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
Author(s)
Pelzer C., Cabalzar K., Wolf A., Gonzalez M., Lenz G., Thome M.
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
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