Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.

Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of...
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Autor*in:	Nitika [verfasserIn] Bo Zheng [verfasserIn] Linhao Ruan [verfasserIn] Jake T Kline [verfasserIn] Siddhi Omkar [verfasserIn] Jacek Sikora [verfasserIn] Mara Texeira Torres [verfasserIn] Yuhao Wang [verfasserIn] Jade E Takakuwa [verfasserIn] Romain Huguet [verfasserIn] Cinzia Klemm [verfasserIn] Verónica A Segarra [verfasserIn] Matthew J Winters [verfasserIn] Peter M Pryciak [verfasserIn] Peter H Thorpe [verfasserIn] Kazuo Tatebayashi [verfasserIn] Rong Li [verfasserIn] Luca Fornelli [verfasserIn] Andrew W Truman [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Übergeordnetes Werk:	In: PLoS Biology - Public Library of Science (PLoS), 2003, 20(2022), 10, p e3001839
Übergeordnetes Werk:	volume:20 ; year:2022 ; number:10, p e3001839

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.1371/journal.pbio.3001839

Katalog-ID:	DOAJ028974239

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520			\|a Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins.
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912			\|a GBV_ILN_4325
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allfields	10.1371/journal.pbio.3001839 doi (DE-627)DOAJ028974239 (DE-599)DOAJ59fc76cc577d413db19b096830ece4f5 DE-627 ger DE-627 rakwb eng QH301-705.5 Nitika verfasserin aut Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications. 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins. Biology (General) Bo Zheng verfasserin aut Linhao Ruan verfasserin aut Jake T Kline verfasserin aut Siddhi Omkar verfasserin aut Jacek Sikora verfasserin aut Mara Texeira Torres verfasserin aut Yuhao Wang verfasserin aut Jade E Takakuwa verfasserin aut Romain Huguet verfasserin aut Cinzia Klemm verfasserin aut Verónica A Segarra verfasserin aut Matthew J Winters verfasserin aut Peter M Pryciak verfasserin aut Peter H Thorpe verfasserin aut Kazuo Tatebayashi verfasserin aut Rong Li verfasserin aut Luca Fornelli verfasserin aut Andrew W Truman verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 20(2022), 10, p e3001839 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:20 year:2022 number:10, p e3001839 https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/article/59fc76cc577d413db19b096830ece4f5 kostenfrei https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2022 10, p e3001839
spelling	10.1371/journal.pbio.3001839 doi (DE-627)DOAJ028974239 (DE-599)DOAJ59fc76cc577d413db19b096830ece4f5 DE-627 ger DE-627 rakwb eng QH301-705.5 Nitika verfasserin aut Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications. 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins. Biology (General) Bo Zheng verfasserin aut Linhao Ruan verfasserin aut Jake T Kline verfasserin aut Siddhi Omkar verfasserin aut Jacek Sikora verfasserin aut Mara Texeira Torres verfasserin aut Yuhao Wang verfasserin aut Jade E Takakuwa verfasserin aut Romain Huguet verfasserin aut Cinzia Klemm verfasserin aut Verónica A Segarra verfasserin aut Matthew J Winters verfasserin aut Peter M Pryciak verfasserin aut Peter H Thorpe verfasserin aut Kazuo Tatebayashi verfasserin aut Rong Li verfasserin aut Luca Fornelli verfasserin aut Andrew W Truman verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 20(2022), 10, p e3001839 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:20 year:2022 number:10, p e3001839 https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/article/59fc76cc577d413db19b096830ece4f5 kostenfrei https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2022 10, p e3001839
allfields_unstemmed	10.1371/journal.pbio.3001839 doi (DE-627)DOAJ028974239 (DE-599)DOAJ59fc76cc577d413db19b096830ece4f5 DE-627 ger DE-627 rakwb eng QH301-705.5 Nitika verfasserin aut Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications. 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins. Biology (General) Bo Zheng verfasserin aut Linhao Ruan verfasserin aut Jake T Kline verfasserin aut Siddhi Omkar verfasserin aut Jacek Sikora verfasserin aut Mara Texeira Torres verfasserin aut Yuhao Wang verfasserin aut Jade E Takakuwa verfasserin aut Romain Huguet verfasserin aut Cinzia Klemm verfasserin aut Verónica A Segarra verfasserin aut Matthew J Winters verfasserin aut Peter M Pryciak verfasserin aut Peter H Thorpe verfasserin aut Kazuo Tatebayashi verfasserin aut Rong Li verfasserin aut Luca Fornelli verfasserin aut Andrew W Truman verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 20(2022), 10, p e3001839 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:20 year:2022 number:10, p e3001839 https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/article/59fc76cc577d413db19b096830ece4f5 kostenfrei https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2022 10, p e3001839
allfieldsGer	10.1371/journal.pbio.3001839 doi (DE-627)DOAJ028974239 (DE-599)DOAJ59fc76cc577d413db19b096830ece4f5 DE-627 ger DE-627 rakwb eng QH301-705.5 Nitika verfasserin aut Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications. 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins. Biology (General) Bo Zheng verfasserin aut Linhao Ruan verfasserin aut Jake T Kline verfasserin aut Siddhi Omkar verfasserin aut Jacek Sikora verfasserin aut Mara Texeira Torres verfasserin aut Yuhao Wang verfasserin aut Jade E Takakuwa verfasserin aut Romain Huguet verfasserin aut Cinzia Klemm verfasserin aut Verónica A Segarra verfasserin aut Matthew J Winters verfasserin aut Peter M Pryciak verfasserin aut Peter H Thorpe verfasserin aut Kazuo Tatebayashi verfasserin aut Rong Li verfasserin aut Luca Fornelli verfasserin aut Andrew W Truman verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 20(2022), 10, p e3001839 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:20 year:2022 number:10, p e3001839 https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/article/59fc76cc577d413db19b096830ece4f5 kostenfrei https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2022 10, p e3001839
allfieldsSound	10.1371/journal.pbio.3001839 doi (DE-627)DOAJ028974239 (DE-599)DOAJ59fc76cc577d413db19b096830ece4f5 DE-627 ger DE-627 rakwb eng QH301-705.5 Nitika verfasserin aut Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications. 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins. Biology (General) Bo Zheng verfasserin aut Linhao Ruan verfasserin aut Jake T Kline verfasserin aut Siddhi Omkar verfasserin aut Jacek Sikora verfasserin aut Mara Texeira Torres verfasserin aut Yuhao Wang verfasserin aut Jade E Takakuwa verfasserin aut Romain Huguet verfasserin aut Cinzia Klemm verfasserin aut Verónica A Segarra verfasserin aut Matthew J Winters verfasserin aut Peter M Pryciak verfasserin aut Peter H Thorpe verfasserin aut Kazuo Tatebayashi verfasserin aut Rong Li verfasserin aut Luca Fornelli verfasserin aut Andrew W Truman verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 20(2022), 10, p e3001839 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:20 year:2022 number:10, p e3001839 https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/article/59fc76cc577d413db19b096830ece4f5 kostenfrei https://doi.org/10.1371/journal.pbio.3001839 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 20 2022 10, p e3001839
language	English
source	In PLoS Biology 20(2022), 10, p e3001839 volume:20 year:2022 number:10, p e3001839
sourceStr	In PLoS Biology 20(2022), 10, p e3001839 volume:20 year:2022 number:10, p e3001839
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Biology (General)
isfreeaccess_bool	true
container_title	PLoS Biology
authorswithroles_txt_mv	Nitika @@aut@@ Bo Zheng @@aut@@ Linhao Ruan @@aut@@ Jake T Kline @@aut@@ Siddhi Omkar @@aut@@ Jacek Sikora @@aut@@ Mara Texeira Torres @@aut@@ Yuhao Wang @@aut@@ Jade E Takakuwa @@aut@@ Romain Huguet @@aut@@ Cinzia Klemm @@aut@@ Verónica A Segarra @@aut@@ Matthew J Winters @@aut@@ Peter M Pryciak @@aut@@ Peter H Thorpe @@aut@@ Kazuo Tatebayashi @@aut@@ Rong Li @@aut@@ Luca Fornelli @@aut@@ Andrew W Truman @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	373755597
id	DOAJ028974239
language_de	englisch
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topic_title	QH301-705.5 Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications
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title	Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.
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title_sort	comprehensive characterization of the hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications
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title_auth	Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.
abstract	Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins.
abstractGer	Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins.
abstract_unstemmed	Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins.
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title_short	Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.
url	https://doi.org/10.1371/journal.pbio.3001839 https://doaj.org/article/59fc76cc577d413db19b096830ece4f5 https://doaj.org/toc/1544-9173 https://doaj.org/toc/1545-7885
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Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.

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