Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic assignment of GO terms using logical inference, based on on GO logical definitions
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Multimodal cell maps as a foundation for structural and functional genomics.
AAGAB Controls AP2 Adaptor Assembly in Clathrin-Mediated Endocytosis.
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AAGAB acts as a chaperone for the AP-2 alpha subunit monomer, and AP-2 assembly begins with an AAGAB-alpha subunit complex.
"AAGAB acts as a specific chaperone for the α subunit monomer."
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AP-2 adaptor assembly takes place in the cytosol before the assembled complex is trafficked to the cell surface, which is why cytosol is the functionally relevant location for AAGAB.
"assembly of the AP2 adaptor complex in the cytosol, prior to the trafficking of the adaptor complex to the cell surface."
AAGAB is an assembly chaperone regulating AP1 and AP2 clathrin adaptors.
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AAGAB is an assembly chaperone for both AP-1 and AP-2 clathrin adaptor complexes.
"AAGAB is an assembly chaperone regulating AP1 and AP2 clathrin adaptors."
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AAGAB promotes AP-1 assembly by binding and stabilising the gamma and sigma subunits; mutation abolishes AP-1 assembly and disrupts AP-1-mediated cargo trafficking.
"AAGAB promotes AP1 assembly by binding and stabilizing the γ and σ subunits of AP1"
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The requirement is specific to particular adaptor complexes - AAGAB is not needed for AP-3 formation.
"However, AAGAB is not involved in the formation of other adaptor complexes, including AP3."
The adaptor protein chaperone AAGAB stabilizes AP-4 complex subunits.
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AAGAB binds and stabilises the AP-4 epsilon and sigma4 subunits, promoting AP-4 complex assembly; knockout cells accumulate ATG9A at the TGN like AP-4 subunit mutants.
"we report that the alpha- and gamma-adaptin-binding protein (AAGAB, also known as p34) binds to and stabilizes the AP-4 ε and σ4 subunits, thus promoting complex assembly."
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AP-4 assembly is not a spontaneous process but requires AAGAB.
"These findings demonstrate that AP-4 assembly is not spontaneous but AAGAB-assisted,"
Oligomer-to-monomer transition underlies the chaperone function of AAGAB in AP1/AP2 assembly.
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AAGAB is a chaperone governing assembly of the heterotetrameric AP-1 and AP-2 complexes; it is a homodimer before client binding and converts to monomer on binding adaptor subunits, using one C-terminal surface for both AP1-gamma and AP2-alpha.
"Alpha and gamma adaptin-binding protein (AAGAB) is a chaperone governing the assembly of the heterotetrameric adaptor complexes 1 and 2 (AP1 and AP2) involved in clathrin-mediated membrane trafficking."
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Assembly chaperones are a recognised class of proteins that facilitate protein complex assembly, distinct from folding chaperones.
"Assembly of protein complexes is facilitated by assembly chaperones."
Haploinsufficiency for AAGAB causes clinically heterogeneous forms of punctate palmoplantar keratoderma.
Nonsense mutations in AAGAB cause punctate palmoplantar keratoderma type Buschke-Fischer-Brauer.
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Exome sequencing in five affected individuals from three families identified two heterozygous AAGAB nonsense mutations causing punctate palmoplantar keratoderma type 1; the paper's own functional reading of AAGAB is only the hedged suggestion that it may act as a trafficking chaperone.
"AAGAB encodes the alpha-and gamma-adaptin-binding protein p34 and might play a role in membrane traffic as a chaperone"
An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex.
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AAGAB initiates AP2 assembly by stabilising the alpha and sigma2 subunits, but the resulting AAGAB:alpha:sigma2 complex cannot recruit further AP2 subunits; CCDC32 takes over the intermediate and templates recruitment of mu2 and beta2. This is the direct evidence that AAGAB leaves before the tetramer is complete.
"AAGAB initiates AP2 assembly by stabilizing its α and σ2 subunits, but the AAGAB:α:σ2 complex cannot recruit additional AP2 subunits"
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The handover is the paper's headline mechanism and generalises beyond AP2.
"AP2 is assembled by a handover mechanism switching from AAGAB-based initiation complexes to CCDC32-based template complexes"
Affinage mechanistic annotation for AAGAB (human)
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Machine-fetched Affinage record (trust gates passed) describing AAGAB as an assembly chaperone that nucleates AP1, AP2 and AP4 formation via an N-terminal pseudoGTPase domain and a C-terminal dimerisation domain.
"AAGAB (p34) is an assembly chaperone for heterotetrameric clathrin adaptor protein complexes, nucleating the formation of AP1, AP2, and AP4 that drive clathrin-mediated membrane trafficking"