The protease activity of the paracaspase MALT1 is controlled by monoubiquitination.
Details
Serval ID
serval:BIB_6A6A58953F95
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The protease activity of the paracaspase MALT1 is controlled by monoubiquitination.
Journal
Nature Immunology
ISSN
1529-2916 (Electronic)
ISSN-L
1529-2908
Publication state
Published
Issued date
2013
Volume
14
Number
4
Pages
337-345
Language
english
Abstract
The protease activity of the paracaspase MALT1 is central to lymphocyte activation and lymphomagenesis, but how this activity is controlled remains unknown. Here we identify a monoubiquitination of MALT1 on Lys644 that activated the protease function of MALT1. Monoubiquitinated MALT1 had enhanced protease activity, whereas a ubiquitination-deficient MALT1 mutant with replacement of that lysine with arginine (MALT1(K644R)) had less protease activity, which correlated with impaired induction of interleukin 2 (IL-2) via the T cell antigen receptor in activated T cells. Expression of MALT1(K644R) diminished the survival of cells derived from diffuse large B cell lymphoma of the activated B cell-like subtype (ABC DLBCL), which require constitutive protease activity of MALT1 for survival. Thus, monoubiquitination of MALT1 is essential for its catalytic activation and is therefore a potential target for the treatment of ABC-DLBCL and for immunomodulation.
Pubmed
Web of science
Create date
18/04/2013 7:42
Last modification date
20/08/2019 14:25