BCL10GFP fusion protein as a substrate for analysis of determinants required for mucosa-associated lymphoid tissue 1 (MALT1)-mediated cleavage
Journal
Journal of biomedical science
Journal Volume
19
Journal Issue
1
Date Issued
2012-10-05
Author(s)
Jou, Shin-Yi
Chang, Chien-Chih
Wu, Chun-Hsien
Chuang, Wen-Hui
Chen, Yun-Hui
Abstract
MALT1 belongs to a family of paracaspase and modulates NF-κB signaling pathways through its scaffolding function and proteolytic activity. MALT1 cleaves protein substrates after a positively charged Arginine residue. BCL10, a 233 amino acids polypeptide, is identified as one of the MALT1 proteolytic substrates. MALT1 cleaves BCL10 at the C-terminal end of Arg228. A mere 5 amino acids difference between the substrate and the proteolytic product made it difficult to tell whether the cleavage event took place by using a simple western blot analysis. Here, BCL10GFP was constructed and utilized to examine the specificity and domain determinants for MALT1 cleavage in cells.
Subjects
BCL10GFP | In vivo | MALT1 | Paracaspase | Processing
Type
journal article