Caspase-mediated cleavage of actin-binding and SH3-domain-containing proteins cortactin, HS1, and HIP-55 during apoptosis
| Autor: | Rajashree Kori, Binujoy John, Yi-Rong Chen, Tse-Hua Tan |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Amino Acid Motifs
Biophysics Arp2/3 complex Caspase 3 Apoptosis macromolecular substances Biochemistry SH3 domain Cell Line Substrate Specificity src Homology Domains Jurkat Cells Mice Animals Humans Actin-binding protein Amino Acid Sequence Molecular Biology Caspase Adaptor Proteins Signal Transducing Cell Size Aspartic Acid Binding Sites biology NLRP1 Chemistry Microfilament Proteins Cell Biology Blood Proteins Actin cytoskeleton Molecular biology Caspase Inhibitors Actins Peptide Fragments Cell biology Caspases biology.protein Carrier Proteins Cortactin HeLa Cells Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 288(4) |
| ISSN: | 0006-291X |
| Popis: | Reorganization of the actin cytoskeleton occurs during apoptosis. We found that actin-binding and Src homology 3 (SH3)-domain-containing proteins cortactin, hematopoietic-specific protein 1 (HS1), and hematopoietic progenitor kinase 1-interacting protein of 55 kDa (HIP-55, also called SH3P7 and Abp1) were degraded in a caspase-dependent manner during apoptosis. Cortactin, HS1, and HIP-55 were direct substrates of caspase 3. Cortactin and HS1 have two clusters of potential caspase cleavage sites; one is in their actin-binding domains, and the other is close to their carboxy-terminal SH3 domains. HIP-55 has one caspase recognition site, EHID 361 . The HIP-55 (D361A) mutant was resistant to caspase cleavage. Cleavage of HIP-55 by caspases dissociated its actin-binding domain from its SH3 domain. The cleavage of these actin-binding and SH3 domain-containing proteins may affect cell signaling to and from the actin cytoskeleton and may be involved in the morphological change of cells during apoptosis. |
| Databáze: | OpenAIRE |
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