Microtubular and Nuclear Functions of gamma-Tubulin: Are They LINCed?
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F19%3A00504271" target="_blank" >RIV/61388971:_____/19:00504271 - isvavai.cz</a>
Výsledek na webu
<a href="https://www.mdpi.com/2073-4409/8/3/259" target="_blank" >https://www.mdpi.com/2073-4409/8/3/259</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/cells8030259" target="_blank" >10.3390/cells8030259</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Microtubular and Nuclear Functions of gamma-Tubulin: Are They LINCed?
Popis výsledku v původním jazyce
gamma-Tubulin is a conserved member of the tubulin superfamily with a function in microtubule nucleation. Proteins of gamma-tubulin complexes serve as nucleation templates as well as a majority of other proteins contributing to centrosomal and non-centrosomal nucleation, conserved across eukaryotes. There is a growing amount of evidence of gamma-tubulin functions besides microtubule nucleation in transcription, DNA damage response, chromatin remodeling, and on its interactions with tumor suppressors. However, the molecular mechanisms are not well understood. Furthermore, interactions with lamin and SUN proteins of the LINC complex suggest the role of gamma-tubulin in the coupling of nuclear organization with cytoskeletons. gamma-Tubulin that belongs to the clade of eukaryotic tubulins shows characteristics of both prokaryotic and eukaryotic tubulins. Both human and plant gamma-tubulins preserve the ability of prokaryotic tubulins to assemble filaments and higher-order fibrillar networks. gamma-Tubulin filaments, with bundling and aggregating capacity, are suggested to perform complex scaffolding and sequestration functions. In this review, we discuss a plethora of gamma-tubulin molecular interactions and cellular functions, as well as recent advances in understanding the molecular mechanisms behind them.
Název v anglickém jazyce
Microtubular and Nuclear Functions of gamma-Tubulin: Are They LINCed?
Popis výsledku anglicky
gamma-Tubulin is a conserved member of the tubulin superfamily with a function in microtubule nucleation. Proteins of gamma-tubulin complexes serve as nucleation templates as well as a majority of other proteins contributing to centrosomal and non-centrosomal nucleation, conserved across eukaryotes. There is a growing amount of evidence of gamma-tubulin functions besides microtubule nucleation in transcription, DNA damage response, chromatin remodeling, and on its interactions with tumor suppressors. However, the molecular mechanisms are not well understood. Furthermore, interactions with lamin and SUN proteins of the LINC complex suggest the role of gamma-tubulin in the coupling of nuclear organization with cytoskeletons. gamma-Tubulin that belongs to the clade of eukaryotic tubulins shows characteristics of both prokaryotic and eukaryotic tubulins. Both human and plant gamma-tubulins preserve the ability of prokaryotic tubulins to assemble filaments and higher-order fibrillar networks. gamma-Tubulin filaments, with bundling and aggregating capacity, are suggested to perform complex scaffolding and sequestration functions. In this review, we discuss a plethora of gamma-tubulin molecular interactions and cellular functions, as well as recent advances in understanding the molecular mechanisms behind them.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10606 - Microbiology
Návaznosti výsledku
Projekt
<a href="/cs/project/GA15-11657S" target="_blank" >GA15-11657S: Úloha gama- tubulinu v koordinaci nukleace mikrotubulů a buněčného dělení s odpovědí buňky na poškození DNA u rostlin</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2019
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Cells
ISSN
2073-4409
e-ISSN
—
Svazek periodika
8
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
17
Strana od-do
259
Kód UT WoS článku
000464194500002
EID výsledku v databázi Scopus
2-s2.0-85042859952