{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Campbell JR"],"funding":["NEI NIH HHS","National Institutes of Health"],"pagination":["587072"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7606922"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14"],"pubmed_abstract":["Neurotransmitter release at retinal ribbon-style synapses utilizes a specialized t-SNARE protein called syntaxin3B (STX3B). In contrast to other syntaxins, STX3 proteins can be phosphorylated <i>in vitro</i> at T14 by Ca<sup>2+/</sup>calmodulin-dependent protein kinase II (CaMKII). This modification has the potential to modulate SNARE complex formation required for neurotransmitter release in an activity-dependent manner. To determine the extent to which T14 phosphorylation occurs <i>in vivo</i> in the mammalian retina and characterize the pathway responsible for the <i>in vivo</i> phosphorylation of T14, we utilized quantitative immunofluorescence to measure the levels of STX3 and STX3 phosphorylated at T14 (pSTX3) in the synaptic terminals of mouse retinal photoreceptors and rod bipolar "],"journal":["Frontiers in cellular neuroscience"],"pubmed_title":["Phosphorylation of the Retinal Ribbon Synapse Specific t-SNARE Protein Syntaxin3B Is Regulated by Light via a Ca<sup>2 +</sup>-Dependent Pathway."],"pmcid":["PMC7606922"],"funding_grant_id":["P30 EY028102","R01 EY012128","P30 EY010608"],"pubmed_authors":["Liu X","Campbell JR","Li H","Kozhemyakin M","Janz R","Wang Y","Hunt AJ","Heidelberger R"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylation of the Retinal Ribbon Synapse Specific t-SNARE Protein Syntaxin3B Is Regulated by Light via a Ca<sup>2 +</sup>-Dependent Pathway.","description":"Neurotransmitter release at retinal ribbon-style synapses utilizes a specialized t-SNARE protein called syntaxin3B (STX3B). In contrast to other syntaxins, STX3 proteins can be phosphorylated <i>in vitro</i> at T14 by Ca<sup>2+/</sup>calmodulin-dependent protein kinase II (CaMKII). This modification has the potential to modulate SNARE complex formation required for neurotransmitter release in an activity-dependent manner. To determine the extent to which T14 phosphorylation occurs <i>in vivo</i> in the mammalian retina and characterize the pathway responsible for the <i>in vivo</i> phosphorylation of T14, we utilized quantitative immunofluorescence to measure the levels of STX3 and STX3 phosphorylated at T14 (pSTX3) in the synaptic terminals of mouse retinal photoreceptors and rod bipolar ","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020","modification":"2025-04-05T11:25:24.38Z","creation":"2020-11-22T09:59:39Z"},"accession":"S-EPMC7606922","cross_references":{"pubmed":["33192329"],"doi":["10.3389/fncel.2020.587072"]}}