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

The Liprin homology domain is essential for the homomeric interaction of SYD-2/Liprin-α protein in presynaptic assembly.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 9 Nov 2011

Taru Hidenori, Jin Yishi

Abstract excerpt

Synapses are asymmetric structures that are specialized for neuronal signal transduction. A unique set of proteins is present at the presynaptic active zone, which is a core structure essential for neurotransmitter release. In Caenorhabditis elegans HSN neurons, SYD-2, a Liprin-α family protein, acts together with a GAP protein SYD-1 to promote presynaptic assembly. Previous studies have shown that elevating the...

Read the complete abstract on PubMed

Topics

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

Share to Caenorhabditis elegans Proteins
Share to Cell Line, Transformed

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

Share to Chlorocebus aethiops

Share to Intercellular Signaling Peptides and Proteins

Share to Motor Neurons

Share to Phosphoproteins

Share to Presynaptic Terminals

Share to Synapses

Source

Open in PubMed Open full text

Identifiers

PMID: 22072677
DOI: 10.1523/JNEUROSCI.0002-11.2011
PMCID: PMC3500560

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

The Liprin homology domain is essential for the homomeric interaction of SYD-2/Liprin-α protein in presynaptic assembly.PMID 22072677Read ↗

SYD-2 Liprin-alpha organizes presynaptic active zone formation through ELKS.Semantic proximity Read ↗

Intramolecular regulation of presynaptic scaffold protein SYD-2/liprin-α.Semantic proximity Read ↗

Hierarchical assembly of presynaptic components in defined C. elegans synapses.Semantic proximity Read ↗

The liprin protein SYD-2 regulates the differentiation of presynaptic termini in C. elegans.Semantic proximity Read ↗

RSY-1 is a local inhibitor of presynaptic assembly in C. elegans.Semantic proximity Read ↗

The C2H2 zinc-finger protein SYD-9 is a putative posttranscriptional regulator for synaptic transmission.Semantic proximity Read ↗

Systematic analyses of rpm-1 suppressors reveal roles for ESS-2 in mRNA splicing in Caenorhabditis elegans.Semantic proximity Read ↗

Assembly of synaptic active zones requires phase separation of scaffold molecules.Semantic proximity Read ↗

NAB-1 instructs synapse assembly by linking adhesion molecules and F-actin to active zone proteins.Semantic proximity Read ↗

The presynaptic dense projection of the Caenorhabditis elegans cholinergic neuromuscular junction localizes synaptic vesicles at the active zone through SYD-2/liprin and UNC-10/RIM-dependent interactions.Semantic proximity Read ↗

HLB-1 functions as a new regulator for the organization and function of neuromuscular junctions in nematode Caenorhabditis elegans.Semantic proximity Read ↗

A Syd-1 homologue regulates pre- and postsynaptic maturation in Drosophila.Semantic proximity Read ↗

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