Phosphatase of Regenerating Liver-1 Selectively Times Circadian Behavior in Darkness via Function in PDF Neurons and Dephosphorylation of TIMELESS.
Animals
Animals, Genetically Modified
Circadian Rhythm
/ physiology
Darkness
Drosophila Proteins
/ genetics
Drosophila melanogaster
Female
Gene Knockdown Techniques
Male
Mutation
Neurons
/ metabolism
Neuropeptides
/ metabolism
Phosphorylation
/ physiology
Photoperiod
Protein Tyrosine Phosphatases
/ genetics
Time Factors
Drosophila
circadian
phosphorylation
photoperiod
seasonality
Journal
Current biology : CB
ISSN: 1879-0445
Titre abrégé: Curr Biol
Pays: England
ID NLM: 9107782
Informations de publication
Date de publication:
11 01 2021
11 01 2021
Historique:
received:
13
03
2020
revised:
25
08
2020
accepted:
07
10
2020
pubmed:
7
11
2020
medline:
1
9
2021
entrez:
6
11
2020
Statut:
ppublish
Résumé
The timing of behavior under natural light-dark conditions is a function of circadian clocks and photic input pathways, but a mechanistic understanding of how these pathways collaborate in animals is lacking. Here we demonstrate in Drosophila that the Phosphatase of Regenerating Liver-1 (PRL-1) sets period length and behavioral phase gated by photic signals. PRL-1 knockdown in PDF clock neurons dramatically lengthens circadian period. PRL-1 mutants exhibit allele-specific interactions with the light- and clock-regulated gene timeless (tim). Moreover, we show that PRL-1 promotes TIM accumulation and dephosphorylation. Interestingly, the PRL-1 mutant period lengthening is suppressed in constant light, and PRL-1 mutants display a delayed phase under short, but not long, photoperiod conditions. Thus, our studies reveal that PRL-1-dependent dephosphorylation of TIM is a core mechanism of the clock that sets period length and phase in darkness, enabling the behavioral adjustment to change day-night cycles.
Identifiants
pubmed: 33157022
pii: S0960-9822(20)31517-7
doi: 10.1016/j.cub.2020.10.013
pmc: PMC7855481
mid: NIHMS1638972
pii:
doi:
Substances chimiques
Drosophila Proteins
0
Neuropeptides
0
pdf protein, Drosophila
0
tim protein, Drosophila
0
PRL-1 protein, Drosophila
EC 3.1.3.48
Protein Tyrosine Phosphatases
EC 3.1.3.48
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
138-149.e5Subventions
Organisme : NINDS NIH HHS
ID : R01 NS106955
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK090625
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM108569
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA060553
Pays : United States
Organisme : NHLBI NIH HHS
ID : T32 HL007909
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK113011
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG065988
Pays : United States
Organisme : NIA NIH HHS
ID : P01 AG011412
Pays : United States
Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interest The authors declare no competing interests.
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