QUASIMODO, a novel GPI-anchored zona pellucida protein involved in light input to the Drosophila circadian clock

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F11%3A00367836" target="_blank" >RIV/60077344:_____/11:00367836 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12410/11:43882657

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.cub.2011.03.049" target="_blank" >http://dx.doi.org/10.1016/j.cub.2011.03.049</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.cub.2011.03.049" target="_blank" >10.1016/j.cub.2011.03.049</a>

Jazyk výsledku

angličtina

Název v původním jazyce

QUASIMODO, a novel GPI-anchored zona pellucida protein involved in light input to the Drosophila circadian clock

Popis výsledku v původním jazyce

We identified a novel clock-controlled gene (quasimodo), which encodes a light-responsive and membrane-anchored Zona Pellucida domain protein that supports light-dependent TIM degradation. Whereas wild type flies become arrhythmic in constant light (LL),quasimodo mutants elicit rhythmic expression of clock proteins and behavior in LL. QUASIMODO can function independently of CRY and is predominantly expressed within the CRY-negative DN3 clock neurons. Interestingly, downregulation of qsm in the clock circuit restores LL PERIOD protein rhythms in the qsm-negative DN1, indicating that qsm-mediated light-input is not cell-autonomous and can be accessed by the clock circuit. Our findings indicate that QUASIMODO constitutes part of a novel light-input to the circadian clock. Its light-responsive character in conjunction with the predicted localization at the outer neuronal membrane, suggests that QUASIMODO function is linked to electrical properties of clock neurons.

Název v anglickém jazyce

QUASIMODO, a novel GPI-anchored zona pellucida protein involved in light input to the Drosophila circadian clock

Popis výsledku anglicky

We identified a novel clock-controlled gene (quasimodo), which encodes a light-responsive and membrane-anchored Zona Pellucida domain protein that supports light-dependent TIM degradation. Whereas wild type flies become arrhythmic in constant light (LL),quasimodo mutants elicit rhythmic expression of clock proteins and behavior in LL. QUASIMODO can function independently of CRY and is predominantly expressed within the CRY-negative DN3 clock neurons. Interestingly, downregulation of qsm in the clock circuit restores LL PERIOD protein rhythms in the qsm-negative DN1, indicating that qsm-mediated light-input is not cell-autonomous and can be accessed by the clock circuit. Our findings indicate that QUASIMODO constitutes part of a novel light-input to the circadian clock. Its light-responsive character in conjunction with the predicted localization at the outer neuronal membrane, suggests that QUASIMODO function is linked to electrical properties of clock neurons.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

ED - Fyziologie

OECD FORD obor

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Projekt

<a href="/cs/project/LC07032" target="_blank" >LC07032: Centrum funkční genetiky</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Current Biology

ISSN

0960-9822

e-ISSN

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Svazek periodika

21

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

719-729

Kód UT WoS článku

000290553800021

EID výsledku v databázi Scopus

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