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Functional characterization of a BCL10 isoform in the rainbow trout Oncorhynchus mykiss.

Mazzone P, Scudiero I, Coccia E, Ferravante A, Paolucci M, D'Andrea EL, Varricchio E, Pizzulo M, Reale C, Zotti T, Vito P, Stilo R - FEBS Open Bio (2015)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Biogem, Via Camporeale, Ariano Irpino (AV), Italy.

ABSTRACT
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.

No MeSH data available.


Subcellular localization of tBCL10. HEK-293 cells were transfected with mammalian FLAG-tagged vector, empty (vector) or expressing tBCL10. 16 h after transfection, cells were stained with anti-FLAG mAb, followed by FITC-conjugated anti-mouse IgG.
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f0020: Subcellular localization of tBCL10. HEK-293 cells were transfected with mammalian FLAG-tagged vector, empty (vector) or expressing tBCL10. 16 h after transfection, cells were stained with anti-FLAG mAb, followed by FITC-conjugated anti-mouse IgG.

Mentions: Fluorescence microscopy experiments and structural studies have shown that the NF-κB-activity produced by hBCL10 is regulated through formation of cytosolic filamentous structures [21,23]. We therefore verified whether also tBCL10 is able to form such structures. As shown in Fig. 4, assembly of filamentous structures is readily visible following expression of tBCL10 in mammalian cells.


Functional characterization of a BCL10 isoform in the rainbow trout Oncorhynchus mykiss.

Mazzone P, Scudiero I, Coccia E, Ferravante A, Paolucci M, D'Andrea EL, Varricchio E, Pizzulo M, Reale C, Zotti T, Vito P, Stilo R - FEBS Open Bio (2015)

Subcellular localization of tBCL10. HEK-293 cells were transfected with mammalian FLAG-tagged vector, empty (vector) or expressing tBCL10. 16 h after transfection, cells were stained with anti-FLAG mAb, followed by FITC-conjugated anti-mouse IgG.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4372615&req=5

f0020: Subcellular localization of tBCL10. HEK-293 cells were transfected with mammalian FLAG-tagged vector, empty (vector) or expressing tBCL10. 16 h after transfection, cells were stained with anti-FLAG mAb, followed by FITC-conjugated anti-mouse IgG.
Mentions: Fluorescence microscopy experiments and structural studies have shown that the NF-κB-activity produced by hBCL10 is regulated through formation of cytosolic filamentous structures [21,23]. We therefore verified whether also tBCL10 is able to form such structures. As shown in Fig. 4, assembly of filamentous structures is readily visible following expression of tBCL10 in mammalian cells.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Biogem, Via Camporeale, Ariano Irpino (AV), Italy.

ABSTRACT
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.

No MeSH data available.