Characterization and functional analysis of grouper (Epinephelus coioides) MEK1 and MEK2.
Amino Acid Sequence
Animals
Bass
/ genetics
Fish Diseases
/ immunology
Fish Proteins
/ chemistry
Gene Expression Profiling
/ veterinary
Gene Expression Regulation
/ immunology
Immunity, Innate
/ genetics
MAP Kinase Kinase 1
/ genetics
MAP Kinase Kinase 2
/ genetics
Phylogeny
Sequence Alignment
/ veterinary
AP1
Cryptocaryon irritans
ERK1/2
Epinephelus coioides
MEK1/2
Journal
Fish & shellfish immunology
ISSN: 1095-9947
Titre abrégé: Fish Shellfish Immunol
Pays: England
ID NLM: 9505220
Informations de publication
Date de publication:
Jan 2019
Jan 2019
Historique:
received:
15
08
2018
revised:
02
11
2018
accepted:
05
11
2018
pubmed:
13
11
2018
medline:
16
4
2019
entrez:
13
11
2018
Statut:
ppublish
Résumé
MEK dual-specificity protein kinases are a group of mitogen-activated protein kinase kinases, which act as an integration point by transferring extracellular signals to the nucleus. To investigate the function of MEK in teleost fish, we cloned MEK1 and MEK2 cDNA sequences from the orange-spotted grouper (Epinephelus coioides). EcMEK1 and EcMEK2 shared 80% amino acid identity with each other. EcMEK1 had 89-99% amino acid identity with teleosts or mammals, whereas EcMEK2 shared 85-97% amino acid identity. The exon structures of the grouper MEK1/2 genes were conserved with zebrafish and human MEK1/2. Tissue distribution analysis showed that EcMEK1 and EcMEK2 had a similar expression pattern in grouper tissues and was mainly transcribe in systemic immune organs. Both EcMEK1 and EcMEK2 were distributed throughout the cytoplasm of transfected GS or HEK293T cells. Overexpression of EcMEK1 or EcMEK2 activated Activator protein 1 dependent luciferase. The phosphorylation levels of EcMEK1/2 and EcERK1/2 were significantly increased in head kidney leukocytes by stimulation with PMA treatment. The grouper MEK1/2-ERK1/2 axis was activated in Cryptocaryon irritans infection and showed an enhanced phosphorylation after immunization.
Identifiants
pubmed: 30419398
pii: S1050-4648(18)30735-6
doi: 10.1016/j.fsi.2018.11.016
pii:
doi:
Substances chimiques
Fish Proteins
0
MAP Kinase Kinase 1
EC 2.7.12.2
MAP Kinase Kinase 2
EC 2.7.12.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1090-1097Informations de copyright
Copyright © 2018 Elsevier Ltd. All rights reserved.