Novel calpain families and novel mechanisms for calpain regulation in Aplysia.
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 k...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2017-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC5650170?pdf=render |
| _version_ | 1818232085353070592 |
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| author | Margaret H Hastings Katrina Gong Alexander Freibauer Caitlin Courchesne Xiaotang Fan Wayne S Sossin |
| author_facet | Margaret H Hastings Katrina Gong Alexander Freibauer Caitlin Courchesne Xiaotang Fan Wayne S Sossin |
| author_sort | Margaret H Hastings |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-12T11:00:41Z |
| format | Article |
| id | doaj.art-7b1655ac47094ea5b6ac8cebc69e8f73 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-12T11:00:41Z |
| publishDate | 2017-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-7b1655ac47094ea5b6ac8cebc69e8f732022-12-22T00:26:33ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-011210e018664610.1371/journal.pone.0186646Novel calpain families and novel mechanisms for calpain regulation in Aplysia.Margaret H HastingsKatrina GongAlexander FreibauerCaitlin CourchesneXiaotang FanWayne S SossinCalpains 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.http://europepmc.org/articles/PMC5650170?pdf=render |
| spellingShingle | Margaret H Hastings Katrina Gong Alexander Freibauer Caitlin Courchesne Xiaotang Fan Wayne S Sossin Novel calpain families and novel mechanisms for calpain regulation in Aplysia. PLoS ONE |
| title | Novel calpain families and novel mechanisms for calpain regulation in Aplysia. |
| title_full | Novel calpain families and novel mechanisms for calpain regulation in Aplysia. |
| title_fullStr | Novel calpain families and novel mechanisms for calpain regulation in Aplysia. |
| title_full_unstemmed | Novel calpain families and novel mechanisms for calpain regulation in Aplysia. |
| title_short | Novel calpain families and novel mechanisms for calpain regulation in Aplysia. |
| title_sort | novel calpain families and novel mechanisms for calpain regulation in aplysia |
| url | http://europepmc.org/articles/PMC5650170?pdf=render |
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