auto-ubiquitination-induced degradation of malt1-api2 prevents bcl10 destabilization in t(11;18)(q21;q21)-positive malt lymphomaauto-ubiquitination-induced malt1-api2防止退化bcl10扰动在t(11;18)(温度系数;温度系数)阳性麦芽淋巴瘤.pdfVIP

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auto-ubiquitination-induced degradation of malt1-api2 prevents bcl10 destabilization in t(11;18)(q21;q21)-positive malt lymphomaauto-ubiquitination-induced malt1-api2防止退化bcl10扰动在t(11;18)(温度系数;温度系数)阳性麦芽淋巴瘤.pdf

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auto-ubiquitination-induced degradation of malt1-api2 prevents bcl10 destabilization in t(11;18)(q21;q21)-positive malt lymphomaauto-ubiquitination-induced malt1-api2防止退化bcl10扰动在t(11;18)(温度系数;温度系数)阳性麦芽淋巴瘤

Auto-Ubiquitination-Induced Degradation of MALT1- API2 Prevents BCL10 Destabilization in t(11;18)(q21;q21)- Positive MALT Lymphoma 1,2¤ 1,2 3 3 3 Heidi Noels , Riet Somers , Hongxiang Liu , Hongtao Ye , Ming-Qing Du , Christiane De Wolf- Peeters4, Peter Marynen1,2, Mathijs Baens1,2* 1 Human Genome Laboratory, Department for Molecular and Developmental Genetics, VIB, Leuven, Belgium, 2 Human Genome Laboratory, Center for Human Genetics, Molecular Genetics, University of Leuven, Leuven, Belgium, 3 Division of Molecular Histopathology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom, 4 Department of Morphology and Molecular Pathology, University of Leuven, Leuven, Belgium Abstract Background: The translocation t(11;18)(q21;q21) is the most frequent chromosomal aberration associated with MALT lymphoma and results in constitutive NF-kB activity via the expression of an API2-MALT1 fusion protein. The properties of the reciprocal MALT1-API2 were never investigated as it was reported to be rarely transcribed. Principal Findings: Our data indicate the presence of MALT1-API2 transcripts in the majority of t(11;18)(q21;q21)-positive MALT lymphomas. Based on the breakpoints in the MALT1 and API2 gene, the MALT1-API2 protein contains the death domain and one or both immunoglobulin-like domains of MALT1 (,90% of cases) - mediating the possible interaction with BCL10 - fused to the RING domain of API2. Here we show that this RING domain enables MALT1-API2 to function as an E3 ubiquitin ligase for BCL10, inducing its ubiquitination and proteasomal degradation in vitro. Expression of MALT1-API2 transcripts in t(11;18)(q21;q21)-positive MALT lymphomas was however not associated with a reduction of BCL10 protein le