Proteomic analysis identifies novel binding partners of BAP1.

BRCA1-associated protein 1 (BAP1) is a tumor suppressor and its loss can result in mesothelioma, uveal and cutaneous melanoma, clear cell renal cell carcinoma and bladder cancer. BAP1 is a deubiquitinating enzyme of the UCH class that has been implicated in various cellular processes like cell growt...

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Autores principales:	Roy Baas, Fenna J van der Wal, Onno B Bleijerveld, Haico van Attikum, Titia K Sixma
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b4f6c5532eb64d32882a826fd0eaf7b3
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spelling	oai:doaj.org-article:b4f6c5532eb64d32882a826fd0eaf7b32021-12-02T20:13:58ZProteomic analysis identifies novel binding partners of BAP1.1932-620310.1371/journal.pone.0257688https://doaj.org/article/b4f6c5532eb64d32882a826fd0eaf7b32021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0257688https://doaj.org/toc/1932-6203BRCA1-associated protein 1 (BAP1) is a tumor suppressor and its loss can result in mesothelioma, uveal and cutaneous melanoma, clear cell renal cell carcinoma and bladder cancer. BAP1 is a deubiquitinating enzyme of the UCH class that has been implicated in various cellular processes like cell growth, cell cycle progression, ferroptosis, DNA damage response and ER metabolic stress response. ASXL proteins activate BAP1 by forming the polycomb repressive deubiquitinase (PR-DUB) complex which acts on H2AK119ub1. Besides the ASXL proteins, BAP1 is known to interact with an established set of additional proteins. Here, we identify novel BAP1 interacting proteins in the cytoplasm by expressing GFP-tagged BAP1 in an endogenous BAP1 deficient cell line using affinity purification followed by mass spectrometry (AP-MS) analysis. Among these novel interacting proteins are Histone acetyltransferase 1 (HAT1) and all subunits of the heptameric coat protein complex I (COPI) that is involved in vesicle formation and protein cargo binding and sorting. We validate that the HAT1 and COPI interactions occur at endogenous levels but find that this interaction with COPI is not mediated through the C-terminal KxKxx cargo sorting signals of the COPI complex.Roy BaasFenna J van der WalOnno B BleijerveldHaico van AttikumTitia K SixmaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 9, p e0257688 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Roy Baas Fenna J van der Wal Onno B Bleijerveld Haico van Attikum Titia K Sixma Proteomic analysis identifies novel binding partners of BAP1.
description	BRCA1-associated protein 1 (BAP1) is a tumor suppressor and its loss can result in mesothelioma, uveal and cutaneous melanoma, clear cell renal cell carcinoma and bladder cancer. BAP1 is a deubiquitinating enzyme of the UCH class that has been implicated in various cellular processes like cell growth, cell cycle progression, ferroptosis, DNA damage response and ER metabolic stress response. ASXL proteins activate BAP1 by forming the polycomb repressive deubiquitinase (PR-DUB) complex which acts on H2AK119ub1. Besides the ASXL proteins, BAP1 is known to interact with an established set of additional proteins. Here, we identify novel BAP1 interacting proteins in the cytoplasm by expressing GFP-tagged BAP1 in an endogenous BAP1 deficient cell line using affinity purification followed by mass spectrometry (AP-MS) analysis. Among these novel interacting proteins are Histone acetyltransferase 1 (HAT1) and all subunits of the heptameric coat protein complex I (COPI) that is involved in vesicle formation and protein cargo binding and sorting. We validate that the HAT1 and COPI interactions occur at endogenous levels but find that this interaction with COPI is not mediated through the C-terminal KxKxx cargo sorting signals of the COPI complex.
format	article
author	Roy Baas Fenna J van der Wal Onno B Bleijerveld Haico van Attikum Titia K Sixma
author_facet	Roy Baas Fenna J van der Wal Onno B Bleijerveld Haico van Attikum Titia K Sixma
author_sort	Roy Baas
title	Proteomic analysis identifies novel binding partners of BAP1.
title_short	Proteomic analysis identifies novel binding partners of BAP1.
title_full	Proteomic analysis identifies novel binding partners of BAP1.
title_fullStr	Proteomic analysis identifies novel binding partners of BAP1.
title_full_unstemmed	Proteomic analysis identifies novel binding partners of BAP1.
title_sort	proteomic analysis identifies novel binding partners of bap1.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/b4f6c5532eb64d32882a826fd0eaf7b3
work_keys_str_mv	AT roybaas proteomicanalysisidentifiesnovelbindingpartnersofbap1 AT fennajvanderwal proteomicanalysisidentifiesnovelbindingpartnersofbap1 AT onnobbleijerveld proteomicanalysisidentifiesnovelbindingpartnersofbap1 AT haicovanattikum proteomicanalysisidentifiesnovelbindingpartnersofbap1 AT titiaksixma proteomicanalysisidentifiesnovelbindingpartnersofbap1
_version_	1718374730241671168

Proteomic analysis identifies novel binding partners of BAP1.

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