Phosphorylation Modulates Ameloblastin Self-assembly and Ca2+ Binding

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00477562" target="_blank" >RIV/61388963:_____/17:00477562 - isvavai.cz</a>

Result on the web

<a href="http://journal.frontiersin.org/article/10.3389/fphys.2017.00531/full" target="_blank" >http://journal.frontiersin.org/article/10.3389/fphys.2017.00531/full</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3389/fphys.2017.00531" target="_blank" >10.3389/fphys.2017.00531</a>

Result language

angličtina

Original language name

Phosphorylation Modulates Ameloblastin Self-assembly and Ca2+ Binding

Original language description

Ameloblastin (AMBN), an important component of the self-assembled enamel extra cellular matrix, contains several in silico predicted phosphorylation sites. However, to what extent these sites actually are phosphorylated and the possible effects of such post-translational modifications are still largely unknown. Here we report on in vitro experiments aimed at investigating what sites in AMBN are phosphorylated by casein kinase 2 (CK2) and protein kinase A (PKA) and the impact such phosphorylation has on self-assembly and calcium binding. All predicted sites in AMBN can be phosphorylated by CK2 and/or PKA. The experiments show that phosphorylation, especially in the exon 5 derived part of the molecule, is inversely correlated with AMBN self-assembly. These results support earlier findings suggesting that AMBN self-assembly is mostly dependent on the exon 5 encoded region of the AMBN gene. Phosphorylation was significantlymore efficient when the AMBN molecules were in solution and not present as supramolecular assemblies, suggesting that post-translational modification of AMBN must take place before the enamel matrix molecules self-assemble inside the ameloblast cell. Moreover, phosphorylation of exon 5, and the consequent reduction in self-assembly, seem to reduce the calcium binding capacity of AMBN suggesting that post-translational modification of AMBN also can be involved in control of free Ca2+ during enamel extra cellular matrix biomineralization. Finally, it is speculated that phosphorylation can provide a functional crossroad for AMBN either to be phosphorylated and act as monomeric signal molecule during early odontogenesis and bone formation, or escape phosphorylation to be subsequently secreted as supramolecular assemblies that partake in enamel matrix structure and mineralization.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Frontiers in physiology

ISSN

1664-042X

e-ISSN

—

Volume of the periodical

8

Issue of the periodical within the volume

Jul 27

Country of publishing house

CH - SWITZERLAND

Number of pages

10

Pages from-to

—

UT code for WoS article

000406530400001

EID of the result in the Scopus database

2-s2.0-85026484154