Novel calpain families and novel mechanisms for calpain regulation in Aplysia
| Autor: | Caitlin Courchesne, Margaret H. Hastings, Xiaotang Fan, Alexander Freibauer, Wayne S. Sossin, Katrina Gong |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Transcription Genetic lcsh:Medicine Biochemistry 0302 clinical medicine Aplysia Medicine and Health Sciences lcsh:Science Phylogeny Data Management Multidisciplinary Neuronal Plasticity biology Kinase Calpain Eukaryota Phylogenetic Analysis Animal Models Cell biology Phylogenetics Experimental Organism Systems Cell Processes Vertebrates Anatomy Research Article Gene isoform Proteases Computer and Information Sciences animal structures Casein Research and Analysis Methods 03 medical and health sciences Developmental Neuroscience Animals Evolutionary Systematics Protein kinase A Gene Taxonomy Evolutionary Biology PKCS lcsh:R Organisms Biology and Life Sciences Proteins Molluscs Cell Biology biology.organism_classification Phosphoproteins Invertebrates 030104 developmental biology Biological Tissue Gastropods Cellular Neuroscience biology.protein Sea Slugs Ganglia lcsh:Q Autolysis 030217 neurology & neurosurgery Neuroscience Synaptic Plasticity |
| Zdroj: | PLoS ONE, Vol 12, Iss 10, p e0186646 (2017) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | Calpains are a family of intracellular proteases defined by a conserved protease domain. In the marine mollusk Aplysia californica, calpains are important for the induction of long-term synaptic plasticity and memory, at least in part by cleaving protein kinase Cs (PKCs) into constitutively active kinases, termed protein kinase Ms (PKMs). We identify 14 genes encoding calpains in Aplysia using bioinformatics, including at least one member of each of the four major calpain families into which metazoan calpains are generally classified, as well as additional truncated and atypical calpains. Six classical calpains containing a penta-EF-hand (PEF) domain are present in Aplysia. Phylogenetic analysis determined that these six calpains come from three separate classical calpain families. One of the classical calpains in Aplysia, AplCCal1, has been implicated in plasticity. We identify three splice cassettes and an alternative transcriptional start site in AplCCal1. We characterize several of the possible isoforms of AplCCal1 in vitro, and demonstrate that AplCCal1 can cleave PKCs into PKMs in a calcium-dependent manner in vitro. We also find that AplCCal1 has a novel mechanism of auto-inactivation through N-terminal cleavage that is modulated through its alternative transcriptional start site. |
| Databáze: | OpenAIRE |
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