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...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-06, Vol.92 (13), p.5778-5782 |
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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. |
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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> |
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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 |
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