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.
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Combined Automated Annotation using Multiple IEA Methods.
The polarity protein Inturned links NPHP4 to Daam1 to control the subapical actin network in multiciliated cells.
The ciliopathy-associated CPLANE proteins direct basal body recruitment of intraflagellar transport machinery.
An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Deep research on INTU function
Falcon (Edison) deep research on INTU function
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INTU is a core CPLANE subunit that is best supported as a basal-body localized scaffold/effector recruiting and organizing IFT machinery (notably IFT-A subset) to enable ciliogenesis; structural work places an Intu-Fuz heterodimer within a crescent-like CPLANE complex, and CPLANE proteins show phosphoinositide binding with a preference for PI(3)P, consistent with operating on PI(3)P-rich vesicles near the nascent ciliary vesicle/base of cilia.
"INTU is best supported as a basal-body localized CPLANE scaffold/effector that recruits/organizes IFT machinery (notably IFT-A subset effects) and thereby enables ciliogenesis."
Structure of the ciliogenesis-associated CPLANE complex.
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The mammalian CPLANE complex is a biochemically stable Wdpcp-Inturned-Fuzzy assembly resolved by cryo-EM at ~3.35 Å, with INTU contributing PDZ and three longin-like domains (LD1-LD3) that form extensive interfaces with Wdpcp and Fuz; the complex adopts a crescent-like architecture in which the Intu-Fuz heterodimer is a major architectural element.
"mammalian CPLANE proteins comprise a bona fide complex and report the near-atomic resolution structures of the human Wdpcp-Inturned-Fuzzy complex and of the mouse Wdpcp-Inturned-Fuzzy complex bound to the small guanosine triphosphatase Rsg1."
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CPLANE proteins, including INTU, directly bind phosphoinositides with a clear preference for PI(3)P; the N-terminal ~300 residues of INTU (encompassing the PDZ region) mediate the strongest PIP binding, providing experimental support for INTU's phosphatidylinositol binding annotation and refining it to PI(3)P binding linked to membrane association at the ciliary base.
"the crescent-shaped CPLANE complex binds phospholipids such as phosphatidylinositol 3-phosphate via multiple modules and a CPLANE ciliopathy mutant exhibits aberrant lipid binding."
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CPLANE proteins act at late stages of ciliogenesis — CPLANE, Rsg1, and Rab23 mutants initiate cilium assembly but arrest at the ciliary vesicle (CV) stage — supporting a role for INTU in vesicle- stage ciliogenesis rather than in mature axonemal transport.
"CPLANE proteins likely operate at late phases of ciliogenesis since CPLANE, Rsg1, and Rab23 mutants initiate cilium assembly yet arrest at the CV stage"
CPLANE Complex and Ciliopathies.
The CPLANE protein Fuzzy regulates ciliogenesis by suppressing actin polymerization at the base of the primary cilium via p190A RhoGAP.