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Assembly dynamics and stoichiometry of the apoptosis signal-regulating kinase signalosome in response to electrophile stress

ABSTRACT: The Thermo .RAW files used in Assembly dynamics and stoichiometry of the apoptosis signal-regulating kinase signalosome in response to electrophile stress by Joel D. Federspiel, Simona G. Codreanu, Amy M. Palubinsky, Ama J. Winland, Carlos Morales Betanzos, BethAnn McLaughlin and Daniel C. Liebler are deposited here.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Daniel C Liebler

PROVIDER: MSV000079399 | MassIVE | Wed Dec 02 09:34:00 GMT 2015

REPOSITORIES: MassIVE

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Dynamic phosphorylation of apoptosis signal regulating kinase 1 (ASK1) in response to oxidative and electrophilic stress

Project description:The Thermo .RAW files used in Dynamic phosphorylation of apoptosis signal regulating kinase 1 (ASK1) in response to oxidative and electrophilic stress by Carlos Morales Betanzos, Joel D. Federspiel, Amy M. Palubinsky,BethAnn McLaughlin and Daniel C. Liebler are deposited here.

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Assembly Dynamics and Stoichiometry of the Apoptosis Signal-regulating Kinase (ASK) Signalosome in Response to Electrophile Stress.

Project description:Apoptosis signal-regulating kinase 1 (ASK1) is a key sensor kinase in the mitogen-activated protein kinase pathway that transduces cellular responses to oxidants and electrophiles. ASK1 is regulated by a large, dynamic multiprotein signalosome complex, potentially including over 90 reported ASK1-interacting proteins. We employed both shotgun and targeted mass spectrometry assays to catalogue the ASK1 protein-protein interactions in HEK-293 cells treated with the prototypical lipid electrophile 4-hydroxy-2-nonenal (HNE). Using both epitope-tagged overexpression and endogenous expression cell systems, we verified most of the previously reported ASK1 protein-protein interactions and identified 14 proteins that exhibited dynamic shifts in association with ASK1 in response to HNE stress. We used precise stable isotope dilution assays to quantify protein stoichiometry in the ASK signalosome complex and identified ASK2 at a 1:1 stoichiometric ratio with ASK1 and 14-3-3 proteins (YWHAQ, YWHAB, YWHAH, and YWHAE) collectively at a 0.5:1 ratio with ASK1 as the main components. Several other proteins, including ASK3, PARK7, PRDX1, and USP9X were detected with stoichiometries of 0.1:1 or less. These data support an ASK signalosome comprising a multimeric core complex of ASK1, ASK2, and 14-3-3 proteins, which dynamically engages other binding partners needed to mediate diverse stress-response signaling events. This study further demonstrates the value of combining global and targeted MS approaches to interrogate multiprotein complex composition and dynamics.

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