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Phosphorylation regulation of Lv-β-catenin of Litopenaeus vannamei by an immediate early protein WSV083 to reduce cell adhesion.
- Source :
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Aquaculture . Jan2024, Vol. 579, pN.PAG-N.PAG. 1p. - Publication Year :
- 2024
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Abstract
- β-catenin that belongs to Armdillo family is a key molecule in the canonical Wnt signaling pathway. It participates in host immunity by activating downstream transcription factors to regulate immune-related genes. In this study, Lv-β-catenin in Pacific white shrimp Litopenaeus vannamei , which is a homologous gene of β-catenin, was investigated to explore the molecular function during white spot syndrome virus (WSSV) infection. Sequence analysis showed that Lv-β-catenin contains abundant phosphorylation sites, which indicated phosphorylation is an important pattern for β-catenin regulation. Immunoprecipitation assay showed that a WSSV immediate early protein WSV083, which was identified as a serine (Ser)/threonine (Thr) kinase, could interact with Lv-β-catenin. Further Western blot and immunofluorescence analysis suggested that WSV083 could promote degradation of Lv-β-catenin through the proteasome pathway. And the degradation of Lv-β-catenin was regulated by phosphorylation initiated at Ser56 site, which was mediated by WSV083. In addition, WSV083 could also affect phosphorylation of other Ser and Thr of Lv-β-catenin, which indicated that WSV083 could regulate Lv-β-catenin by numerous ways. Moreover, it is found that Lv-β-catenin could promote cell adhesion, while this effect could be inhibited by WSV083. In conclusion, WSSV could down regulate Lv-β-catenin and decrease cell adhesion mediated by WSV083 to resist host immunity. The study will improve understanding of the pathogenic molecular mechanism of WSSV and promote disease control. • WSV083 interacted with Lv-β-catenin, and promoted its degradation through the proteasome pathway. • Lv-β-catenin was regulated by phosphorylation initiated at Ser56, which was mediated by WSV083. • WSV083 could down regulate Lv-β-catenin and reduce cell adhesion. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00448486
- Volume :
- 579
- Database :
- Academic Search Index
- Journal :
- Aquaculture
- Publication Type :
- Academic Journal
- Accession number :
- 173693377
- Full Text :
- https://doi.org/10.1016/j.aquaculture.2023.740244