<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Campbell JR</submitter><funding>NEI NIH HHS</funding><funding>National Institutes of Health</funding><pagination>587072</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7606922</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14</volume><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 &lt;i>in vitro&lt;/i> at T14 by Ca&lt;sup>2+/&lt;/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 &lt;i>in vivo&lt;/i> in the mammalian retina and characterize the pathway responsible for the &lt;i>in vivo&lt;/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 </pubmed_abstract><journal>Frontiers in cellular neuroscience</journal><pubmed_title>Phosphorylation of the Retinal Ribbon Synapse Specific t-SNARE Protein Syntaxin3B Is Regulated by Light via a Ca&lt;sup>2 +&lt;/sup>-Dependent Pathway.</pubmed_title><pmcid>PMC7606922</pmcid><funding_grant_id>P30 EY028102</funding_grant_id><funding_grant_id>R01 EY012128</funding_grant_id><funding_grant_id>P30 EY010608</funding_grant_id><pubmed_authors>Liu X</pubmed_authors><pubmed_authors>Campbell JR</pubmed_authors><pubmed_authors>Li H</pubmed_authors><pubmed_authors>Kozhemyakin M</pubmed_authors><pubmed_authors>Janz R</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>Hunt AJ</pubmed_authors><pubmed_authors>Heidelberger R</pubmed_authors></additional><is_claimable>false</is_claimable><name>Phosphorylation of the Retinal Ribbon Synapse Specific t-SNARE Protein Syntaxin3B Is Regulated by Light via a Ca&lt;sup>2 +&lt;/sup>-Dependent Pathway.</name><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 &lt;i>in vitro&lt;/i> at T14 by Ca&lt;sup>2+/&lt;/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 &lt;i>in vivo&lt;/i> in the mammalian retina and characterize the pathway responsible for the &lt;i>in vivo&lt;/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 </description><dates><release>2020-01-01T00:00:00Z</release><publication>2020</publication><modification>2025-04-05T11:25:24.38Z</modification><creation>2020-11-22T09:59:39Z</creation></dates><accession>S-EPMC7606922</accession><cross_references><pubmed>33192329</pubmed><doi>10.3389/fncel.2020.587072</doi></cross_references></HashMap>