Activity Dependent CAM cleavage and Neurotransmission
Spatially localized proteolysis represents an elegant means by which neuronal activity dependent changes in synaptic structure, and thus experience dependent learning and memory, can be achieved. In vitro and in vivo studies suggest that matrix metalloproteinase and adamalysin activity is concentrat...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2015-08-01
|
| Series: | Frontiers in Cellular Neuroscience |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00305/full |
| _version_ | 1819102914755428352 |
|---|---|
| author | Katherine eConant Megan eAllen Seung T. Lim |
| author_facet | Katherine eConant Megan eAllen Seung T. Lim |
| author_sort | Katherine eConant |
| collection | DOAJ |
| description | Spatially localized proteolysis represents an elegant means by which neuronal activity dependent changes in synaptic structure, and thus experience dependent learning and memory, can be achieved. In vitro and in vivo studies suggest that matrix metalloproteinase and adamalysin activity is concentrated at the cell surface, and emerging evidence suggests that increased peri-synaptic expression, release and/or activation of these proteinases occurs with enhanced excitatory neurotransmission. Synaptically expressed cell adhesion molecules (CAMs) could therefore represent important targets for neuronal activity-dependent proteolysis. Several CAM subtypes are expressed at the synapse, and their cleavage can influence the efficacy of synaptic transmission through a variety of non-mutually exclusive mechanisms. In the following review, we discuss mechanisms that regulate neuronal activity-dependent synaptic CAM shedding, including those that may be calcium dependent. We also highlight CAM targets of activity-dependent proteolysis including neuroligin and intercellular adhesion molecule-5 (ICAM-5). We include discussion focused on potential consequences of synaptic CAM shedding, with an emphasis on interactions between soluble CAM cleavage products and specific pre- and post-synaptic receptors. |
| first_indexed | 2024-12-22T01:42:08Z |
| format | Article |
| id | doaj.art-93edff73cf0e40a9a283982b20025ad9 |
| institution | Directory Open Access Journal |
| issn | 1662-5102 |
| language | English |
| last_indexed | 2024-12-22T01:42:08Z |
| publishDate | 2015-08-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular Neuroscience |
| spelling | doaj.art-93edff73cf0e40a9a283982b20025ad92022-12-21T18:43:11ZengFrontiers Media S.A.Frontiers in Cellular Neuroscience1662-51022015-08-01910.3389/fncel.2015.00305146226Activity Dependent CAM cleavage and NeurotransmissionKatherine eConant0Megan eAllen1Seung T. Lim2Georgetown UniversityGeorgetown UniversityGeorgetown UniversitySpatially localized proteolysis represents an elegant means by which neuronal activity dependent changes in synaptic structure, and thus experience dependent learning and memory, can be achieved. In vitro and in vivo studies suggest that matrix metalloproteinase and adamalysin activity is concentrated at the cell surface, and emerging evidence suggests that increased peri-synaptic expression, release and/or activation of these proteinases occurs with enhanced excitatory neurotransmission. Synaptically expressed cell adhesion molecules (CAMs) could therefore represent important targets for neuronal activity-dependent proteolysis. Several CAM subtypes are expressed at the synapse, and their cleavage can influence the efficacy of synaptic transmission through a variety of non-mutually exclusive mechanisms. In the following review, we discuss mechanisms that regulate neuronal activity-dependent synaptic CAM shedding, including those that may be calcium dependent. We also highlight CAM targets of activity-dependent proteolysis including neuroligin and intercellular adhesion molecule-5 (ICAM-5). We include discussion focused on potential consequences of synaptic CAM shedding, with an emphasis on interactions between soluble CAM cleavage products and specific pre- and post-synaptic receptors.http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00305/fullMetalloproteasesGlutamatedendritic spineAdhesionCAMMMP |
| spellingShingle | Katherine eConant Megan eAllen Seung T. Lim Activity Dependent CAM cleavage and Neurotransmission Frontiers in Cellular Neuroscience Metalloproteases Glutamate dendritic spine Adhesion CAM MMP |
| title | Activity Dependent CAM cleavage and Neurotransmission |
| title_full | Activity Dependent CAM cleavage and Neurotransmission |
| title_fullStr | Activity Dependent CAM cleavage and Neurotransmission |
| title_full_unstemmed | Activity Dependent CAM cleavage and Neurotransmission |
| title_short | Activity Dependent CAM cleavage and Neurotransmission |
| title_sort | activity dependent cam cleavage and neurotransmission |
| topic | Metalloproteases Glutamate dendritic spine Adhesion CAM MMP |
| url | http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00305/full |
| work_keys_str_mv | AT katherineeconant activitydependentcamcleavageandneurotransmission AT meganeallen activitydependentcamcleavageandneurotransmission AT seungtlim activitydependentcamcleavageandneurotransmission |