPHORYLATION AND MITOTIC ACTIVATION OF P60C-SRC [J].
BAGRODIA, S ;
CHACKALAPARAMPIL, I ;
KMIECIK, TE ;
SHALLOWAY, D .
NATURE, 1991, 349 (6305) :172-175
[5]   PRODUCTION IN ESCHERICHIA-COLI AND ONE-STEP PURIFICATION OF BIFUNCTIONAL HYBRID PROTEINS WHICH BIND MALTOSE - EXPORT OF THE KLENOW POLYMERASE INTO THE PERIPLASMIC SPACE [J].
BEDOUELLE, H ;
DUPLAY, P .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 171 (03) :541-549
[6]  
BEYERS A D, 1992, Trends in Cell Biology, V2, P253, DOI 10.1016/0962-8924(92)90190-X
[7]   MOLECULAR ASSOCIATIONS BETWEEN THE LYMPHOCYTE-T ANTIGEN RECEPTOR COMPLEX AND THE SURFACE ANTIGEN-CD2, ANTIGEN-CD4, OR ANTIGEN-CD8 AND ANTIGEN-CD5 [J].
BEYERS, AD ;
SPRUYT, LL ;
WILLIAMS, AF .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (07) :2945-2949
[8]   CD5 ACTS AS A TYROSINE KINASE SUBSTRATE WITHIN A RECEPTOR COMPLEX COMPRISING T-CELL RECEPTOR ZETA-CHAIN CD3 AND PROTEIN-TYROSINE KINASES P56LCK AND P59FYN [J].
BURGESS, KE ;
YAMAMOTO, M ;
PRASAD, KVS ;
RUDD, CE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (19) :9311-9315
[9]   ZAPPING THE T-CELL RECEPTOR [J].
BURNS, CM ;
ASHWELL, JD .
CURRENT BIOLOGY, 1993, 3 (02) :97-99
[10]   PRODUCT OF VAV PROTOONCOGENE DEFINES A NEW CLASS OF TYROSINE PROTEIN-KINASE SUBSTRATES [J].
BUSTELO, XR ;
LEDBETTER, JA ;
BARBACID, M .
NATURE, 1992, 356 (6364) :68-71