Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00474116" target="_blank" >RIV/61388971:_____/17:00474116 - isvavai.cz</a>
Alternative codes found
RIV/68378050:_____/17:00474116 RIV/00216208:11310/17:10361039
Result on the web
<a href="http://dx.doi.org/10.1073/pnas.1615334114" target="_blank" >http://dx.doi.org/10.1073/pnas.1615334114</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.1615334114" target="_blank" >10.1073/pnas.1615334114</a>
Alternative languages
Result language
angličtina
Original language name
Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424
e-ISSN
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Volume of the periodical
114
Issue of the periodical within the volume
9
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
1641-1650
UT code for WoS article
000395101200010
EID of the result in the Scopus database
2-s2.0-85014219871