Triple SILAC identified progestin-independent and dependent PRA and PRB interacting partners in breast cancer

Pateetin, P; Hutvagner, G; Padula, MP; McGowan, EM; Boonyaratanakornkit, V

Triple SILAC identified progestin-independent and dependent PRA and PRB interacting partners in breast cancer

Pateetin, P Hutvagner, G

Padula, MP McGowan, EM Boonyaratanakornkit, V

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Publisher:: NATURE RESEARCH
Publication Type:: Journal Article
Citation:: Scientific Data, 2021, 8, (1), pp. 100
Issue Date:: 2021-04-12

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Field	Value	Language
dc.contributor.author	Pateetin, P
dc.contributor.author	Hutvagner, G https://orcid.org/0000-0002-7231-9446
dc.contributor.author	Padula, MP
dc.contributor.author	McGowan, EM
dc.contributor.author	Boonyaratanakornkit, V
dc.date.accessioned	2022-01-12T01:58:51Z
dc.date.available	2021-02-24
dc.date.available	2022-01-12T01:58:51Z
dc.date.issued	2021-04-12
dc.identifier.citation	Scientific Data, 2021, 8, (1), pp. 100
dc.identifier.issn	2052-4463
dc.identifier.issn	2052-4463
dc.identifier.uri	http://hdl.handle.net/10453/152955
dc.description.abstract	Progesterone receptor (PR) isoforms, PRA and PRB, act in a progesterone-independent and dependent manner to differentially modulate the biology of breast cancer cells. Here we show that the differences in PRA and PRB structure facilitate the binding of common and distinct protein interacting partners affecting the downstream signaling events of each PR-isoform. Tet-inducible HA-tagged PRA or HA-tagged PRB constructs were expressed in T47DC42 (PR/ER negative) breast cancer cells. Affinity purification coupled with stable isotope labeling of amino acids in cell culture (SILAC) mass spectrometry technique was performed to comprehensively study PRA and PRB interacting partners in both unliganded and liganded conditions. To validate our findings, we applied both forward and reverse SILAC conditions to effectively minimize experimental errors. These datasets will be useful in investigating PRA- and PRB-specific molecular mechanisms and as a database for subsequent experiments to identify novel PRA and PRB interacting proteins that differentially mediated different biological functions in breast cancer.
dc.format	Electronic
dc.language	eng
dc.publisher	NATURE RESEARCH
dc.relation.ispartof	Scientific Data
dc.relation.isbasedon	10.1038/s41597-021-00884-0
dc.rights	info:eu-repo/semantics/openAccess
dc.subject.mesh	Amino Acids
dc.subject.mesh	Breast Neoplasms
dc.subject.mesh	Cell Line, Tumor
dc.subject.mesh	Female
dc.subject.mesh	Humans
dc.subject.mesh	Isotope Labeling
dc.subject.mesh	Mass Spectrometry
dc.subject.mesh	Receptors, Progesterone
dc.subject.mesh	Two-Hybrid System Techniques
dc.subject.mesh	Cell Line, Tumor
dc.subject.mesh	Humans
dc.subject.mesh	Breast Neoplasms
dc.subject.mesh	Amino Acids
dc.subject.mesh	Receptors, Progesterone
dc.subject.mesh	Two-Hybrid System Techniques
dc.subject.mesh	Isotope Labeling
dc.subject.mesh	Female
dc.subject.mesh	Mass Spectrometry
dc.title	Triple SILAC identified progestin-independent and dependent PRA and PRB interacting partners in breast cancer
dc.type	Journal Article
utslib.citation.volume	8
utslib.location.activity	England
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Biomedical Engineering
pubs.organisational-group	/University of Technology Sydney/Centre for Health Technologies (CHT)
utslib.copyright.status	open_access	*
dc.date.updated	2022-01-12T01:58:46Z
pubs.issue	1
pubs.publication-status	Published online
pubs.volume	8
utslib.citation.issue	1

Abstract:

Progesterone receptor (PR) isoforms, PRA and PRB, act in a progesterone-independent and dependent manner to differentially modulate the biology of breast cancer cells. Here we show that the differences in PRA and PRB structure facilitate the binding of common and distinct protein interacting partners affecting the downstream signaling events of each PR-isoform. Tet-inducible HA-tagged PRA or HA-tagged PRB constructs were expressed in T47DC42 (PR/ER negative) breast cancer cells. Affinity purification coupled with stable isotope labeling of amino acids in cell culture (SILAC) mass spectrometry technique was performed to comprehensively study PRA and PRB interacting partners in both unliganded and liganded conditions. To validate our findings, we applied both forward and reverse SILAC conditions to effectively minimize experimental errors. These datasets will be useful in investigating PRA- and PRB-specific molecular mechanisms and as a database for subsequent experiments to identify novel PRA and PRB interacting proteins that differentially mediated different biological functions in breast cancer.

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http://hdl.handle.net/10453/152955