{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bourgeois-Jaarsma Q"],"funding":["UE, Erasmus Mundus Joint Doctorate program, ENC network cycle 4, project 3","ZonMw"],"pagination":["14408"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6783474"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(1)"],"pubmed_abstract":["Communication between neurons involves presynaptic neurotransmitter release which can be evoked by action potentials or occur spontaneously as a result of stochastic vesicle fusion. The Ca<sup>2+</sup>-binding double C<sub>2</sub> proteins Doc2a and -b were implicated in spontaneous and asynchronous evoked release, but the mechanism remains unclear. Here, we compared wildtype Doc2b with two Ca<sup>2+</sup> binding site mutants named DN and 6A, previously classified as gain- and loss-of-function mutants. They carry the substitutions D218,220N or D163,218,220,303,357,359A respectively. We found that both mutants bound phospholipids at low Ca<sup>2+</sup> concentrations and were membrane-associated in resting neurons, thus mimicking a Ca<sup>2+</sup>-activated state. Their overexpression in h"],"journal":["Scientific reports"],"pubmed_title":["Doc2b Ca<sup>2+</sup> binding site mutants enhance synaptic release at rest at the expense of sustained synaptic strength."],"pmcid":["PMC6783474"],"funding_grant_id":["91113022"],"pubmed_authors":["Bourgeois-Jaarsma Q","Groffen AJ","Verhage M"],"additional_accession":[]},"is_claimable":false,"name":"Doc2b Ca<sup>2+</sup> binding site mutants enhance synaptic release at rest at the expense of sustained synaptic strength.","description":"Communication between neurons involves presynaptic neurotransmitter release which can be evoked by action potentials or occur spontaneously as a result of stochastic vesicle fusion. The Ca<sup>2+</sup>-binding double C<sub>2</sub> proteins Doc2a and -b were implicated in spontaneous and asynchronous evoked release, but the mechanism remains unclear. Here, we compared wildtype Doc2b with two Ca<sup>2+</sup> binding site mutants named DN and 6A, previously classified as gain- and loss-of-function mutants. They carry the substitutions D218,220N or D163,218,220,303,357,359A respectively. We found that both mutants bound phospholipids at low Ca<sup>2+</sup> concentrations and were membrane-associated in resting neurons, thus mimicking a Ca<sup>2+</sup>-activated state. Their overexpression in h","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Oct","modification":"2025-04-05T13:18:19.236Z","creation":"2019-10-30T08:18:48Z"},"accession":"S-EPMC6783474","cross_references":{"pubmed":["31594980"],"doi":["10.1038/s41598-019-50684-1"]}}