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  Simultaneous Assessment of Kinetic, Site-Specific, and Structural Aspects of Enzymatic Protein Phosphorylation

van de Waterbeemd, M., Lössl, P., Gautier, V., Marino, F., Yamashita, M., Conti, E., et al. (2014). Simultaneous Assessment of Kinetic, Site-Specific, and Structural Aspects of Enzymatic Protein Phosphorylation. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 53(36), 9660-9664. doi:10.1002/anie.201404637.

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 Creators:
van de Waterbeemd, Michiel1, Author
Lössl, Philip1, Author
Gautier, Violette1, Author
Marino, Fabio1, Author
Yamashita, Masami2, Author              
Conti, Elena2, Author              
Scholten, Arjen1, Author
Heck, Albert J. R.1, Author
Affiliations:
1external, ou_persistent22              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: NATIVE MASS-SPECTROMETRY; POSTTRANSLATIONAL MODIFICATIONS; KINASE AURORA; PHOSPHOPROTEOMICS; DEGRADATION; MECHANISMS; ANTIBODIES; BIOLOGY; PLK1; BORAanalytical methods; kinase assay; mass spectrometry; protein modifications; protein-protein interactions;
 Abstract: Protein phosphorylation is a widespread process forming the mechanistic basis of cellular signaling. Up to now, different aspects, for example, site-specificity, kinetics, role of co-factors, and structure-function relationships have been typically investigated by multiple techniques that are incompatible with one another. The approach introduced here maximizes the amount of information gained on protein (complex) phosphorylation while minimizing sample handling. Using high-resolution native mass spectrometry on intact protein (assemblies) up to 150 kDa we track the sequential incorporation of phosphate groups and map their localization by peptide LC-MS/MS. On two model systems, the protein kinase G and the interplay between Aurora kinase A and Bora, we demonstrate the simultaneous monitoring of various aspects of the phosphorylation process, namely the effect of different cofactors on PKG autophosphorylation and the interaction of AurA and Bora as both an enzyme-substrate pair and physical binding partners.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000342677000046
DOI: 10.1002/anie.201404637
 Degree: -

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Title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Source Genre: Journal
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Publ. Info: BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY : WILEY-V C H VERLAG GMBH
Pages: - Volume / Issue: 53 (36) Sequence Number: - Start / End Page: 9660 - 9664 Identifier: ISSN: 1433-7851