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Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5

dc.contributor.authorSkarra, Dana V.en_US
dc.contributor.authorGoudreault, Marilynen_US
dc.contributor.authorChoi, Hyungwonen_US
dc.contributor.authorMullin, Michaelen_US
dc.contributor.authorNesvizhskii, Alexey I.en_US
dc.contributor.authorGingras, Anne-Claudeen_US
dc.contributor.authorHonkanen, Richard E.en_US
dc.date.accessioned2011-04-07T18:52:40Z
dc.date.accessioned2011-04-07T18:52:40Z
dc.date.available2012-05-14T20:40:08Zen_US
dc.date.issued2011-04en_US
dc.identifier.citationSkarra, Dana V.; Goudreault, Marilyn; Choi, Hyungwon; Mullin, Michael; Nesvizhskii, Alexey I.; Gingras, Anne-Claude; Honkanen, Richard E. (2011). "Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5." PROTEOMICS 11(8): 1508-1516. <http://hdl.handle.net/2027.42/83479>en_US
dc.identifier.issn1615-9853en_US
dc.identifier.issn1615-9861en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/83479
dc.description.abstractAffinity purification coupled to mass spectrometry (AP-MS) represents a powerful and proven approach for the analysis of protein–protein interactions. However, the detection of true interactions for proteins that are commonly considered background contaminants is currently a limitation of AP-MS. Here using spectral counts and the new statistical tool, Significance Analysis of INTeractome (SAINT), true interaction between the serine/threonine protein phosphatase 5 (PP5) and a chaperonin, heat shock protein 90 (Hsp90), is discerned. Furthermore, we report and validate a new interaction between PP5 and an Hsp90 adaptor protein, stress-induced phosphoprotein 1 (STIP1; HOP). Mutation of PP5, replacing key basic amino acids (K97A and R101A) in the tetratricopeptide repeat (TPR) region known to be necessary for the interactions with Hsp90, abolished both the known interaction of PP5 with cell division cycle 37 homolog and the novel interaction of PP5 with stress-induced phosphoprotein 1. Taken together, the results presented demonstrate the usefulness of label-free quantitative proteomics and statistical tools to discriminate between noise and true interactions, even for proteins normally considered as background contaminants.en_US
dc.publisherWILEY-VCH Verlagen_US
dc.subject.otherLife and Medical Sciencesen_US
dc.titleLabel-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Pathology, University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Pathology, University of Michigan, Ann Arbor, MI, USA ; Center for Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationotherDepartment of Biochemistry and Molecular Biology, University of South Alabama, Mobile, AL, USA ; These authors have contributed equally to this study.en_US
dc.contributor.affiliationotherCentre for Systems Biology, Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, Ontario, Canadaen_US
dc.contributor.affiliationotherCentre for Systems Biology, Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, Ontario, Canadaen_US
dc.contributor.affiliationotherCentre for Systems Biology, Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, Ontario, Canada ; Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canadaen_US
dc.contributor.affiliationotherDepartment of Biochemistry and Molecular Biology, University of South Alabama, Mobile, AL, USA ; Department of Clinical Science and Education, Karolinska Institute, Stockholm, Sweden ; Department of Biochemistry and Molecular Biology, University of South Alabama, 307 University BLVD N, Mobile, AL 36688, USA Fax: +1-251-460-6850en_US
dc.identifier.pmid21360678en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/83479/1/1508_ftp.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/83479/2/pmic_201000770_sm_SupplInfo.pdf
dc.identifier.doi10.1002/pmic.201000770en_US
dc.identifier.sourcePROTEOMICSen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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