WDPCP

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0001736 establishment of planar polarity	NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	ACCEPT	Summary: WDPCP is a PCP effector that executes polarized cytoskeletal organization downstream of core PCP proteins. Reason: Fritz/WDPCP is one of the planar polarity effector proteins first defined in Drosophila wing hairs, and the vertebrate orthologs (same PANTHER subfamily PTHR13667:SF5) retain a polarity-effector role. Mouse Wdpcp mutants show misoriented cochlear hair-cell stereocilia and lose asymmetric Vangl2, and mutant fibroblasts fail to establish polarity, through loss of SEPT2-actin organization. WDPCP does some of the work of polarity establishment (it organizes the polarized actin/septin cytoskeleton) rather than merely being required for it. Not core PCP signaling, but an effector component of the process. Supporting Evidence: PMID:24302887 Examination of the cochlea of WdpcpCys40 mutants showed the hair cells were disarrayed, with some of the chevron misaligned PMID:24302887 decreased membrane ruffling, failure to establish cell polarity, and loss of directional cell migration. PMID:24302887 in Wdpcp-deficient cells, Sept2 was lost from the actin cytoskeleton, suggesting Wdpcp is required for Sept2 recruitment to actin filaments.
GO:0005886 plasma membrane	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: WDPCP is a peripheral, cortex-associated protein; plasma-membrane association is plausible but indirect. Reason: The UniProt "Cell membrane" subcellular location is by similarity to Xenopus Fritz (Q32NR9), where Fritz-GFP is concentrated at the cell cortex, and mouse Wdpcp sits on cortical actin and at focal adhesions. Its phosphoinositide-binding C-terminal tail provides a plausible mechanism for peripheral membrane association. WDPCP has no transmembrane segment. The cortical location (GO:0005938) is better supported than an integral plasma-membrane location, so this row is kept as non-core. Supporting Evidence: PMID:20671153 both sept2 fused to green fluorescent protein (sept2-GFP) and Fritz-GFP were concentrated at the cell cortex during CE PMID:24302887 Wdpcp is also found in the cytoplasm, where it is localized in the actin cytoskeleton and in focal adhesions. PMID:35427153 Wdpcp engages PIPs via the last 60 C-terminal residues.
GO:0005886 plasma membrane	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Cortical, membrane-proximal colocalization transferred from Xenopus Fritz. Reason: Xenopus Fritz (Q32NR9, same PANTHER subfamily PTHR13667:SF5 as human WDPCP) concentrates at the cell cortex together with SEPT2 during convergent extension. A colocalizes_with plasma membrane claim is consistent with that, but the cortex term carries the information; kept as non-core. Supporting Evidence: PMID:20671153 both sept2 fused to green fluorescent protein (sept2-GFP) and Fritz-GFP were concentrated at the cell cortex during CE
GO:0005886 plasma membrane	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Same claim as the other plasma membrane rows; peripheral cortical association. Reason: Transferred from Xenopus Fritz, which localizes to the cell cortex rather than being shown as an integral plasma membrane protein. Kept as non-core, consistent with the other plasma membrane rows. Supporting Evidence: PMID:20671153 both sept2 fused to green fluorescent protein (sept2-GFP) and Fritz-GFP were concentrated at the cell cortex during CE
GO:0005929 cilium	NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	ACCEPT	Summary: WDPCP localizes to cilia, at the transition zone, the ciliary base and along the axoneme. Reason: Vertebrate orthologs in the same subfamily localize to the ciliary transition zone, a ring at the ciliary base and the axoneme (mouse IMCD3 and MEF cells, zebrafish pronephros, Xenopus multiciliated cells). Cilium is a correct general term; the more specific transition zone and axoneme locations are captured in core_functions and in the axoneme rows. Supporting Evidence: PMID:24302887 Wdpcp is localized to the transition zone PMID:24302887 Wdpcp is localized to the ciliary axoneme and in a ring-like structure at the base of the cilia in IMCD3 cells
GO:0005930 axoneme	IEA GO_REF:0000044	ACCEPT	Summary: An axonemal pool of WDPCP is reported in three vertebrates, in addition to the transition-zone pool. Reason: The earlier review left this UNDECIDED because the transition zone is the best-resolved location. On re-reading the full texts, axonemal localization is reported directly in mouse IMCD3 cells (antibody against endogenous Wdpcp), along zebrafish pronephric cilia (lost in morphants, so the antibody is specific), and for Xenopus Fritz along multiciliated-cell axonemes. All three are orthologs in PTHR13667:SF5. The axoneme is therefore a genuine second ciliary pool, not a conflation with the ciliary base. Supporting Evidence: PMID:24302887 Wdpcp is localized to the ciliary axoneme and in a ring-like structure at the base of the cilia in IMCD3 cells PMID:24302887 Wdpcp antibody staining showed punctate Wdpcp localization in the ciliary axoneme in the pronephric tubule PMID:20671153 sept7 and Fritz were localized along ciliary axonemes and in distinct foci near basal bodies
GO:0005930 axoneme	ISS GO_REF:0000024	ACCEPT	Summary: Transferred from Xenopus Fritz, which localizes along ciliary axonemes. Reason: The donor Q32NR9 is the Xenopus ortholog in the same PANTHER subfamily, and its axonemal localization is reported directly; mouse and zebrafish Wdpcp show the same axonemal pool. Supporting Evidence: PMID:20671153 sept7 and Fritz were localized along ciliary axonemes and in distinct foci near basal bodies PMID:24302887 Wdpcp is localized to the ciliary axoneme and in a ring-like structure at the base of the cilia in IMCD3 cells
GO:0005938 cell cortex	ISS GO_REF:0000024	ACCEPT	Summary: WDPCP colocalizes with SEPT2 at the cell cortex, where it controls cortical septin recruitment. Reason: Xenopus Fritz-GFP and SEPT2-GFP concentrate at the cell cortex, and the cortical-to-cytoplasmic SEPT2 ratio falls in Fritz morphants. Mouse Wdpcp likewise colocalizes with SEPT2 on cortical actin and focal adhesions. This is the cytoplasmic functional site of WDPCP. Supporting Evidence: PMID:20671153 both sept2 fused to green fluorescent protein (sept2-GFP) and Fritz-GFP were concentrated at the cell cortex during CE PMID:20671153 the ratio of cortical-to-cytoplasmic sept2-GFP was consistently reduced in Fritz morphants compared with controls PMID:24302887 Wdpcp is also found in the cytoplasm, where it is localized in the actin cytoskeleton and in focal adhesions.
GO:0007399 nervous system development	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: A broad developmental consequence of the ciliary and polarity roles. Reason: PAINT placed this at the bilaterian node PTN001007408, from fly fritz and mouse Wdpcp. Human WDPCP descends from that node, and mouse Wdpcp mutants show neural tube dorsalization from defective cilium-dependent Shh signaling. The term describes an organismal outcome of WDPCP's cellular roles (ciliogenesis, cytoskeletal polarity), not a separate activity, so it is kept as non-core. Supporting Evidence: PMID:24302887 We also observed disruption of Shh signaling in the neural tube, which was indicated by dorsalization of the neural tube
GO:0016324 apical plasma membrane	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Apical, basal-body-proximal colocalization in multiciliated cells, transferred from Xenopus. Reason: In Xenopus multiciliated cells Fritz is in foci near the apically docked basal bodies and along axonemes, and Fritz is needed to keep SEPT2/SEPT7 at the apical surface. Colocalization with the apical membrane follows from that, but it describes the ciliary-base pool indirectly. Kept as non-core. Supporting Evidence: PMID:20671153 both sept7 and sept2 were restricted to the apical surface and axonemes of control multiciliated cells but were detected consistently throughout the cytoplasm of Fritz morphant cells
GO:0016476 regulation of embryonic cell shape	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Xenopus Fritz controls cell elongation and membrane stability during convergent extension via cortical septins. Reason: The donor's experimental basis is direct. Fritz morphant mesodermal cells fail to elongate and have unstable membranes, and Fritz acts through septins rather than through polarization itself. The cell-shape role is a cellular output of the cortical septin-recruitment function and is kept as non-core. Most of the evidence comes from morpholinos in a single species. Supporting Evidence: PMID:20671153 Thus, Fritz controls cell shape but not polarization during CE
GO:0021915 neural tube development	NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	KEEP AS NON CORE	Summary: An organismal developmental consequence of loss of cilia and Shh signaling. Reason: Mouse Wdpcp mutants show a neural tube patterning defect (dorsalization) secondary to defective ciliary Shh signaling. This is a downstream organismal phenotype of the ciliogenesis role, not a distinct activity. Kept as non-core rather than removed, since the NAS reflects a ComplexPortal complex-level statement. Supporting Evidence: PMID:24302887 We also observed disruption of Shh signaling in the neural tube, which was indicated by dorsalization of the neural tube
GO:0032185 septin cytoskeleton organization	ISS GO_REF:0000024	ACCEPT	Summary: WDPCP recruits and organizes septins at the cortex, on actin, and at the ciliary base. Reason: Xenopus Fritz controls cortical and ciliary septin localization and SEPT7 ring structure; mouse Wdpcp binds SEPT2 and is needed for SEPT2 recruitment to actin filaments and to the transition zone. WDPCP participates directly as the recruiting scaffold. This is a conserved core function within PTHR13667:SF5. Supporting Evidence: PMID:20671153 the ratio of cortical-to-cytoplasmic sept2-GFP was consistently reduced in Fritz morphants compared with controls PMID:24302887 in Wdpcp-deficient cells, Sept2 was lost from the actin cytoskeleton, suggesting Wdpcp is required for Sept2 recruitment to actin filaments.
GO:0032880 regulation of protein localization	ISS GO_REF:0000024	ACCEPT	Summary: WDPCP controls where septins and transition-zone proteins are localized. Reason: Both donor (Xenopus, septin localization) and mouse evidence (SEPT2, NPHP1 and MKS1 at the transition zone) support WDPCP as a determinant of protein localization. Its recruiting role is described more specifically by the establishment-of-protein-localization IBA, but this term is also correct. Supporting Evidence: PMID:24302887 These results show Wdpcp is required for recruitment of Mks1 and Nphp1 to the ciliary transition zone. PMID:20671153 both sept7 and sept2 were restricted to the apical surface and axonemes of control multiciliated cells but were detected consistently throughout the cytoplasm of Fritz morphant cells
GO:0035091 phosphatidylinositol binding	IEA GO_REF:0000107	ACCEPT	Summary: WDPCP binds monophosphorylated phosphoinositides through its disordered C-terminal tail. Reason: Recombinant mouse Wdpcp binds PIPs on its own, with PI(3)P > PI(5)P > PI(4)P, and the binding maps to the last 60 residues. The human Wdpcp C-terminal fragment (485-746) also binds PIP strips, and the BBS-associated S708F variant increases binding, so the activity is shown directly for the human protein too. The specificity is broad across monophosphates on lipid strips/arrays, so the general phosphatidylinositol binding term is as precise as the evidence allows. Supporting Evidence: PMID:35427153 Wdpcp engages PIPs via the last 60 C-terminal residues. PMID:35427153 individual subunits bind PI(3)P with highest affinity, followed by PI(5)P and PI(4)P PMID:35427153 HsWdpcp_485-746 (helical α-solenoid) binding to PIP strip for wild-type (WT) and S708F mutant
GO:0035091 phosphatidylinositol binding	ISS GO_REF:0000024	ACCEPT	Summary: The same claim as the IEA row; supported by direct mouse and human-fragment PIP-binding data. Reason: Donor mouse Wdpcp (Q8C456, PTHR13667:SF5) binds PIPs individually; the human C-terminal fragment binds as well. Supporting Evidence: PMID:35427153 Wdpcp engages PIPs via the last 60 C-terminal residues. PMID:35427153 HsWdpcp_485-746 (helical α-solenoid) binding to PIP strip for wild-type (WT) and S708F mutant
GO:0042073 intraciliary transport	NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	KEEP AS NON CORE	Summary: CPLANE acts upstream of IFT by loading peripheral IFT-A subunits at the basal body; it is not part of the moving train. Reason: Toriyama et al. show that CPLANE, including Wdpcp (knockdown gives similar effects), recruits peripheral IFT-A proteins to basal bodies. Without CPLANE the IFT-A core still moves bidirectionally, while IFT-B movement is impaired. In mouse Wdpcp mutants, IFT88 distribution is normal. WDPCP therefore contributes to assembling IFT particles at the ciliary base, which affects IFT, rather than carrying out intraciliary transport itself. The earlier ACCEPT overstated this, so the row is downgraded to non-core. No more specific GO process term for basal-body recruitment of IFT-A was found. Supporting Evidence: PMID:27158779 These data suggest that CPLANE acts by recruiting peripheral IFT-A proteins to the basal body for assembly onto the IFT-A core. PMID:27158779 Similar effects on IFT-A and IFT-B were observed after Wdpcp knockdown PMID:24302887 Ift88 distribution in the ciliary axoneme and basal body was unchanged in WdpcpCys40 mutant MEFs, indicating IFT transport is not disrupted by Wdpcp deficiency
GO:0042733 embryonic digit morphogenesis	IMP PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	KEEP AS NON CORE	Summary: Polydactyly in human WDPCP-variant patients and mouse mutants is a ciliopathy outcome of defective Shh signaling. Reason: The curator's IMP rests on a compound-heterozygous patient with postaxial polydactyly, with variant protein instability tested in Xenopus. Mouse Wdpcp mutants also have polydactyly with altered GLI3 processing. This is a valid but downstream developmental manifestation of WDPCP's ciliary role. Kept as non-core; the curator's IMP is not overruled. Supporting Evidence: PMID:27158779 In one patient, a 5-year-old male presenting with facial dysmorphism, tongue hamartoma, high arched palate, tooth abnormalities, and postaxial polydactyly, we found trans-heterozygous mutations in WDPCP.
GO:0043587 tongue morphogenesis	IMP PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	KEEP AS NON CORE	Summary: Tongue hamartoma in a WDPCP compound heterozygote; a downstream ciliopathy phenotype. Reason: Based on a single compound-heterozygous patient with tongue hamartoma (an oral-facial-digital feature). It is an organismal manifestation of a ciliary defect, not a WDPCP-specific morphogenetic activity. The curator's IMP is retained as non-core. Supporting Evidence: PMID:27158779 In one patient, a 5-year-old male presenting with facial dysmorphism, tongue hamartoma, high arched palate, tooth abnormalities, and postaxial polydactyly, we found trans-heterozygous mutations in WDPCP.
GO:0044782 cilium organization	IBA GO_REF:0000033	ACCEPT	Summary: A conserved role in cilium organization, inherited from the bilaterian fritz/WDPCP node. Reason: PAINT placed cilium organization at PTN001007408 from mouse and Xenopus experimental data. Human WDPCP is in the same subfamily (SF5) under that node, and no evidence of divergence exists. WDPCP builds the ciliary base by recruiting transition-zone proteins and peripheral IFT-A, which is direct participation. Supporting Evidence: PMID:24302887 These results show Wdpcp is required for recruitment of Mks1 and Nphp1 to the ciliary transition zone. PMID:27158779 These data suggest that CPLANE acts by recruiting peripheral IFT-A proteins to the basal body for assembly onto the IFT-A core.
GO:0045184 establishment of protein localization	IBA GO_REF:0000033	ACCEPT	Summary: WDPCP recruits SEPT2, NPHP1, MKS1 and peripheral IFT-A to their sites of action. Reason: The IBA from the bilaterian node is supported by the mouse recruitment data (SEPT2 to actin and the transition zone; NPHP1 and MKS1 to the transition zone) and by CPLANE-mediated IFT-A recruitment. WDPCP is the recruiting scaffold, so it does part of the work of the process. Supporting Evidence: PMID:24302887 These results show Wdpcp is required for recruitment of Mks1 and Nphp1 to the ciliary transition zone. PMID:24302887 in Wdpcp-deficient cells, Sept2 was lost from the actin cytoskeleton, suggesting Wdpcp is required for Sept2 recruitment to actin filaments.
GO:0060021 roof of mouth development	IMP PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	KEEP AS NON CORE	Summary: High arched palate in a WDPCP compound heterozygote; a downstream ciliopathy phenotype. Reason: As for tongue morphogenesis, this rests on one patient's craniofacial features. It is a valid developmental manifestation of the ciliary role, not a separate function. The curator's IMP is kept as non-core. Supporting Evidence: PMID:27158779 In one patient, a 5-year-old male presenting with facial dysmorphism, tongue hamartoma, high arched palate, tooth abnormalities, and postaxial polydactyly, we found trans-heterozygous mutations in WDPCP.
GO:0060271 cilium assembly	ISS GO_REF:0000024	ACCEPT	Summary: WDPCP is required for, and participates in, ciliogenesis in multiple vertebrates. Reason: Xenopus Fritz morphants have defective ciliogenesis with disorganized ciliary-base septin rings, and mouse Wdpcp mutant cells rarely form cilia. WDPCP participates by assembling transition-zone and IFT-A components at the ciliary base. This is the core ciliary process term. Supporting Evidence: PMID:20671153 sept7 and Fritz were localized along ciliary axonemes and in distinct foci near basal bodies PMID:24302887 These results show Wdpcp is required for recruitment of Mks1 and Nphp1 to the ciliary transition zone.
GO:0097541 axonemal basal plate	IBA GO_REF:0000033	ACCEPT	Summary: A transition-zone-region location propagated from mouse Wdpcp. Reason: The axonemal basal plate lies at the distal end of the ciliary transition zone. Mouse Wdpcp is localized at the transition zone, the source of the MGI seed. Light-microscopy resolution cannot separate the basal plate from the rest of the transition zone, so the precise substructure is not established. The ciliary transition zone (GO:0035869) is recorded as the best-supported location in core_functions. Accepted in deference to the PAINT and MGI curation. Supporting Evidence: PMID:24302887 Wdpcp is localized to the transition zone
GO:0097541 axonemal basal plate	IEA GO_REF:0000107	ACCEPT	Summary: An Ensembl Compara transfer of the mouse transition-zone-region location. Reason: Same claim as the IBA row; consistent action. Supporting Evidence: PMID:24302887 Wdpcp is localized to the transition zone
GO:1902017 regulation of cilium assembly	NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ...	KEEP AS NON CORE	Summary: WDPCP participates in cilium assembly; the evidence does not establish a regulatory role. Reason: The CPLANE data show WDPCP acting as part of the assembly machinery (recruitment of IFT-A and transition-zone proteins). They do not show it modulating the rate or extent of ciliogenesis as a regulator. The participation term cilium assembly (GO:0060271) is accepted separately. This complex-level NAS is kept as non-core rather than accepted. Supporting Evidence: PMID:27158779 These data suggest that CPLANE acts by recruiting peripheral IFT-A proteins to the basal body for assembly onto the IFT-A core.
GO:0035869 ciliary transition zone	ISS PMID:24302887 Wdpcp, a PCP protein required for ciliogenesis, regulates di...	NEW	Summary: WDPCP localizes to the ciliary transition zone, its best-resolved ciliary location. Reason: Mouse Wdpcp (Q8C456, PTHR13667:SF5, same subfamily as human WDPCP under PAINT node PTN001007408) is localized to the transition zone independently of MKS1, and is required there for SEPT2, NPHP1 and MKS1 recruitment. GOA carries only the more specific axonemal basal plate and the general cilium term. The transition zone is the compartment the evidence actually resolves. Supporting Evidence: PMID:24302887 Wdpcp is localized to the transition zone PMID:24302887 These results show Wdpcp is required for recruitment of Mks1 and Nphp1 to the ciliary transition zone.

Gene Description

Existing Annotations Review

Core Functions

CPLANE scaffold subunit at the ciliary base. It recruits transition-zone proteins (SEPT2, NPHP1, MKS1) and, with INTU and FUZ, peripheral IFT-A subunits needed for cilium assembly. Its C-terminal tail binds phosphoinositides.

A cortical planar polarity effector. It recruits SEPT2 to actin filaments and the cell cortex, organizing the septin-actin cytoskeleton for cell-shape stability, polarized protrusion and directional migration.

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