Biochemical Characterization of Apoptotic Cleavage of KH-Type Splicing Regulatory Protein (KSRP) / Far Upstream Element-Binding Protein 2 (FBP2)

Title: Biochemical Characterization of Apoptotic Cleavage of KH-Type Splicing Regulatory Protein (KSRP) / Far Upstream Element-Binding Protein 2 (FBP2)

Volume: 9 Issue: 6

Author(s): Heeyoung Seok, Jinsun Cho, Minseok Cheon and II-Seon Park

Affiliation:

Keywords: ksrp, caspases, proteome, substrate specificity

Abstract: 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.

Cite this article as:

Seok Heeyoung, Cho Jinsun, Cheon Minseok and Park II-Seon, Biochemical Characterization of Apoptotic Cleavage of KH-Type Splicing Regulatory Protein (KSRP) / Far Upstream Element-Binding Protein 2 (FBP2), Protein & Peptide Letters 2002; 9 (6) . https://dx.doi.org/10.2174/0929866023408454