Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Characterization of the adaptor-related protein complex, AP-3.
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AP-3 is a heterotetrameric complex with beta3A (AP3B1), delta, mu3, and sigma3 subunits
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AP-3 localizes to Golgi and peripheral endosomal structures
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AP-3 is involved in protein sorting to lysosomes/LROs
Association of the AP-3 adaptor complex with clathrin.
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AP-3 associates with clathrin via the beta3 appendage domain
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AP-3 colocalizes with clathrin in cells
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AP-3 functions in signal-mediated protein sorting to endosomal-lysosomal organelles
The beta3A subunit gene (Ap3b1) of the AP-3 adaptor complex is altered in the mouse hypopigmentation mutant pearl, a model for Hermansky-Pudlak syndrome and night blindness.
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Mutations in Ap3b1 cause the pearl mouse phenotype
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Pearl mice have abnormal lysosomes, melanosomes, and platelet dense granules
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Pearl is a model for human HPS
AP-3 mediates tyrosinase but not TRP-1 trafficking in human melanocytes.
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AP-3 is required for tyrosinase trafficking to melanosomes
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HPS-2 melanocytes show abnormal tyrosinase localization
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Tyrosinase and TRP-1 use different trafficking mechanisms
Involvement of beta3A subunit of adaptor protein-3 in intracellular trafficking of receptor-like protein tyrosine phosphatase PCP-2.
Integral and associated lysosomal membrane proteins.
AP-1 and KIF13A coordinate endosomal sorting and positioning during melanosome biogenesis.
Defining the membrane proteome of NK cells.
BLOC-2, AP-3, and AP-1 proteins function in concert with Rab38 and Rab32 proteins to mediate protein trafficking to lysosome-related organelles.
Cell type-specific Rab32 and Rab38 cooperate with the ubiquitous lysosome biogenesis machinery to synthesize specialized lysosome-related organelles.
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AP-3 localizes to early endosomal tubular domains
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Rab32/38 redirect AP-3 to LRO biogenesis pathways
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AP-3 mutations cause HPS with defects in melanosomes, dense granules, lamellar bodies
Ribosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson's disease.
LRRK2 and RAB7L1 coordinately regulate axonal morphology and lysosome integrity in diverse cellular contexts.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
AP3B1 deep research (cyberian)
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AP-3 exists in a constitutively open, active conformation (Begley 2024)
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Stepwise mechanism of AP-3 activation and coat polymerization elucidated
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AP-3 cooperates with BLOC-1 and BLOC-2 for LRO biogenesis
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Clathrin binding via beta3 hinge is dispensable for AP-3 cargo sorting function
A structure-based mechanism for initiation of AP-3 coated vesicle formation.
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Cryo-EM reveals AP-3 exists in constitutively open conformation, unlike AP-1/AP-2
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Initial Arf1-GTP binds to delta subunit, second Arf1 binds beta3 after cargo engagement
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Two amphipathic helices in AP-3 (delta and mu3) insert into lipid bilayer for membrane deformation
ADP-Ribosylation Factor 1 (ARF1) Regulates Recruitment of the AP-3 Adaptor Complex to Membranes.
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AP-3 membrane recruitment is Arf1-GTP dependent
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Brefeldin A inhibits AP-3 membrane association
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Arf1 is the most potent Arf family member for AP-3 recruitment
An Ear-Core Interaction Regulates the Recruitment of the AP-3 Complex to Membranes.
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Delta-ear domain interacts with sigma3 subunit
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This intramolecular interaction inhibits Arf1 binding and membrane recruitment
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Autoinhibitory mechanism regulates AP-3 membrane engagement
Structural basis for the recognition of tyrosine-based sorting signals by the μ3A subunit of the AP-3 adaptor complex.
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Crystal structure of mu3A C-terminal domain at 1.85 A resolution
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YXXF signals bind with 14-19 uM affinity, ~10-fold weaker than mu2
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Less basic surface explains AP-3 preference for intracellular membranes over plasma membrane
Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins.
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Only ~4% of AP-3 labeling at TGN, 43% at endosomal tubules
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LAMP-1/LAMP-2 enriched 8.5/3.6-fold in AP-3-positive domains
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CD63 shows 1.8-3.3-fold increased surface levels in AP-3-deficient cells
BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate protein trafficking on endosomes.
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Physical and functional interaction between BLOC-1 and AP-3
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BLOC-1/AP-3 assembly stability regulated by GTP
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Tyrosinase trafficked by AP-3-dependent, BLOC-1-independent pathway
The Neuronal Form of Adaptor Protein-3 Is Required for Synaptic Vesicle Formation from Endosomes.
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Only neuronal AP-3 (AP-3B with beta3B) generates synaptic vesicles from endosomes
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Neuronal AP-3 concentrates in axonal varicosities
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Loss of neuronal AP-3 causes seizures, balance problems, hearing defects