Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5
dc.contributor.author | Skarra, Dana V. | en_US |
dc.contributor.author | Goudreault, Marilyn | en_US |
dc.contributor.author | Choi, Hyungwon | en_US |
dc.contributor.author | Mullin, Michael | en_US |
dc.contributor.author | Nesvizhskii, Alexey I. | en_US |
dc.contributor.author | Gingras, Anne-Claude | en_US |
dc.contributor.author | Honkanen, Richard E. | en_US |
dc.date.accessioned | 2011-04-07T18:52:40Z | |
dc.date.accessioned | 2011-04-07T18:52:40Z | |
dc.date.available | 2012-05-14T20:40:08Z | en_US |
dc.date.issued | 2011-04 | en_US |
dc.identifier.citation | Skarra, 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.issn | 1615-9853 | en_US |
dc.identifier.issn | 1615-9861 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/83479 | |
dc.description.abstract | Affinity 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.publisher | WILEY-VCH Verlag | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.title | Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5 | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pathology, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Pathology, University of Michigan, Ann Arbor, MI, USA ; Center for Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | Department of Biochemistry and Molecular Biology, University of South Alabama, Mobile, AL, USA ; These authors have contributed equally to this study. | en_US |
dc.contributor.affiliationother | Centre for Systems Biology, Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, Ontario, Canada | en_US |
dc.contributor.affiliationother | Centre for Systems Biology, Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, Ontario, Canada | en_US |
dc.contributor.affiliationother | Centre for Systems Biology, Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, Ontario, Canada ; Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada | en_US |
dc.contributor.affiliationother | Department 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: +1-251-460-6850 | en_US |
dc.identifier.pmid | 21360678 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/83479/1/1508_ftp.pdf | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/83479/2/pmic_201000770_sm_SupplInfo.pdf | |
dc.identifier.doi | 10.1002/pmic.201000770 | en_US |
dc.identifier.source | PROTEOMICS | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.