Abstract
Protein inhibitor of activated STAT (PIAS) proteins are activation-suppressing proteins for signal transducer and activator of transcription (STAT), which involves gene transcriptional regulation. The inhibitory mechanism of PIAS proteins in the Janus kinase (JAK)/STAT signaling pathway has been well studied in mammals and Drosophila. However, the roles of PIAS in crustaceans are unclear. In the present study, we identified PIAS in kuruma shrimp Marsupenaeus japonicus and found that its relative expression could be induced by Vibrio anguillarum stimulation. To explore the function of PIAS in shrimp infected with V. anguillarum, we performed an RNA interference assay. After knockdown of PIAS expression in shrimp subjected to V. anguillarum infection, bacterial clearance was enhanced and the survival rate increased compared with those in the control shrimp (dsGFP injection). Simultaneously, the expression levels of antimicrobial peptides (AMPs), including anti-lipopolysaccharide factor (ALF) A1, C1, C2, and CruI-1, increased. Further study revealed that knockdown of PIAS also enhanced STAT phosphorylation and translocation. Pulldown assay indicated that PIAS interacts with activated STAT in shrimp. In conclusion, PIAS negatively regulates JAK/STAT signaling by inhibiting the phosphorylation and translocation of STAT through the interaction between PIAS and STAT, which leads to the reduction of AMP expression in shrimp. Our results revealed a new mechanism of PIAS-mediated gene regulation of the STAT signal pathway.
Highlights
The protein inhibitor of activated STAT (PIAS) family was identified an inhibitor of signal transducer and activator of transcription (STAT) acting on the Janus kinase (JAK)/STAT signaling pathway [1, 2]
We identified MjPIAS, which was determined to negatively regulate STAT by analyzing the antimicrobial peptides (AMPs) transcription regulated by the JAK/STAT pathway in kuruma shrimp
Protein inhibitor of activated STAT (PIAS) proteins interact with several transcription factors, such as STAT, NFκB, Jun, and p53, many of which are key transcription factors involved in the immune system
Summary
The protein inhibitor of activated STAT (PIAS) family was identified an inhibitor of signal transducer and activator of transcription (STAT) acting on the Janus kinase (JAK)/STAT signaling pathway [1, 2]. The PIAS family in mammals has at least five members: PIAS1, PIASxα, PIASxβ, PIAS3, and PIASy. All the PIAS proteins are highly conserved and have common structural features. All the PIAS proteins are highly conserved and have common structural features They have an N-terminal SAFA/B, Acinus and PIAS (SAP) domain [3], a Pro-Ile-Asn-Ile-Thr (PINIT) motif [4], a RING finger-like Zinc binding domain (RLD) [5], an acidic amino acid domain (AD) [6, 7], and C-terminal Ser/Thr amino acids enriched region (S/T). PIAS Negatively Regulates JAK/STAT Pathway domain is involved in sequence- or structure-specific DNA binding [8]. The PINIT motif, a highly conserved region of PIAS proteins, is involved in the nuclear retention [4]. The C-terminal S/T-rich region is the least conserved and its function remains to be defined
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