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Bardet, M.* ; Seeholzer, T. ; Unterreiner, A.* ; Woods, S. ; Krappmann, D. ; Bornancin, F.*

MALT1 activation by TRAF6 needs neither BCL10 nor CARD11.

Biochem. Biophys. Res. Commun. 506, 48-52 (2018)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter 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
Zeitschrift Biochemical and Biophysical Research Communications
Quellenangaben Band: 506, Heft: 1, Seiten: 48-52 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort 525 B St, Ste 1900, San Diego, Ca 92101-4495 Usa
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Research Unit Signaling and Translation (SAT)