Journal Article

DKFZ-2019-00483

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Synthetic phosphopeptides: From spike-in standards to affinity tools for protein-protein interaction studies.

Winter, M. (First author)DKFZ* ; Mayer, R.DKFZ* ; Warnken, U.DKFZ* ; Debus, J.DKFZ* ; Abdollahi, A.DKFZ* ; Schnölzer, M. (Last author)DKFZ*

2019
Elsevier San Diego, Calif.

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Please use a persistent id in citations: doi:10.1016/j.ab.2018.12.018

Abstract: Synthetic isotope labeled phosphopeptides are valuable tools for the quantification and validation of phosphoproteome data. Here, we report that the same set of phosphopeptides, which are used as spike-in standards, can be successfully applied for identification of stimulus specific protein-protein interactions mediated by the respective phosphorylation sites. As a proof-of-concept, binding of two γH2AX (pS139) phosphosite specific interaction partners, MDC1 and 53BP1, was confirmed and elevated binding affinity was revealed in response to ionizing radiation. Our strategy is generally applicable and enables multiplexed validation and functional analysis of phosphorylation sites offering great potential for the follow-up of phosphoproteome studies.

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Contributing Institute(s):

1. Funktionelle Proteomanalyse (B100)
2. KKE Strahlentherapie (E050)
3. Translationale Radioonkologie (E210)
4. DKTK Heidelberg (L101)

Research Program(s):

1. 312 - Functional and structural genomics (POF3-312) (POF3-312)

Appears in the scientific report 2019

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Database coverage:
; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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