The proteolytic activity of the paracaspase MALT1 is key in T cell activation

被引：252

作者：

Rebeaud, Fabien ^{[1
]}

Hailfinger, Stephan ^{[1
]}

Posevitz-Fejfar, Anita ^{[1
]}

Tapernoux, Myriam ^{[1
]}

Moser, Roger ^{[1
]}

Rueda, Daniel ^{[1
]}

Gaide, Olivier ^{[1
]}

Guzzardi, Montserrat ^{[1
]}

Iancu, Emanuela M. ^{[2
]}

Rufer, Nathalie ^{[2
]}

Fasel, Nicolas ^{[1
]}

Thome, Margot ^{[1
]}

机构：

[1] Univ Lausanne, Dept Biochem, CH-1066 Epalinges, Switzerland

[2] Univ Lausanne Hosp, Multidisciplinary Oncol Ctr, CH-1005 Lausanne, Switzerland

来源：

NATURE IMMUNOLOGY | 2008年 / 9卷 / 03期

关键词：

D O I：

10.1038/ni1568

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

The paracaspase MALT1 is pivotal in antigen receptor-mediated lymphocyte activation and lymphomagenesis. MALT1 contains a caspase-like domain, but it is unknown whether this domain is proteolytically active. Here we report that MALT1 had arginine-directed proteolytic activity that was activated after T cell stimulation, and we identify the signaling protein Bcl-10 as a MALT1 substrate. Processing of Bcl-10 after Arg228 was required for T cell receptor-induced cell adhesion to fibronectin. In contrast, MALT1 activity but not Bcl-10 cleavage was essential for optimal activation of transcription factor NF-kappa B and production of interleukin 2. Thus, the proteolytic activity of MALT1 is central to T cell activation, which suggests a possible target for the development of immunomodulatory or anticancer drugs.

引用

页码：272 / 281

页数：10

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