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Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif
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SYSNO ASEP 0474116 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif Author(s) Wald, Tomáš (MBU-M) RID
Špoutil, František (UMG-J)
Osičková, Adriana (MBU-M) RID, ORCID
Procházková, Michaela (UMG-J)
Benada, Oldřich (MBU-M) ORCID, RID
Kašpárek, Petr (UMG-J)
Bumba, Ladislav (MBU-M) RID, ORCID
Klein, O. D. (US)
Sedláček, Radislav (UMG-J) RID
Šebo, Peter (MBU-M) RID, ORCID
Procházka, Jan (UMG-J) ORCID
Osička, Radim (MBU-M) RID, ORCIDSource Title Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences - ISSN 0027-8424
Roč. 114, č. 9 (2017), s. 1641-1650Number of pages 10 s. Language eng - English Country US - United States Keywords ameloblastin ; amelogenin ; biomineralization Subject RIV EE - Microbiology, Virology OECD category Microbiology Subject RIV - cooperation Institute of Molecular Genetics - Genetics ; Molecular Biology R&D Projects LM2015064 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LQ1604 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2011032 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2015040 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LO1509 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) ED2.1.00/19.0395 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support MBU-M - RVO:61388971 ; UMG-J - RVO:68378050 UT WOS 000395101200010 EID SCOPUS 85014219871 DOI 10.1073/pnas.1615334114 Annotation The formation of mineralized tissues is governed by extracellular matrix proteins that assemble into a 3D organic matrix directing the deposition of hydroxyapatite. Although the formation of bones and dentin depends on the self-assembly of type I collagen via the Gly-X-Y motif, the molecular mechanism by which enamel matrix proteins (EMPs) assemble into the organic matrix remains poorly understood. Here we identified a Y/F-x-x-Y/L/F-x-Y/F motif, evolutionarily conserved from the first tetrapods to man, that is crucial for higher order structure self-assembly of the key intrinsically disordered EMPs, ameloblastin and amelogenin. Using targeted mutations in mice and high-resolution imaging, we show that impairment of ameloblastin self-assembly causes disorganization of the enamel organic matrix and yields enamel with disordered hydroxyapatite crystallites. These findings define a paradigm for the molecular mechanism by which the EMPs self-assemble into supramolecular structures and demonstrate that this process is crucial for organization of the organic matrix and formation of properly structured enamel. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2018
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