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Open Access Green as soon as Postprint is submitted to ZB.
MALT1 activation by TRAF6 needs neither BCL10 nor CARD11.
Biochem. Biophys. Res. Commun. 506, 48-52 (2018)
The MALT1 (Mucosa associated lymphoid tissue lymphoma translocation protein 1) paracaspase couples antigen receptors on lymphocytes to downstream signaling events. Activation of MALT1 is known to involve stimulus-dependent CBM complex formation, that is, the recruitment of BCL10-bound MALT1 to a CARD-Coiled Coil protein. Beyond this canonical, CBM-dependent mechanism of MALT1 activation, recent studies suggest that MALT1 protease activity may be triggered by alternative mechanisms. For instance, the E3-ligase TRAF6 can activate MALT1 proteolytic function and induce MALT1 auto-cleavage. However, the interplay between CBM and TRAF6 with regard to MALT1 activation has remained incompletely elucidated. Here, by generating CRISPR/Cas9-derived knock-out Jurkat T-cells, we show that TRAF6 was dispensable for CARD11/BCL10-dependent MALT1 activation upon T-cell stimulation. However, ectopically-expressed TRAF6 could induce MALT1 activity in Jurkat T-cells devoid of either CARD11 or BCL10. These data provide unequivocal evidence that TRAF6-mediated MALT1 activation does not require the upstream scaffold CARD11 or the interaction between MALT1 and BCL10. Thus, TRAF6 may be part of a previously unidentified non-canonical pathway that triggers MALT1 protease activity independently of canonical CBM signalosomes. (C) 2018 Elsevier Inc. All rights reserved.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Malt1 ; Traf6 ; Cbm Complex ; Mono-ubiquitination ; Proteolytic Activation; Paracaspase Malt1; Carma1; Phosphorylation; Lymphoma; Cleavage; Plays; Key
ISSN (print) / ISBN
0006-291X
e-ISSN
1090-2104
Quellenangaben
Volume: 506,
Issue: 1,
Pages: 48-52
Publisher
Elsevier
Publishing Place
525 B St, Ste 1900, San Diego, Ca 92101-4495 Usa
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Research Unit Signaling and Translation (SAT)