Tyrosine 192 within the SH2 domain of the Src-protein tyrosine kinase p56Lck regulates T-cell activation independently of Lck/CD45 interactions

Background Upon engagement of the T-cell receptor (TCR), the Src-family protein tyrosine kinase p56Lck phosphorylates components of the TCR (e.g. the TCRζ chains), thereby initiating T-cell activation. The enzymatic activity of Lck is primarily regulated via reversible and dynamic phosphorylation of...

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Veröffentlicht in:Cell communication and signaling 2020-11, Vol.18 (1), p.1, Article 183
Hauptverfasser: Kästle, Matthias, Merten, Camilla, Hartig, Roland, Kaehne, Thilo, Liaunardy-Jopeace, Ardiyanto, Woessner, Nadine M., Schamel, Wolfgang W., James, John, Minguet, Susana, Simeoni, Luca, Schraven, Burkhart
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container_title Cell communication and signaling
container_volume 18
creator Kästle, Matthias
Merten, Camilla
Hartig, Roland
Kaehne, Thilo
Liaunardy-Jopeace, Ardiyanto
Woessner, Nadine M.
Schamel, Wolfgang W.
James, John
Minguet, Susana
Simeoni, Luca
Schraven, Burkhart
description Background Upon engagement of the T-cell receptor (TCR), the Src-family protein tyrosine kinase p56Lck phosphorylates components of the TCR (e.g. the TCRζ chains), thereby initiating T-cell activation. The enzymatic activity of Lck is primarily regulated via reversible and dynamic phosphorylation of two tyrosine residues, Y394 and Y505. Lck possesses an additional highly conserved tyrosine Y192, located within the SH2 domain, whose role in T-cell activation is not fully understood. Methods Knock-in mice expressing a phospho-mimetic (Y192E) form of Lck were generated. Cellular and biochemical characterization was performed to elucidate the function of Y192 in primary T cells. HEK 293T and Jurkat T cells were used for in vitro studies. Results Co-immunoprecipitation studies and biochemical analyses using T cells from LckY192E knock-in mice revealed a diminished binding of LckY192E to CD45 and a concomitant hyperphosphorylation of Y505, thus corroborating previous data obtained in Jurkat T cells. Surprisingly however, in vitro kinase assays showed that LckY192E possesses a normal enzymatic activity in human and murine T cells. FLIM/FRET measurements employing an LckY192E biosensor further indicated that the steady state conformation of the LckY192E mutant is similar to Lckwt. These data suggest that Y192 might regulate Lck functions also independently from the Lck/CD45-association. Indeed, when LckY192E was expressed in CD45−/−/Csk−/− non-T cells (HEK 293T cells), phosphorylation of Y505 was similar to Lckwt, but LckY192E still failed to optimally phosphorylate and activate the Lck downstream substrate ZAP70. Furthermore, LckY19E was recruited less to CD3 after TCR stimulation. Conclusions Taken together, phosphorylation of Y192 regulates Lck functions in T cells at least twofold, by preventing Lck association to CD45 and by modulating ligand-induced recruitment of Lck to the TCR. Major findings Our data change the current view on the function of Y192 and suggest that Y192 also regulates Lck activity in a manner independent of Y505 phosphorylation. Video Abstract
doi_str_mv 10.1186/s12964-020-00673-z
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The enzymatic activity of Lck is primarily regulated via reversible and dynamic phosphorylation of two tyrosine residues, Y394 and Y505. Lck possesses an additional highly conserved tyrosine Y192, located within the SH2 domain, whose role in T-cell activation is not fully understood. Methods Knock-in mice expressing a phospho-mimetic (Y192E) form of Lck were generated. Cellular and biochemical characterization was performed to elucidate the function of Y192 in primary T cells. HEK 293T and Jurkat T cells were used for in vitro studies. Results Co-immunoprecipitation studies and biochemical analyses using T cells from LckY192E knock-in mice revealed a diminished binding of LckY192E to CD45 and a concomitant hyperphosphorylation of Y505, thus corroborating previous data obtained in Jurkat T cells. Surprisingly however, in vitro kinase assays showed that LckY192E possesses a normal enzymatic activity in human and murine T cells. FLIM/FRET measurements employing an LckY192E biosensor further indicated that the steady state conformation of the LckY192E mutant is similar to Lckwt. These data suggest that Y192 might regulate Lck functions also independently from the Lck/CD45-association. Indeed, when LckY192E was expressed in CD45−/−/Csk−/− non-T cells (HEK 293T cells), phosphorylation of Y505 was similar to Lckwt, but LckY192E still failed to optimally phosphorylate and activate the Lck downstream substrate ZAP70. Furthermore, LckY19E was recruited less to CD3 after TCR stimulation. Conclusions Taken together, phosphorylation of Y192 regulates Lck functions in T cells at least twofold, by preventing Lck association to CD45 and by modulating ligand-induced recruitment of Lck to the TCR. Major findings Our data change the current view on the function of Y192 and suggest that Y192 also regulates Lck activity in a manner independent of Y505 phosphorylation. Video Abstract</description><identifier>ISSN: 1478-811X</identifier><identifier>EISSN: 1478-811X</identifier><identifier>DOI: 10.1186/s12964-020-00673-z</identifier><identifier>PMID: 33225946</identifier><language>eng</language><publisher>London: BioMed Central</publisher><subject>Adapter proteins ; Antibodies ; Biosensors ; CD3 antigen ; CD45 antigen ; Cell activation ; Enzymatic activity ; Fluorescence resonance energy transfer ; Immunoprecipitation ; Kinases ; Lck protein ; Ligands ; Lymphocytes ; Lymphocytes T ; Phosphatase ; Phosphorylation ; Plasmids ; Protein-tyrosine kinase ; Src protein ; T cell receptors ; ZAP-70 protein</subject><ispartof>Cell communication and signaling, 2020-11, Vol.18 (1), p.1, Article 183</ispartof><rights>2020. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>The Author(s) 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c219z-598503dc327c5b88e61b872d47f3a87b3e6a9d5e0a884ee4f5fe0865a4943dab3</citedby><cites>FETCH-LOGICAL-c219z-598503dc327c5b88e61b872d47f3a87b3e6a9d5e0a884ee4f5fe0865a4943dab3</cites><orcidid>0000-0003-4321-7405</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7682018/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7682018/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,53791,53793</link.rule.ids></links><search><creatorcontrib>Kästle, Matthias</creatorcontrib><creatorcontrib>Merten, Camilla</creatorcontrib><creatorcontrib>Hartig, Roland</creatorcontrib><creatorcontrib>Kaehne, Thilo</creatorcontrib><creatorcontrib>Liaunardy-Jopeace, Ardiyanto</creatorcontrib><creatorcontrib>Woessner, Nadine M.</creatorcontrib><creatorcontrib>Schamel, Wolfgang W.</creatorcontrib><creatorcontrib>James, John</creatorcontrib><creatorcontrib>Minguet, Susana</creatorcontrib><creatorcontrib>Simeoni, Luca</creatorcontrib><creatorcontrib>Schraven, Burkhart</creatorcontrib><title>Tyrosine 192 within the SH2 domain of the Src-protein tyrosine kinase p56Lck regulates T-cell activation independently of Lck/CD45 interactions</title><title>Cell communication and signaling</title><description>Background Upon engagement of the T-cell receptor (TCR), the Src-family protein tyrosine kinase p56Lck phosphorylates components of the TCR (e.g. the TCRζ chains), thereby initiating T-cell activation. The enzymatic activity of Lck is primarily regulated via reversible and dynamic phosphorylation of two tyrosine residues, Y394 and Y505. Lck possesses an additional highly conserved tyrosine Y192, located within the SH2 domain, whose role in T-cell activation is not fully understood. Methods Knock-in mice expressing a phospho-mimetic (Y192E) form of Lck were generated. Cellular and biochemical characterization was performed to elucidate the function of Y192 in primary T cells. HEK 293T and Jurkat T cells were used for in vitro studies. Results Co-immunoprecipitation studies and biochemical analyses using T cells from LckY192E knock-in mice revealed a diminished binding of LckY192E to CD45 and a concomitant hyperphosphorylation of Y505, thus corroborating previous data obtained in Jurkat T cells. Surprisingly however, in vitro kinase assays showed that LckY192E possesses a normal enzymatic activity in human and murine T cells. FLIM/FRET measurements employing an LckY192E biosensor further indicated that the steady state conformation of the LckY192E mutant is similar to Lckwt. These data suggest that Y192 might regulate Lck functions also independently from the Lck/CD45-association. Indeed, when LckY192E was expressed in CD45−/−/Csk−/− non-T cells (HEK 293T cells), phosphorylation of Y505 was similar to Lckwt, but LckY192E still failed to optimally phosphorylate and activate the Lck downstream substrate ZAP70. Furthermore, LckY19E was recruited less to CD3 after TCR stimulation. Conclusions Taken together, phosphorylation of Y192 regulates Lck functions in T cells at least twofold, by preventing Lck association to CD45 and by modulating ligand-induced recruitment of Lck to the TCR. Major findings Our data change the current view on the function of Y192 and suggest that Y192 also regulates Lck activity in a manner independent of Y505 phosphorylation. 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Merten, Camilla ; Hartig, Roland ; Kaehne, Thilo ; Liaunardy-Jopeace, Ardiyanto ; Woessner, Nadine M. ; Schamel, Wolfgang W. ; James, John ; Minguet, Susana ; Simeoni, Luca ; Schraven, Burkhart</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c219z-598503dc327c5b88e61b872d47f3a87b3e6a9d5e0a884ee4f5fe0865a4943dab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Adapter proteins</topic><topic>Antibodies</topic><topic>Biosensors</topic><topic>CD3 antigen</topic><topic>CD45 antigen</topic><topic>Cell activation</topic><topic>Enzymatic activity</topic><topic>Fluorescence resonance energy transfer</topic><topic>Immunoprecipitation</topic><topic>Kinases</topic><topic>Lck protein</topic><topic>Ligands</topic><topic>Lymphocytes</topic><topic>Lymphocytes T</topic><topic>Phosphatase</topic><topic>Phosphorylation</topic><topic>Plasmids</topic><topic>Protein-tyrosine kinase</topic><topic>Src protein</topic><topic>T cell receptors</topic><topic>ZAP-70 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kästle, Matthias</creatorcontrib><creatorcontrib>Merten, Camilla</creatorcontrib><creatorcontrib>Hartig, Roland</creatorcontrib><creatorcontrib>Kaehne, Thilo</creatorcontrib><creatorcontrib>Liaunardy-Jopeace, Ardiyanto</creatorcontrib><creatorcontrib>Woessner, Nadine M.</creatorcontrib><creatorcontrib>Schamel, Wolfgang W.</creatorcontrib><creatorcontrib>James, John</creatorcontrib><creatorcontrib>Minguet, Susana</creatorcontrib><creatorcontrib>Simeoni, Luca</creatorcontrib><creatorcontrib>Schraven, Burkhart</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium &amp; 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The enzymatic activity of Lck is primarily regulated via reversible and dynamic phosphorylation of two tyrosine residues, Y394 and Y505. Lck possesses an additional highly conserved tyrosine Y192, located within the SH2 domain, whose role in T-cell activation is not fully understood. Methods Knock-in mice expressing a phospho-mimetic (Y192E) form of Lck were generated. Cellular and biochemical characterization was performed to elucidate the function of Y192 in primary T cells. HEK 293T and Jurkat T cells were used for in vitro studies. Results Co-immunoprecipitation studies and biochemical analyses using T cells from LckY192E knock-in mice revealed a diminished binding of LckY192E to CD45 and a concomitant hyperphosphorylation of Y505, thus corroborating previous data obtained in Jurkat T cells. Surprisingly however, in vitro kinase assays showed that LckY192E possesses a normal enzymatic activity in human and murine T cells. FLIM/FRET measurements employing an LckY192E biosensor further indicated that the steady state conformation of the LckY192E mutant is similar to Lckwt. These data suggest that Y192 might regulate Lck functions also independently from the Lck/CD45-association. Indeed, when LckY192E was expressed in CD45−/−/Csk−/− non-T cells (HEK 293T cells), phosphorylation of Y505 was similar to Lckwt, but LckY192E still failed to optimally phosphorylate and activate the Lck downstream substrate ZAP70. Furthermore, LckY19E was recruited less to CD3 after TCR stimulation. Conclusions Taken together, phosphorylation of Y192 regulates Lck functions in T cells at least twofold, by preventing Lck association to CD45 and by modulating ligand-induced recruitment of Lck to the TCR. Major findings Our data change the current view on the function of Y192 and suggest that Y192 also regulates Lck activity in a manner independent of Y505 phosphorylation. 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subjects Adapter proteins
Antibodies
Biosensors
CD3 antigen
CD45 antigen
Cell activation
Enzymatic activity
Fluorescence resonance energy transfer
Immunoprecipitation
Kinases
Lck protein
Ligands
Lymphocytes
Lymphocytes T
Phosphatase
Phosphorylation
Plasmids
Protein-tyrosine kinase
Src protein
T cell receptors
ZAP-70 protein
title Tyrosine 192 within the SH2 domain of the Src-protein tyrosine kinase p56Lck regulates T-cell activation independently of Lck/CD45 interactions
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