ß-Arrestin 1's Interaction with TC45 Attenuates Stat signaling by dephosphorylating Stat to inhibit antimicrobial peptide expression.
Sci Rep
; 6: 35808, 2016 10 26.
Article
en En
| MEDLINE
| ID: mdl-27782165
Impaired phosphatase activity leads to the persistent activation of signal transducers and activators of transcription (Stat). In mammals, Stat family members are often phosphorylated or dephosphorylated by the same enzymes. To date, only one Stat similar to mammalian Stat5a/b has been found in crustaceans and there have been few studies in Stat signal regulation in crustaceans. Here, we report that ß-arrestin1 interacts with TC45 (45-kDa form of T cell protein tyrosine phosphatase) in the nucleus to attenuate Stat signaling by promoting dephosphorylation of Stat. Initially, we showed that Stat translocates into the nucleus to induce antimicrobial peptide (AMP) expression after bacterial infection. ßArr1 enters the nucleus of hemocytes and recruits TC45 to form the ßarr1-TC45-Stat complex, which dephosphorylates Stat efficiently. The interaction of TC45 with Stat decreased and Stat phosphorylation increased in ßarr1-silenced shrimp (Marsupenaeus japonicus) after challenge with Vibrio anguillarum. ßArr1 directly interacts with Stat in nucleus and accelerates Stat dephosphorylation by recruiting TC45 after V. anguillarum challenge. Further study showed that ßarr1 and TC45 also affect AMP expression, which is regulated by Stat. Therefore, ßarr1 and TC45 are involved in the anti-V. anguillarum immune response by regulating Stat activity negatively to decrease AMP expression in shrimp.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos Catiónicos Antimicrobianos
/
Factores de Transcripción STAT
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Proteína Tirosina Fosfatasa no Receptora Tipo 2
/
Beta-Arrestina 1
Límite:
Animals
Idioma:
En
Revista:
Sci Rep
Año:
2016
Tipo del documento:
Article
País de afiliación:
China
Pais de publicación:
Reino Unido