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Functional characterization of a BCL10 isoform in the rainbow trout Oncorhynchus mykiss
Author(s) -
Mazzone Pellegrino,
Scudiero Ivan,
Coccia Elena,
Ferravante Angela,
Paolucci Marina,
D'Andrea Egildo Luca,
Varricchio Ettore,
Pizzulo Maddalena,
Reale Carla,
Zotti Tiziana,
Vito Pasquale,
Stilo Romania
Publication year - 2015
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2015.01.007
Subject(s) - rainbow trout , gene isoform , transcription factor , microbiology and biotechnology , biology , trout , model organism , deubiquitinating enzyme , genetics , gene , ubiquitin , fish <actinopterygii> , fishery
The complexes formed by BCL10, MALT1 and members of the family of CARMA proteins have recently been the focus of much attention because they represent a key mechanism for regulating activation of the transcription factor NF‐κB. Here, we report the functional characterization of a novel isoform of BCL10 in the trout Oncorhynchus mykiss , which we named tBCL10. tBCL10 dimerizes, binds to components of the CBM complex and forms cytoplasmic filaments. Functionally, tBCL10 activates NF‐κB transcription factor and is inhibited by the deubiquitinating enzyme A20. Finally, depletion experiments indicate that tBCL10 can functionally replace the human protein. This work demonstrates the evolutionary conservation of the mechanism of NF‐κB activation through the CBM complex, and indicates that the rainbow trout O. mykiss can serve as a model organism to study this pathway.

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