Biochemical characterization of apoptotic cleavage of KH-type splicing regulatory protein (KSRP)/far upstream element-binding protein 2 (FBP2)

• Published in: Protein and peptide letters Vol. 9; no. 6; p. 511
• Main Authors: Seok, Heeyoung, Cho, Jinsun, Cheon, Minseok, Park, Il-Seon
• Format: Journal Article
• Language: English
• Published: Netherlands 01-12-2002
• Subjects: Animals; Apoptosis - physiology; Caspase 3; Caspases - metabolism; Humans; Rats; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - metabolism; Substrate Specificity; Trans-Activators; Tumor Cells, Cultured
• ISSN: 0929-8665
• DOI: 10.2174/0929866023408454

Caspases, Asp-specific cysteine protease, cleave proteins upon apoptosis. To identify and characterize new caspase substrate in the nucleus, the proteome of the rat liver extracts was analyzed after the treatment with caspases. One of the identified proteins was KSRP/FBP2 that is preferentially cleaved by caspase-3 and 7 at two sites after Asp102 and Asp183. The second site was cleaved only in the protein produced in cells, but not in in vitro translated protein. These results indicate that more than the primary sequence may be important for the recognition by caspases.