Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase-3
| Autor: | Wilma Wasco, Nikhat F. Zaidi, Joseph D. Buxbaum, Janice S. Miller, Eun-Kyoung Choi, E. Salih |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Phosphatase
Repressor macromolecular substances Biology Serine Mice Neuroblastoma Cellular and Molecular Neuroscience chemistry.chemical_compound Antibody Specificity Casein Kinase I Phosphoprotein Phosphatases Tumor Cells Cultured Animals Humans Phosphorylation Threonine Molecular Biology Neurons Caspase 3 Calcium-Binding Proteins Kv Channel-Interacting Proteins Cell Biology Cell biology Repressor Proteins Biochemistry chemistry Caspases Calsenilin Calcium Casein kinases Casein Kinases Protein Kinases |
| Zdroj: | Molecular and Cellular Neuroscience. 23:495-506 |
| ISSN: | 1044-7431 |
| DOI: | 10.1016/s1044-7431(03)00072-1 |
| Popis: | Calsenilin is a member of the neuronal calcium sensor (NCS) family of proteins that interacts with the presenilins. Calsenilin has been found to act as a Kv4alpha channel interactor and as a transcriptional repressor. We have recently shown that calsenilin can be cleaved by caspase-3 and that its cleavage separates the conserved calcium-binding domain from the variable N-terminal domain. Here, we demonstrate that calsenilin can be phosphorylated by casein kinase I and that its phosphorylation can be regulated by intracellular calcium. In addition, phosphorylated calsenilin is a substrate for serine/threonine protein phosphatase (PP) 1 and/or 2A. Phosphorylation within the N-terminal domain at Ser63, the major phosphorylation site of calsenilin, inhibits cleavage of the molecule by caspase-3. Given that the N-terminal domain of calsenilin is not conserved in the larger NCS family including other KChIP/CALP proteins, phosphorylation of calsenilin may regulate a functional role that is unique to this member of the superfamily. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect