NCU09721 is a large beta-adaptin assigned to the AP-1 cargo-adaptor complex by curated phylogenetic inference. It provides a noncatalytic scaffold for membrane-cargo sorting within the Golgi/endosomal trafficking system. Characterized filamentous-fungal AP-1 complexes support post-Golgi secretion, endosome recycling, and clathrin-associated carrier traffic. These conserved roles support Golgi and carrier-membrane recruitment in Neurospora crassa, while its individual cargoes and direct clathrin-binding mechanism remain uncharacterized.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005737 cytoplasm | IEA GO_REF:0000117 | ACCEPT | Summary: Beta-adaptin is a cytoplasmic coat-adaptor subunit that is recruited to the cytoplasmic surfaces of intracellular membranes. The AP-family fold and characterized fungal AP1 assemblies support this broad location. Supporting Evidence: file:NEUCR/NCU09721/NCU09721-uniprot.txt DR InterPro; IPR026739; AP_beta. PMID:36836259 FgAP1Ξ² interacts with FgAP1Ο, FgAP1Ξ³, and FgAP1ΞΌ PMID:36836259 FgAP1Ξ²-GFP, FgAP1Ξ³-GFP, and FgAP1ΞΌ-GFP also localize to the Golgi apparatus. |
| GO:0005802 trans-Golgi network | IBA GO_REF:0000033 | ACCEPT | Summary: The target AP-1 membership IBA and beta-adaptin domain support transfer from experimentally localized filamentous-fungal AP1 beta subunits. Fusarium AP1 beta colocalizes with a trans-Golgi marker, supporting the TGN assignment. Supporting Evidence: PMID:36836259 FgAP1Ξ²-GFP, FgAP1Ξ³-GFP, and FgAP1ΞΌ-GFP also localize to the Golgi apparatus. |
| GO:0006886 intracellular protein transport | IEA GO_REF:0000002 | ACCEPT | Summary: Characterized filamentous-fungal AP1 supports secretory carrier sorting and endosome recycling. The curated AP1-family assignment grounds a conserved role in intracellular vesicle-mediated protein traffic. Supporting Evidence: PMID:29925567 its role in clathrin-dependent maintenance of polar traffic of specific membrane cargoes toward the apex of growing hyphae. We provide evidence that AP-1 is involved in both anterograde sorting of RabERab11-labeled SVs and RabA/BRab5-dependent endosome recycling. |
| GO:0006897 endocytosis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: AP1 contributes to endosomal recycling and endocytic itineraries in filamentous fungi; Fusarium AP1 loss delays internalization of the endocytic dye FM4-64. This supports a process contribution without reassigning the beta subunit to AP2 or claiming a primary plasma-membrane uptake function. Supporting Evidence: PMID:36836259 the loss of FgAP1Ο blocks the transportation of the v-SNARE protein FgSnc1 from the Golgi to the plasma membrane and delays the internalization of FM4-64 dye into the vacuole. |
| GO:0012505 endomembrane system | IEA GO_REF:0000044 | MODIFY | Summary: The AP1-family placement and direct Golgi localization of the related Fusarium beta subunit support a more precise trans-Golgi-network compartment. Proposed replacements: trans-Golgi network Supporting Evidence: PMID:36836259 FgAP1Ξ²-GFP, FgAP1Ξ³-GFP, and FgAP1ΞΌ-GFP also localize to the Golgi apparatus. |
| GO:0015031 protein transport | IEA GO_REF:0000002 | ACCEPT | Summary: Characterized filamentous-fungal AP1 supports secretory carrier sorting and endosome recycling. The curated AP1-family assignment grounds a conserved role in intracellular vesicle-mediated protein traffic. Supporting Evidence: PMID:29925567 its role in clathrin-dependent maintenance of polar traffic of specific membrane cargoes toward the apex of growing hyphae. We provide evidence that AP-1 is involved in both anterograde sorting of RabERab11-labeled SVs and RabA/BRab5-dependent endosome recycling. |
| GO:0016192 vesicle-mediated transport | IEA GO_REF:0000002 | ACCEPT | Summary: Characterized filamentous-fungal AP1 supports secretory carrier sorting and endosome recycling. The curated AP1-family assignment grounds a conserved role in intracellular vesicle-mediated protein traffic. Supporting Evidence: PMID:29925567 its role in clathrin-dependent maintenance of polar traffic of specific membrane cargoes toward the apex of growing hyphae. We provide evidence that AP-1 is involved in both anterograde sorting of RabERab11-labeled SVs and RabA/BRab5-dependent endosome recycling. |
| GO:0030117 membrane coat | IEA GO_REF:0000002 | ACCEPT | Summary: AP1 beta forms part of a membrane-associated cargo-adaptor coat. Filamentous-fungal AP1 assembles with other AP1 subunits and supports clathrin-dependent traffic, consistent with membrane coat membership. Supporting Evidence: file:NEUCR/NCU09721/NCU09721-uniprot.txt DR InterPro; IPR026739; AP_beta. PMID:36836259 FgAP1Ξ² interacts with FgAP1Ο, FgAP1Ξ³, and FgAP1ΞΌ PMID:29925567 its role in clathrin-dependent maintenance of polar traffic of specific membrane cargoes toward the apex of growing hyphae. We provide evidence that AP-1 is involved in both anterograde sorting of RabERab11-labeled SVs and RabA/BRab5-dependent endosome recycling. |
| GO:0030121 AP-1 adaptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: The curated IBA at PTN000123672 assigns this beta-adaptin to AP1 with experimentally characterized fungal AP1 beta descendants. The AP-beta domain and fungal AP1 subunit-interaction experiments support that inherited complex role; it is not inferred from the generic beta1/2/4 domain alone. Supporting Evidence: file:NEUCR/NCU09721/NCU09721-uniprot.txt DR InterPro; IPR026739; AP_beta. PMID:36836259 FgAP1Ξ² interacts with FgAP1Ο, FgAP1Ξ³, and FgAP1ΞΌ |
| GO:0030276 clathrin binding | IEA GO_REF:0000002 | UNDECIDED | Summary: Dikaryan beta-adaptins lack the canonical C-terminal clathrin-binding appendage, but Aspergillus AP1 beta uses alternative tail motifs. The target sequence contains LLDID at residues 629β633, matching one tested Aspergillus motif, and terminal LLGLF at 745β749; the stronger Aspergillus LLNGF motif is not identical. These observations support clathrin-association plausibility, but short motif similarity and complex traffic do not establish the exact intrinsic target-binding mechanism. Direct target binding remains unresolved. Supporting Evidence: PMID:28220754 clathrin binding domains are also missing from the AP-1 Ξ² subunit (Ξ²1) of all Dikarya PMID:29925567 its role in clathrin-dependent maintenance of polar traffic of specific membrane cargoes toward the apex of growing hyphae. We provide evidence that AP-1 is involved in both anterograde sorting of RabERab11-labeled SVs and RabA/BRab5-dependent endosome recycling. file:NEUCR/NCU09721/NCU09721-uniprot.txt QRQNAAENPI AASVAAAAKG GQQNNVENLL DIDFDGGAPA |
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