Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling

Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes...
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Autor*in:	Sumana Sanyal [verfasserIn] Akhee S. Jahan Hidde L. Ploegh Christopher S. Theile Ying Fan Roberto Bruzzone Mart M. Lamers Fikadu G. Tafesse Eric Spooner Lee Kim Swee Maxime Lestra

Format:	Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	Genomes Proteins Phosphorylation T cell receptors Rodents

Übergeordnetes Werk:	Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 113(2016), 6, Seite E705
Übergeordnetes Werk:	volume:113 ; year:2016 ; number:6 ; pages:E705

Links:	Volltext Link aufrufen Link aufrufen Link aufrufen

DOI / URN:	10.1073/pnas.1521763113

Katalog-ID:	OLC1972281666

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520			\|a Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades.
650		4	\|a Genomes
650		4	\|a Proteins
650		4	\|a Phosphorylation
650		4	\|a T cell receptors
650		4	\|a Rodents
700	0		\|a Akhee S. Jahan \|4 oth
700	0		\|a Hidde L. Ploegh \|4 oth
700	0		\|a Christopher S. Theile \|4 oth
700	0		\|a Ying Fan \|4 oth
700	0		\|a Roberto Bruzzone \|4 oth
700	0		\|a Mart M. Lamers \|4 oth
700	0		\|a Fikadu G. Tafesse \|4 oth
700	0		\|a Eric Spooner \|4 oth
700	0		\|a Lee Kim Swee \|4 oth
700	0		\|a Maxime Lestra \|4 oth
773	0	8	\|i Enthalten in \|t Proceedings of the National Academy of Sciences of the United States of America \|d Washington, DC : NAS, 1877 \|g 113(2016), 6, Seite E705 \|w (DE-627)129505269 \|w (DE-600)209104-5 \|w (DE-576)014909189 \|x 0027-8424 \|7 nnns
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856	4	2	\|u http://www.pnas.org/content/113/6/E705.abstract
856	4	2	\|u http://www.ncbi.nlm.nih.gov/pubmed/26811477
856	4	2	\|u http://search.proquest.com/docview/1767703945
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allfields	10.1073/pnas.1521763113 doi PQ20160307 (DE-627)OLC1972281666 (DE-599)GBVOLC1972281666 (PRQ)p980-75909affbc1edca8e67ec53b2cad96a56a61687bb06263e24800074e4f1be61f0 (KEY)0583363920160000113000600705usp12stabilizesthetcellreceptorcomplexatthecellsur DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Sumana Sanyal verfasserin aut Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades. Genomes Proteins Phosphorylation T cell receptors Rodents Akhee S. Jahan oth Hidde L. Ploegh oth Christopher S. Theile oth Ying Fan oth Roberto Bruzzone oth Mart M. Lamers oth Fikadu G. Tafesse oth Eric Spooner oth Lee Kim Swee oth Maxime Lestra oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 6, Seite E705 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:6 pages:E705 http://dx.doi.org/10.1073/pnas.1521763113 Volltext http://www.pnas.org/content/113/6/E705.abstract http://www.ncbi.nlm.nih.gov/pubmed/26811477 http://search.proquest.com/docview/1767703945 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 6 E705
spelling	10.1073/pnas.1521763113 doi PQ20160307 (DE-627)OLC1972281666 (DE-599)GBVOLC1972281666 (PRQ)p980-75909affbc1edca8e67ec53b2cad96a56a61687bb06263e24800074e4f1be61f0 (KEY)0583363920160000113000600705usp12stabilizesthetcellreceptorcomplexatthecellsur DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Sumana Sanyal verfasserin aut Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades. Genomes Proteins Phosphorylation T cell receptors Rodents Akhee S. Jahan oth Hidde L. Ploegh oth Christopher S. Theile oth Ying Fan oth Roberto Bruzzone oth Mart M. Lamers oth Fikadu G. Tafesse oth Eric Spooner oth Lee Kim Swee oth Maxime Lestra oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 6, Seite E705 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:6 pages:E705 http://dx.doi.org/10.1073/pnas.1521763113 Volltext http://www.pnas.org/content/113/6/E705.abstract http://www.ncbi.nlm.nih.gov/pubmed/26811477 http://search.proquest.com/docview/1767703945 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 6 E705
allfields_unstemmed	10.1073/pnas.1521763113 doi PQ20160307 (DE-627)OLC1972281666 (DE-599)GBVOLC1972281666 (PRQ)p980-75909affbc1edca8e67ec53b2cad96a56a61687bb06263e24800074e4f1be61f0 (KEY)0583363920160000113000600705usp12stabilizesthetcellreceptorcomplexatthecellsur DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Sumana Sanyal verfasserin aut Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades. Genomes Proteins Phosphorylation T cell receptors Rodents Akhee S. Jahan oth Hidde L. Ploegh oth Christopher S. Theile oth Ying Fan oth Roberto Bruzzone oth Mart M. Lamers oth Fikadu G. Tafesse oth Eric Spooner oth Lee Kim Swee oth Maxime Lestra oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 6, Seite E705 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:6 pages:E705 http://dx.doi.org/10.1073/pnas.1521763113 Volltext http://www.pnas.org/content/113/6/E705.abstract http://www.ncbi.nlm.nih.gov/pubmed/26811477 http://search.proquest.com/docview/1767703945 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 6 E705
allfieldsGer	10.1073/pnas.1521763113 doi PQ20160307 (DE-627)OLC1972281666 (DE-599)GBVOLC1972281666 (PRQ)p980-75909affbc1edca8e67ec53b2cad96a56a61687bb06263e24800074e4f1be61f0 (KEY)0583363920160000113000600705usp12stabilizesthetcellreceptorcomplexatthecellsur DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Sumana Sanyal verfasserin aut Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades. Genomes Proteins Phosphorylation T cell receptors Rodents Akhee S. Jahan oth Hidde L. Ploegh oth Christopher S. Theile oth Ying Fan oth Roberto Bruzzone oth Mart M. Lamers oth Fikadu G. Tafesse oth Eric Spooner oth Lee Kim Swee oth Maxime Lestra oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 6, Seite E705 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:6 pages:E705 http://dx.doi.org/10.1073/pnas.1521763113 Volltext http://www.pnas.org/content/113/6/E705.abstract http://www.ncbi.nlm.nih.gov/pubmed/26811477 http://search.proquest.com/docview/1767703945 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 6 E705
allfieldsSound	10.1073/pnas.1521763113 doi PQ20160307 (DE-627)OLC1972281666 (DE-599)GBVOLC1972281666 (PRQ)p980-75909affbc1edca8e67ec53b2cad96a56a61687bb06263e24800074e4f1be61f0 (KEY)0583363920160000113000600705usp12stabilizesthetcellreceptorcomplexatthecellsur DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Sumana Sanyal verfasserin aut Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades. Genomes Proteins Phosphorylation T cell receptors Rodents Akhee S. Jahan oth Hidde L. Ploegh oth Christopher S. Theile oth Ying Fan oth Roberto Bruzzone oth Mart M. Lamers oth Fikadu G. Tafesse oth Eric Spooner oth Lee Kim Swee oth Maxime Lestra oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 113(2016), 6, Seite E705 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:113 year:2016 number:6 pages:E705 http://dx.doi.org/10.1073/pnas.1521763113 Volltext http://www.pnas.org/content/113/6/E705.abstract http://www.ncbi.nlm.nih.gov/pubmed/26811477 http://search.proquest.com/docview/1767703945 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 113 2016 6 E705
language	English
source	Enthalten in Proceedings of the National Academy of Sciences of the United States of America 113(2016), 6, Seite E705 volume:113 year:2016 number:6 pages:E705
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topic_facet	Genomes Proteins Phosphorylation T cell receptors Rodents
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authorswithroles_txt_mv	Sumana Sanyal @@aut@@ Akhee S. Jahan @@oth@@ Hidde L. Ploegh @@oth@@ Christopher S. Theile @@oth@@ Ying Fan @@oth@@ Roberto Bruzzone @@oth@@ Mart M. Lamers @@oth@@ Fikadu G. Tafesse @@oth@@ Eric Spooner @@oth@@ Lee Kim Swee @@oth@@ Maxime Lestra @@oth@@
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author	Sumana Sanyal
spellingShingle	Sumana Sanyal ddc 500 ddc 570 fid LING fid BIODIV misc Genomes misc Proteins misc Phosphorylation misc T cell receptors misc Rodents Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling
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topic_title	500 DNB 570 AVZ LING fid BIODIV fid Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling Genomes Proteins Phosphorylation T cell receptors Rodents
topic	ddc 500 ddc 570 fid LING fid BIODIV misc Genomes misc Proteins misc Phosphorylation misc T cell receptors misc Rodents
topic_unstemmed	ddc 500 ddc 570 fid LING fid BIODIV misc Genomes misc Proteins misc Phosphorylation misc T cell receptors misc Rodents
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title	Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling
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title_full	Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling
author_sort	Sumana Sanyal
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title_sort	usp12 stabilizes the t-cell receptor complex at the cell surface during signaling
title_auth	Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling
abstract	Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades.
abstractGer	Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades.
abstract_unstemmed	Posttranslational modifications are central to the spatial and temporal regulation of protein function. Among others, phosphorylation and ubiquitylation are known to regulate proximal T-cell receptor (TCR) signaling. Here we used a systematic and unbiased approach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary mouse T lymphocytes. Using a C-terminally modified vinyl methyl ester variant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on TCR activation. We identified ubiquitin-specific peptidase (Usp) 12 and Usp46, which had not been previously described in this pathway. Stimulation with anti-CD3 resulted in phosphorylation and time-dependent translocation of Usp12 from the nucleus to the cytosol. Usp12(-/-) Jurkat cells displayed defective NFκB, NFAT, and MAPK activities owing to attenuated surface expression of TCR, which were rescued on reconstitution of wild type Usp12. Proximity-based labeling with BirA-Usp12 revealed several TCR adaptor proteins acting as interactors in stimulated cells, of which LAT and Trat1 displayed reduced expression in Usp12(-/-) cells. We demonstrate that Usp12 deubiquitylates and prevents lysosomal degradation of LAT and Trat1 to maintain the proximal TCR complex for the duration of signaling. Our approach benefits from the use of activity-based probes in primary cells without any previous genome modification, and underscores the importance of ubiquitin-mediated regulation to refine signaling cascades.
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container_issue	6
title_short	Usp12 stabilizes the T-cell receptor complex at the cell surface during signaling
url	http://dx.doi.org/10.1073/pnas.1521763113 http://www.pnas.org/content/113/6/E705.abstract http://www.ncbi.nlm.nih.gov/pubmed/26811477 http://search.proquest.com/docview/1767703945
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author2	Akhee S. Jahan Hidde L. Ploegh Christopher S. Theile Ying Fan Roberto Bruzzone Mart M. Lamers Fikadu G. Tafesse Eric Spooner Lee Kim Swee Maxime Lestra
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up_date	2024-07-03T22:53:51.032Z
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