Interaction of the unique N-terminal region of tyrosine kinase p56 super(lck) with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs
p56 super(lck), a lymphocyte-specific member of the src family of cytoplasmic protein-tyrosine kinases, is associated noncovalently with the cell surface glycoproteins CD4 and CD8, which are expressed on functionally distinct subpopulations of T cells. Using transient co-expression of p56 super(lck)...
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Veröffentlicht in: | Cell 1990-01, Vol.60 (5), p.755-765 |
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creator | Turner, J M Brodsky, M H Irving, BA Levin, S D Perlmutter, R M Littman, DR |
description | p56 super(lck), a lymphocyte-specific member of the src family of cytoplasmic protein-tyrosine kinases, is associated noncovalently with the cell surface glycoproteins CD4 and CD8, which are expressed on functionally distinct subpopulations of T cells. Using transient co-expression of p56 super(lck) with CD4 or CD8 alpha in COS-7 cells, we show that the unique N-terminal region of p56 super(lck) binds to the membrane-proximal 10 and 28 cytoplasmic residues of CD8 alpha and CD4, respectively. Two cysteine residues in each of the critical sequences in CD4, CD8 alpha , and p56 super(lck) are required for association. Our results suggest a novel role for cysteine-mediated interactions between unrelated proteins and provide a model for the association of other src -like cytoplasmic kinases with transmembrane proteins. |
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Using transient co-expression of p56 super(lck) with CD4 or CD8 alpha in COS-7 cells, we show that the unique N-terminal region of p56 super(lck) binds to the membrane-proximal 10 and 28 cytoplasmic residues of CD8 alpha and CD4, respectively. Two cysteine residues in each of the critical sequences in CD4, CD8 alpha , and p56 super(lck) are required for association. Our results suggest a novel role for cysteine-mediated interactions between unrelated proteins and provide a model for the association of other src -like cytoplasmic kinases with transmembrane proteins.</description><identifier>ISSN: 0092-8674</identifier><language>eng</language><subject>CD4 antigen ; CD8 antigen ; cysteine ; lck ; protein p56</subject><ispartof>Cell, 1990-01, Vol.60 (5), p.755-765</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids></links><search><creatorcontrib>Turner, J M</creatorcontrib><creatorcontrib>Brodsky, M H</creatorcontrib><creatorcontrib>Irving, BA</creatorcontrib><creatorcontrib>Levin, S D</creatorcontrib><creatorcontrib>Perlmutter, R M</creatorcontrib><creatorcontrib>Littman, DR</creatorcontrib><title>Interaction of the unique N-terminal region of tyrosine kinase p56 super(lck) with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs</title><title>Cell</title><description>p56 super(lck), a lymphocyte-specific member of the src family of cytoplasmic protein-tyrosine kinases, is associated noncovalently with the cell surface glycoproteins CD4 and CD8, which are expressed on functionally distinct subpopulations of T cells. Using transient co-expression of p56 super(lck) with CD4 or CD8 alpha in COS-7 cells, we show that the unique N-terminal region of p56 super(lck) binds to the membrane-proximal 10 and 28 cytoplasmic residues of CD8 alpha and CD4, respectively. Two cysteine residues in each of the critical sequences in CD4, CD8 alpha , and p56 super(lck) are required for association. Our results suggest a novel role for cysteine-mediated interactions between unrelated proteins and provide a model for the association of other src -like cytoplasmic kinases with transmembrane proteins.</description><subject>CD4 antigen</subject><subject>CD8 antigen</subject><subject>cysteine</subject><subject>lck</subject><subject>protein p56</subject><issn>0092-8674</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><recordid>eNqNjrtOw0AQRbcAKeHxD1MhKCxtgtc2dQBBQ5U-WtbjZMg-zM5YyP_BB7ORoKe6xbnn6p6ppdYP66pr2nqhLpg_tNadMWapvl-jYLZOKEVIA8gBYYr0OSG8VYUEitZDxv0fn3NiigjHAhhhNA3wNGK-9e54B18kB3CzpNFbDuSgT8FS5JO6eazBxr5kB8QQsCcr2MP7XAwWPK2GJDTwlTofrGe8_s1LdfP8tN28VGNO5RnLLhA79N5GTBPvVqZZrdu2vv938QdAg1mF</recordid><startdate>19900101</startdate><enddate>19900101</enddate><creator>Turner, J M</creator><creator>Brodsky, M H</creator><creator>Irving, BA</creator><creator>Levin, S D</creator><creator>Perlmutter, R M</creator><creator>Littman, DR</creator><scope>7QL</scope><scope>7TO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19900101</creationdate><title>Interaction of the unique N-terminal region of tyrosine kinase p56 super(lck) with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs</title><author>Turner, J M ; Brodsky, M H ; Irving, BA ; Levin, S D ; Perlmutter, R M ; Littman, DR</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_miscellaneous_156127743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>CD4 antigen</topic><topic>CD8 antigen</topic><topic>cysteine</topic><topic>lck</topic><topic>protein p56</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Turner, J M</creatorcontrib><creatorcontrib>Brodsky, M H</creatorcontrib><creatorcontrib>Irving, BA</creatorcontrib><creatorcontrib>Levin, S D</creatorcontrib><creatorcontrib>Perlmutter, R M</creatorcontrib><creatorcontrib>Littman, DR</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Turner, J M</au><au>Brodsky, M H</au><au>Irving, BA</au><au>Levin, S D</au><au>Perlmutter, R M</au><au>Littman, DR</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of the unique N-terminal region of tyrosine kinase p56 super(lck) with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs</atitle><jtitle>Cell</jtitle><date>1990-01-01</date><risdate>1990</risdate><volume>60</volume><issue>5</issue><spage>755</spage><epage>765</epage><pages>755-765</pages><issn>0092-8674</issn><abstract>p56 super(lck), a lymphocyte-specific member of the src family of cytoplasmic protein-tyrosine kinases, is associated noncovalently with the cell surface glycoproteins CD4 and CD8, which are expressed on functionally distinct subpopulations of T cells. Using transient co-expression of p56 super(lck) with CD4 or CD8 alpha in COS-7 cells, we show that the unique N-terminal region of p56 super(lck) binds to the membrane-proximal 10 and 28 cytoplasmic residues of CD8 alpha and CD4, respectively. Two cysteine residues in each of the critical sequences in CD4, CD8 alpha , and p56 super(lck) are required for association. Our results suggest a novel role for cysteine-mediated interactions between unrelated proteins and provide a model for the association of other src -like cytoplasmic kinases with transmembrane proteins.</abstract></addata></record> |
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ispartof | Cell, 1990-01, Vol.60 (5), p.755-765 |
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language | eng |
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source | Elsevier ScienceDirect Journals |
subjects | CD4 antigen CD8 antigen cysteine lck protein p56 |
title | Interaction of the unique N-terminal region of tyrosine kinase p56 super(lck) with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs |
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