Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
A role for the clathrin assembly domain of AP180 in synaptic vesicle endocytosis.
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Squid AP180 encodes a 751 amino acid protein with 40% sequence identity to mouse AP180
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The N-terminal inositide-binding domain is highly conserved while the C-terminal clathrin assembly domain is divergent
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Recombinant squid AP180 assembles clathrin in vitro
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Microinjection of the C-terminal domain into squid giant presynaptic terminal enhanced synaptic transmission
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An inhibitory peptide from the C-terminal domain completely blocked synaptic transmission
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Electron microscopy showed depletion of synaptic vesicles and coated vesicles upon AP180 inhibition
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AP180 clathrin assembly is necessary for maintaining a pool of releasable synaptic vesicles
Eps15 homology domain-NPF motif interactions regulate clathrin coat assembly during synaptic vesicle recycling.
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Eps15 potently stimulates AP180-mediated clathrin assembly at physiological pH
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Eps15 binds squid AP180 at sites containing NPF motifs
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NPF-derived peptides inhibit Eps15-stimulated clathrin assembly in vitro
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Injection of NPF peptides into squid presynaptic terminals inhibits clathrin-coated pit and vesicle formation
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Eps15 EH domain-NPF motif interactions regulate clathrin coat assembly in vivo
A conserved clathrin assembly motif essential for synaptic vesicle endocytosis.
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AP180 binds to the N-terminal domain of clathrin heavy chain
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DLL motifs in AP180 mediate clathrin binding and assembly
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Progressive deletion of DLL motifs caused gradual reduction in clathrin assembly
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Peptides containing DLL motifs competitively inhibited clathrin assembly
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Microinjection of DLL peptides into squid presynaptic terminals blocked synaptic transmission and endocytosis
Clathrin and synaptic vesicle endocytosis studies at the squid giant synapse.
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Procedures that prevent clathrin assembly completely prevent membrane budding during endocytosis
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Impairment of AP180 and AP-2 adaptor protein binding blocks coated pit formation
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A clathrin-dependent pathway is the primary means of synaptic vesicle recycling at the squid giant synapse
Synaptic vesicle size and number are regulated by a clathrin adaptor protein required for endocytosis.
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Loss of the Drosophila AP180 homolog (LAP) severely impairs synaptic vesicle endocytosis and causes abnormally enlarged, irregular synaptic vesicles.
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AP180 normally constrains vesicle size during clathrin-dependent reassembly, and its absence leads to increased miniature excitatory junction potential amplitudes reflecting larger vesicle quantal content.
Vesicular Synaptobrevin/VAMP2 Levels Guarded by AP180 Control Efficient Neurotransmission.
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AP180-knockout mice show greatly reduced VAMP2 levels in synaptic vesicles, resulting in impaired neurotransmitter release, epileptic seizures, and premature death.
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AP180 is required for proper sorting of VAMP2/synaptobrevin into synaptic vesicles during clathrin-mediated endocytosis at nerve terminals.
An extended interaction site determines binding between AP180 and AP2 in clathrin mediated endocytosis.
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NMR mapping of the AP180 disordered region reveals a high-affinity AP-2 beta2 appendage binding site with interaction strength orders of magnitude greater than previously known sites.
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AP180 organizes a dynamic interaction network bridging AP-2 and clathrin at nascent endocytic pits, acting as both clathrin recruiter and adaptor organizer.
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The AP180 IDR contains multiple small AP-2 interaction interfaces plus one dominant binding site, creating a multivalent interaction landscape.