HARNOŠ, Jakub, Jan RYNEŠ, Pavlína VÍŠKOVÁ, Silvie TRANTÍRKOVÁ, Lola Murielle BAJARD ÉP.ESNER, Lukáš TRANTÍREK and Vítězslav BRYJA. Analysis of binding interfaces of the human scaffold protein AXIN1 by peptide microarrays. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2018, vol. 293, No 42, p. 16337-16347. ISSN 0021-9258. Available from: https://dx.doi.org/10.1074/jbc.RA118.005127. |
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@article{1495637, author = {Harnoš, Jakub and Ryneš, Jan and Víšková, Pavlína and Trantírková, Silvie and Bajard ép.Esner, Lola Murielle and Trantírek, Lukáš and Bryja, Vítězslav}, article_location = {Bethesda, USA}, article_number = {42}, doi = {http://dx.doi.org/10.1074/jbc.RA118.005127}, keywords = {peptide array; scaffold protein; axin; serine; threonine protein kinase; p53; Myc (c-Myc); casein kinase 1E; dishevelled; intrinsically disordered region; Wnt pathway}, language = {eng}, issn = {0021-9258}, journal = {Journal of Biological Chemistry}, title = {Analysis of binding interfaces of the human scaffold protein AXIN1 by peptide microarrays}, url = {http://www.jbc.org/content/293/42/16337}, volume = {293}, year = {2018} }
TY - JOUR ID - 1495637 AU - Harnoš, Jakub - Ryneš, Jan - Víšková, Pavlína - Trantírková, Silvie - Bajard ép.Esner, Lola Murielle - Trantírek, Lukáš - Bryja, Vítězslav PY - 2018 TI - Analysis of binding interfaces of the human scaffold protein AXIN1 by peptide microarrays JF - Journal of Biological Chemistry VL - 293 IS - 42 SP - 16337-16347 EP - 16337-16347 PB - Amer. Soc. Biochem. Mol. Biol. SN - 00219258 KW - peptide array KW - scaffold protein KW - axin KW - serine KW - threonine protein kinase KW - p53 KW - Myc (c-Myc) KW - casein kinase 1E KW - dishevelled KW - intrinsically disordered region KW - Wnt pathway UR - http://www.jbc.org/content/293/42/16337 L2 - http://www.jbc.org/content/293/42/16337 N2 - 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. ER -
HARNOŠ, Jakub, Jan RYNEŠ, Pavlína VÍŠKOVÁ, Silvie TRANTÍRKOVÁ, Lola Murielle BAJARD ÉP.ESNER, Lukáš TRANTÍREK and Vítězslav BRYJA. Analysis of binding interfaces of the human scaffold protein AXIN1 by peptide microarrays. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2018, vol.~293, No~42, p.~16337-16347. ISSN~0021-9258. Available from: https://dx.doi.org/10.1074/jbc.RA118.005127.
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