Detailed Information on Publication Record
2018
Analysis of binding interfaces of the human scaffold protein AXIN1 by peptide microarrays
HARNOŠ, Jakub, Jan RYNEŠ, Pavlína VÍŠKOVÁ, Silvie TRANTÍRKOVÁ, Lola Murielle BAJARD ÉP.ESNER et. al.Basic information
Original name
Analysis of binding interfaces of the human scaffold protein AXIN1 by peptide microarrays
Authors
HARNOŠ, Jakub (203 Czech Republic, belonging to the institution), Jan RYNEŠ (203 Czech Republic, belonging to the institution), Pavlína VÍŠKOVÁ (203 Czech Republic, belonging to the institution), Silvie TRANTÍRKOVÁ (203 Czech Republic, belonging to the institution), Lola Murielle BAJARD ÉP.ESNER (250 France, belonging to the institution), Lukáš TRANTÍREK (203 Czech Republic, belonging to the institution) and Vítězslav BRYJA (203 Czech Republic, guarantor, belonging to the institution)
Edition
Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2018, 0021-9258
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.106
RIV identification code
RIV/00216224:14310/18:00101698
Organization unit
Faculty of Science
UT WoS
000447833600018
Keywords in English
peptide array; scaffold protein; axin; serine; threonine protein kinase; p53; Myc (c-Myc); casein kinase 1E; dishevelled; intrinsically disordered region; Wnt pathway
Tags
Tags
International impact, Reviewed
Změněno: 26/3/2019 13:07, Mgr. Pavla Foltynová, Ph.D.
Abstract
V originále
Intrinsically disordered regions (IDRs) are protein regions that lack persistent secondary or tertiary structure under native conditions. IDRs represent >40% of the eukaryotic proteome and play a crucial role in protein-protein interactions. The classical approach for identification of these interaction interfaces is based on mutagenesis combined with biochemical techniques such as coimmunoprecipitation or yeast two-hybrid screening. This approach either provides information of low resolution (large deletions) or very laboriously tries to precisely define the binding epitope via single amino acid substitutions. Here, we report the use of a peptide microarray based on the human scaffold protein AXIN1 for high-throughput and -resolution mapping of binding sites for several AXIN1 interaction partners in vitro. For each of the AXIN1-binding partners tested, i.e. casein kinase 1 E (CK1E); c-Myc; peptidyl-prolyl cis/trans isomerase, NIMA-interacting 1 (Pin1); and p53, we found at least three different epitopes, predominantly in the central IDR of AXIN1. We functionally validated the specific AXIN1-CK1E interaction identified here with epitope-mimicking peptides and with AXIN1 variants having deletions of short binding epitopes. On the basis of these results, we propose a model in which AXIN1 competes with dishevelled (DVL) for CK1E and regulates CK1E-induced phosphorylation of DVL and activation of Wnt/-catenin signaling.
Links
| GA17-12075S, research and development project |
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| GA18-17658S, research and development project |
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| GJ15-22380Y, research and development project |
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| LQ1601, research and development project |
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| MUNI/A/1145/2017, interní kód MU |
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| MUNI/G/1100/2016, interní kód MU |
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| NV15-34405A, research and development project |
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