Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutations in the second C2 domain of synaptotagmin disrupt synaptic transmission at Drosophila neuromuscular junctions.

The Journal of comparative neurology - 16 Jul 2001

Mackler J M, Reist N E

Abstract excerpt

The synaptic vesicle protein, synaptotagmin, has been hypothesized to mediate several functions in neurotransmitter release including calcium sensing, vesicle recycling, and synaptic vesicle docking. These hypotheses are based on evidence from in vitro binding assays, peptide and antibody injection experiments, and genetic knockout studies. Synaptotagmin contains two domains that are homologous to the calcium ion...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Calcium-Binding Proteins
Share to Electrophysiology
Share to Larva

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Neuromuscular Junction

Share to Synaptic Transmission

Share to Synaptotagmin I

Share to Synaptotagmins

Share to Transgenes

Source

Identifiers

PMID: 11413542

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the second C2 domain of synaptotagmin disrupt synaptic transmission at Drosophila neuromuscular junctions.PMID 11413542Read ↗

The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo.Semantic proximity Read ↗

synaptotagmin mutants reveal essential functions for the C2B domain in Ca2+-triggered fusion and recycling of synaptic vesicles in vivo.Semantic proximity Read ↗

Synaptotagmin I stabilizes synaptic vesicles via its C(2)A polylysine motif.Semantic proximity Read ↗

The C2A domain of synaptotagmin alters the kinetics of voltage-gated Ca2+ channels Ca(v)1.2 (Lc-type) and Ca(v)2.3 (R-type).Semantic proximity Read ↗

C2B polylysine motif of synaptotagmin facilitates a Ca2+-independent stage of synaptic vesicle priming in vivo.Semantic proximity Read ↗

Genetic analysis of synaptotagmin C2 domain specificity in regulating spontaneous and evoked neurotransmitter release.Semantic proximity Read ↗

Drosophila studies support a role for a presynaptic synaptotagmin mutation in a human congenital myasthenic syndrome.Semantic proximity Read ↗

Disease-causing mutations in Synaptotagmin can act via dominant-negative, gain-of-function or haploinsufficient mechanismsSemantic proximity Read ↗

Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release.Semantic proximity Read ↗

Synaptotagmin 2 mutations cause an autosomal-dominant form of lambert-eaton myasthenic syndrome and nonprogressive motor neuropathy.Semantic proximity Read ↗

Functional and biochemical analysis of the C2 domains of synaptotagmin IV.Semantic proximity Read ↗

Differential expression and function of synaptotagmin 1 isoforms in Caenorhabditis elegans.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.