Modification of Ser59in the Unique N-Terminal Region of Tyrosine Kinase p56lckRegulates Specificity of its Src Homology 2 Domain

During T-cell activation, Ser59in the unique N-terminal region of p56lckis phosphorylated. Mutation of Ser59to Glu59mimics Ser59phosphorylation, and upon CD4 crosslinking, this mutant p56lckinduces tyrosine phosphorylation of intracellular proteins distinct from those induced by wild-type p56lck. Mu...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1995-06, Vol.92 (13), p.5778-5782
Hauptverfasser: Joung, Insil, Kim, TaeUe, Stolz, Lesley A., Payne, Gillian, Winkler, David G., Walsh, Christopher T., Strominger, Jack L., Shin, Jaekyoon
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 5782
container_issue 13
container_start_page 5778
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 92
creator Joung, Insil
Kim, TaeUe
Stolz, Lesley A.
Payne, Gillian
Winkler, David G.
Walsh, Christopher T.
Strominger, Jack L.
Shin, Jaekyoon
description During T-cell activation, Ser59in the unique N-terminal region of p56lckis phosphorylated. Mutation of Ser59to Glu59mimics Ser59phosphorylation, and upon CD4 crosslinking, this mutant p56lckinduces tyrosine phosphorylation of intracellular proteins distinct from those induced by wild-type p56lck. Mutant and wild-type p56lckhave similar affinities for CD4 and similar kinase activities. In glutathione S-transferase fusion proteins, the p56lckSrc homology 2 (SH2) domain with the SH3 domain and the unique N-terminal region (including Ser59) has a different binding specificity for phosphotyrosyl proteins than the SH2 domain alone. Either deletion of the unique N-terminal region or mutation of Ser59to Glu59in the fusion protein reverts the phosphotyrosyl protein binding specificity back to that of the SH2 domain alone. These results suggest that phosphorylation of Ser59regulates the function of p56lckby controlling binding specificity of its SH2 domain.
format Article
fullrecord <record><control><sourceid>jstor</sourceid><recordid>TN_cdi_jstor_primary_2367911</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>2367911</jstor_id><sourcerecordid>2367911</sourcerecordid><originalsourceid>FETCH-jstor_primary_23679113</originalsourceid><addsrcrecordid>eNqFjLsKwkAQRbdQ8PkHFvMDgTUaY2ofCKKFibUscRJHNztxdy3S-elGsLe6cM7hdkRfyjAOlvNw3hMD5-5SyiRayr54H_hKBeXKExvgAlK0UUIG_A3hbOj5QjgGGdqKjNJwwvLXZY1lRwZh3wqHUEcLnT9a_9LKo4O0xvx7TL755uRbZHPYccWaywZCWHOlyIxEt1Da4fi3QzHZbrLVLrg7z_ZSW6qUbS7hbBEn0-nsj_4Aa8VKAA</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Modification of Ser59in the Unique N-Terminal Region of Tyrosine Kinase p56lckRegulates Specificity of its Src Homology 2 Domain</title><source>Jstor Complete Legacy</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Joung, Insil ; Kim, TaeUe ; Stolz, Lesley A. ; Payne, Gillian ; Winkler, David G. ; Walsh, Christopher T. ; Strominger, Jack L. ; Shin, Jaekyoon</creator><creatorcontrib>Joung, Insil ; Kim, TaeUe ; Stolz, Lesley A. ; Payne, Gillian ; Winkler, David G. ; Walsh, Christopher T. ; Strominger, Jack L. ; Shin, Jaekyoon</creatorcontrib><description>During T-cell activation, Ser59in the unique N-terminal region of p56lckis phosphorylated. Mutation of Ser59to Glu59mimics Ser59phosphorylation, and upon CD4 crosslinking, this mutant p56lckinduces tyrosine phosphorylation of intracellular proteins distinct from those induced by wild-type p56lck. Mutant and wild-type p56lckhave similar affinities for CD4 and similar kinase activities. In glutathione S-transferase fusion proteins, the p56lckSrc homology 2 (SH2) domain with the SH3 domain and the unique N-terminal region (including Ser59) has a different binding specificity for phosphotyrosyl proteins than the SH2 domain alone. Either deletion of the unique N-terminal region or mutation of Ser59to Glu59in the fusion protein reverts the phosphotyrosyl protein binding specificity back to that of the SH2 domain alone. These results suggest that phosphorylation of Ser59regulates the function of p56lckby controlling binding specificity of its SH2 domain.</description><identifier>ISSN: 0027-8424</identifier><language>eng</language><publisher>National Academy of Sciences of the United States of America</publisher><subject>Antibodies ; Biochemistry ; Crosslinking ; Goods and services tax ; HeLa cells ; Phosphatases ; Phosphorylation ; Physiological regulation ; Proteins ; T lymphocytes</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-06, Vol.92 (13), p.5778-5782</ispartof><rights>Copyright 1995 The National Academy of Sciences of the United States of America</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2367911$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2367911$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,778,782,801,58004,58237</link.rule.ids></links><search><creatorcontrib>Joung, Insil</creatorcontrib><creatorcontrib>Kim, TaeUe</creatorcontrib><creatorcontrib>Stolz, Lesley A.</creatorcontrib><creatorcontrib>Payne, Gillian</creatorcontrib><creatorcontrib>Winkler, David G.</creatorcontrib><creatorcontrib>Walsh, Christopher T.</creatorcontrib><creatorcontrib>Strominger, Jack L.</creatorcontrib><creatorcontrib>Shin, Jaekyoon</creatorcontrib><title>Modification of Ser59in the Unique N-Terminal Region of Tyrosine Kinase p56lckRegulates Specificity of its Src Homology 2 Domain</title><title>Proceedings of the National Academy of Sciences - PNAS</title><description>During T-cell activation, Ser59in the unique N-terminal region of p56lckis phosphorylated. Mutation of Ser59to Glu59mimics Ser59phosphorylation, and upon CD4 crosslinking, this mutant p56lckinduces tyrosine phosphorylation of intracellular proteins distinct from those induced by wild-type p56lck. Mutant and wild-type p56lckhave similar affinities for CD4 and similar kinase activities. In glutathione S-transferase fusion proteins, the p56lckSrc homology 2 (SH2) domain with the SH3 domain and the unique N-terminal region (including Ser59) has a different binding specificity for phosphotyrosyl proteins than the SH2 domain alone. Either deletion of the unique N-terminal region or mutation of Ser59to Glu59in the fusion protein reverts the phosphotyrosyl protein binding specificity back to that of the SH2 domain alone. These results suggest that phosphorylation of Ser59regulates the function of p56lckby controlling binding specificity of its SH2 domain.</description><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Crosslinking</subject><subject>Goods and services tax</subject><subject>HeLa cells</subject><subject>Phosphatases</subject><subject>Phosphorylation</subject><subject>Physiological regulation</subject><subject>Proteins</subject><subject>T lymphocytes</subject><issn>0027-8424</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqFjLsKwkAQRbdQ8PkHFvMDgTUaY2ofCKKFibUscRJHNztxdy3S-elGsLe6cM7hdkRfyjAOlvNw3hMD5-5SyiRayr54H_hKBeXKExvgAlK0UUIG_A3hbOj5QjgGGdqKjNJwwvLXZY1lRwZh3wqHUEcLnT9a_9LKo4O0xvx7TL755uRbZHPYccWaywZCWHOlyIxEt1Da4fi3QzHZbrLVLrg7z_ZSW6qUbS7hbBEn0-nsj_4Aa8VKAA</recordid><startdate>19950620</startdate><enddate>19950620</enddate><creator>Joung, Insil</creator><creator>Kim, TaeUe</creator><creator>Stolz, Lesley A.</creator><creator>Payne, Gillian</creator><creator>Winkler, David G.</creator><creator>Walsh, Christopher T.</creator><creator>Strominger, Jack L.</creator><creator>Shin, Jaekyoon</creator><general>National Academy of Sciences of the United States of America</general><scope/></search><sort><creationdate>19950620</creationdate><title>Modification of Ser59in the Unique N-Terminal Region of Tyrosine Kinase p56lckRegulates Specificity of its Src Homology 2 Domain</title><author>Joung, Insil ; Kim, TaeUe ; Stolz, Lesley A. ; Payne, Gillian ; Winkler, David G. ; Walsh, Christopher T. ; Strominger, Jack L. ; Shin, Jaekyoon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-jstor_primary_23679113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Antibodies</topic><topic>Biochemistry</topic><topic>Crosslinking</topic><topic>Goods and services tax</topic><topic>HeLa cells</topic><topic>Phosphatases</topic><topic>Phosphorylation</topic><topic>Physiological regulation</topic><topic>Proteins</topic><topic>T lymphocytes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joung, Insil</creatorcontrib><creatorcontrib>Kim, TaeUe</creatorcontrib><creatorcontrib>Stolz, Lesley A.</creatorcontrib><creatorcontrib>Payne, Gillian</creatorcontrib><creatorcontrib>Winkler, David G.</creatorcontrib><creatorcontrib>Walsh, Christopher T.</creatorcontrib><creatorcontrib>Strominger, Jack L.</creatorcontrib><creatorcontrib>Shin, Jaekyoon</creatorcontrib><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joung, Insil</au><au>Kim, TaeUe</au><au>Stolz, Lesley A.</au><au>Payne, Gillian</au><au>Winkler, David G.</au><au>Walsh, Christopher T.</au><au>Strominger, Jack L.</au><au>Shin, Jaekyoon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modification of Ser59in the Unique N-Terminal Region of Tyrosine Kinase p56lckRegulates Specificity of its Src Homology 2 Domain</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><date>1995-06-20</date><risdate>1995</risdate><volume>92</volume><issue>13</issue><spage>5778</spage><epage>5782</epage><pages>5778-5782</pages><issn>0027-8424</issn><abstract>During T-cell activation, Ser59in the unique N-terminal region of p56lckis phosphorylated. Mutation of Ser59to Glu59mimics Ser59phosphorylation, and upon CD4 crosslinking, this mutant p56lckinduces tyrosine phosphorylation of intracellular proteins distinct from those induced by wild-type p56lck. Mutant and wild-type p56lckhave similar affinities for CD4 and similar kinase activities. In glutathione S-transferase fusion proteins, the p56lckSrc homology 2 (SH2) domain with the SH3 domain and the unique N-terminal region (including Ser59) has a different binding specificity for phosphotyrosyl proteins than the SH2 domain alone. Either deletion of the unique N-terminal region or mutation of Ser59to Glu59in the fusion protein reverts the phosphotyrosyl protein binding specificity back to that of the SH2 domain alone. These results suggest that phosphorylation of Ser59regulates the function of p56lckby controlling binding specificity of its SH2 domain.</abstract><pub>National Academy of Sciences of the United States of America</pub></addata></record>
fulltext fulltext
identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 1995-06, Vol.92 (13), p.5778-5782
issn 0027-8424
language eng
recordid cdi_jstor_primary_2367911
source Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry
subjects Antibodies
Biochemistry
Crosslinking
Goods and services tax
HeLa cells
Phosphatases
Phosphorylation
Physiological regulation
Proteins
T lymphocytes
title Modification of Ser59in the Unique N-Terminal Region of Tyrosine Kinase p56lckRegulates Specificity of its Src Homology 2 Domain
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-15T11%3A33%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Modification%20of%20Ser59in%20the%20Unique%20N-Terminal%20Region%20of%20Tyrosine%20Kinase%20p56lckRegulates%20Specificity%20of%20its%20Src%20Homology%202%20Domain&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Joung,%20Insil&rft.date=1995-06-20&rft.volume=92&rft.issue=13&rft.spage=5778&rft.epage=5782&rft.pages=5778-5782&rft.issn=0027-8424&rft_id=info:doi/&rft_dat=%3Cjstor%3E2367911%3C/jstor%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rft_jstor_id=2367911&rfr_iscdi=true