WDPCP is a component of the CPLANE ciliogenesis machinery and a regulator of cytoskeletal organization and planar cell polarity. It acts at the ciliary base and in cytoplasmic actin-associated pools, helping recruit septins and other proteins required for cilia formation and directional cell behavior. Its C-terminal region binds phosphoinositides. Loss of WDPCP disrupts ciliogenesis and embryonic patterning.
| 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 helps establish planar cell polarity through cytoskeletal organization. Reason: Mouse loss-of-function analysis links WDPCP-dependent actin and septin organization to polarity and directional migration, independently of simply observing a ciliary phenotype. Supporting Evidence: PMID:24302887 in Wdpcp-deficient cells, Sept2 was lost from the actin cytoskeleton, suggesting Wdpcp is required for Sept2 recruitment to actin filaments. PMID:24302887 decreased membrane ruffling, failure to establish cell polarity, and loss of directional cell migration. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: WDPCP occupies cortical and membrane-associated cytoskeletal pools. Reason: Localization to focal adhesions and actin structures, together with phosphoinositide binding, supports membrane/cortical association. This is a peripheral scaffold, not an integral membrane receptor. Supporting Evidence: 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 | ACCEPT | Summary: WDPCP occupies cortical and membrane-associated cytoskeletal pools. Reason: Localization to focal adhesions and actin structures, together with phosphoinositide binding, supports membrane/cortical association. This is a peripheral scaffold, not an integral membrane receptor. Supporting Evidence: 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 | ACCEPT | Summary: WDPCP occupies cortical and membrane-associated cytoskeletal pools. Reason: Localization to focal adhesions and actin structures, together with phosphoinositide binding, supports membrane/cortical association. This is a peripheral scaffold, not an integral membrane receptor. Supporting Evidence: 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:0005929 cilium | NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ... | ACCEPT | Summary: WDPCP acts at the base of cilia. Reason: Transition-zone localization and recruitment functions support the ciliary-base annotations. The broad cilium term includes this specialized basal pool. Supporting Evidence: PMID:24302887 Wdpcp is localized to the 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:0005930 axoneme | IEA GO_REF:0000044 | UNDECIDED | Summary: Axonemal localization needs more precise spatial evidence. Reason: The best resolved evidence places WDPCP at the transition zone/ciliary base. The retrieved text does not resolve whether the transferred axoneme annotation denotes an additional axonemal pool or conflates the base with the shaft. Basal localization alone does not refute it. Supporting Evidence: PMID:24302887 Wdpcp is localized to the transition zone |
| GO:0005930 axoneme | ISS GO_REF:0000024 | UNDECIDED | Summary: Axonemal localization needs more precise spatial evidence. Reason: The best resolved evidence places WDPCP at the transition zone/ciliary base. The retrieved text does not resolve whether the transferred axoneme annotation denotes an additional axonemal pool or conflates the base with the shaft. Basal localization alone does not refute it. Supporting Evidence: PMID:24302887 Wdpcp is localized to the transition zone |
| GO:0005938 cell cortex | ISS GO_REF:0000024 | ACCEPT | Summary: WDPCP occupies cortical and membrane-associated cytoskeletal pools. Reason: Localization to focal adhesions and actin structures, together with phosphoinositide binding, supports membrane/cortical association. This is a peripheral scaffold, not an integral membrane receptor. Supporting Evidence: 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:0007399 nervous system development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: WDPCP-dependent cilia and polarity support embryonic development. Reason: Developmental defects are consistent with its cellular role but do not define an additional tissue-specific molecular activity. Supporting Evidence: PMID:24302887 decreased membrane ruffling, failure to establish cell polarity, and loss of directional cell migration. 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:0016324 apical plasma membrane | ISS GO_REF:0000024 | ACCEPT | Summary: WDPCP occupies cortical and membrane-associated cytoskeletal pools. Reason: Localization to focal adhesions and actin structures, together with phosphoinositide binding, supports membrane/cortical association. This is a peripheral scaffold, not an integral membrane receptor. Supporting Evidence: 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:0016476 regulation of embryonic cell shape | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: WDPCP-dependent cilia and polarity support embryonic development. Reason: Developmental defects are consistent with its cellular role but do not define an additional tissue-specific molecular activity. Supporting Evidence: PMID:24302887 decreased membrane ruffling, failure to establish cell polarity, and loss of directional cell migration. 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:0021915 neural tube development | NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ... | KEEP AS NON CORE | Summary: WDPCP-dependent cilia and polarity support embryonic development. Reason: Developmental defects are consistent with its cellular role but do not define an additional tissue-specific molecular activity. Supporting Evidence: PMID:24302887 decreased membrane ruffling, failure to establish cell polarity, and loss of directional cell migration. 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:0032185 septin cytoskeleton organization | ISS GO_REF:0000024 | ACCEPT | Summary: WDPCP recruits and organizes cytoskeletal/ciliary proteins. Reason: Sept2 loss from actin structures and ciliary transition-zone recruitment defects provide direct evidence for protein localization and septin organization. Supporting Evidence: PMID:24302887 in Wdpcp-deficient cells, Sept2 was lost from the actin cytoskeleton, suggesting Wdpcp is required for Sept2 recruitment to actin filaments. PMID:24302887 Wdpcp is localized to the transition zone |
| GO:0032880 regulation of protein localization | ISS GO_REF:0000024 | ACCEPT | Summary: WDPCP recruits and organizes cytoskeletal/ciliary proteins. Reason: Sept2 loss from actin structures and ciliary transition-zone recruitment defects provide direct evidence for protein localization and septin organization. Supporting Evidence: PMID:24302887 in Wdpcp-deficient cells, Sept2 was lost from the actin cytoskeleton, suggesting Wdpcp is required for Sept2 recruitment to actin filaments. PMID:24302887 Wdpcp is localized to the transition zone |
| GO:0035091 phosphatidylinositol binding | IEA GO_REF:0000107 | ACCEPT | Summary: WDPCP directly binds phosphoinositides through its C-terminal tail. Reason: The recombinant structural/biochemical study tests CPLANE subunits individually and identifies the WDPCP C-terminal lipid-binding segment. The assignment is not inferred merely from complex membership. Supporting Evidence: PMID:35427153 Wdpcp engages PIPs via the last 60 C-terminal residues. |
| GO:0035091 phosphatidylinositol binding | ISS GO_REF:0000024 | ACCEPT | Summary: WDPCP directly binds phosphoinositides through its C-terminal tail. Reason: The recombinant structural/biochemical study tests CPLANE subunits individually and identifies the WDPCP C-terminal lipid-binding segment. The assignment is not inferred merely from complex membership. Supporting Evidence: PMID:35427153 Wdpcp engages PIPs via the last 60 C-terminal residues. |
| GO:0042073 intraciliary transport | NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ... | ACCEPT | Summary: WDPCP organizes ciliary assembly and trafficking machinery. Reason: CPLANE experiments and the Wdpcp mutant establish recruitment of proteins required for ciliogenesis and IFT organization. WDPCP is a scaffold for this machinery, not the processive motor. Supporting Evidence: PMID:24302887 Wdpcp is localized to the 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:0042733 embryonic digit morphogenesis | IMP PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ... | KEEP AS NON CORE | Summary: WDPCP-associated ciliopathy affects digit, tongue and palate morphogenesis. Reason: The full study reports compound WDPCP variants in a patient with polydactyly, tongue hamartoma and high arched palate, and tests variant protein stability. These are valid developmental manifestations of the ciliary/polarity role, rather than independent core functions. 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: WDPCP-associated ciliopathy affects digit, tongue and palate morphogenesis. Reason: The full study reports compound WDPCP variants in a patient with polydactyly, tongue hamartoma and high arched palate, and tests variant protein stability. These are valid developmental manifestations of the ciliary/polarity role, rather than independent core functions. 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: WDPCP organizes ciliary assembly and trafficking machinery. Reason: CPLANE experiments and the Wdpcp mutant establish recruitment of proteins required for ciliogenesis and IFT organization. WDPCP is a scaffold for this machinery, not the processive motor. Supporting Evidence: PMID:24302887 Wdpcp is localized to the 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:0045184 establishment of protein localization | IBA GO_REF:0000033 | ACCEPT | Summary: WDPCP recruits and organizes cytoskeletal/ciliary proteins. Reason: Sept2 loss from actin structures and ciliary transition-zone recruitment defects provide direct evidence for protein localization and septin organization. Supporting Evidence: PMID:24302887 in Wdpcp-deficient cells, Sept2 was lost from the actin cytoskeleton, suggesting Wdpcp is required for Sept2 recruitment to actin filaments. PMID:24302887 Wdpcp is localized to the transition zone |
| GO:0060021 roof of mouth development | IMP PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ... | KEEP AS NON CORE | Summary: WDPCP-associated ciliopathy affects digit, tongue and palate morphogenesis. Reason: The full study reports compound WDPCP variants in a patient with polydactyly, tongue hamartoma and high arched palate, and tests variant protein stability. These are valid developmental manifestations of the ciliary/polarity role, rather than independent core functions. 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 organizes ciliary assembly and trafficking machinery. Reason: CPLANE experiments and the Wdpcp mutant establish recruitment of proteins required for ciliogenesis and IFT organization. WDPCP is a scaffold for this machinery, not the processive motor. Supporting Evidence: PMID:24302887 Wdpcp is localized to the 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:0097541 axonemal basal plate | IBA GO_REF:0000033 | ACCEPT | Summary: WDPCP acts at the base of cilia. Reason: Transition-zone localization and recruitment functions support the ciliary-base annotations. The broad cilium term includes this specialized basal pool. Supporting Evidence: PMID:24302887 Wdpcp is localized to the 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:0097541 axonemal basal plate | IEA GO_REF:0000107 | ACCEPT | Summary: WDPCP acts at the base of cilia. Reason: Transition-zone localization and recruitment functions support the ciliary-base annotations. The broad cilium term includes this specialized basal pool. Supporting Evidence: PMID:24302887 Wdpcp is localized to the 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:1902017 regulation of cilium assembly | NAS PMID:27158779 The ciliopathy-associated CPLANE proteins direct basal body ... | ACCEPT | Summary: WDPCP organizes ciliary assembly and trafficking machinery. Reason: CPLANE experiments and the Wdpcp mutant establish recruitment of proteins required for ciliogenesis and IFT organization. WDPCP is a scaffold for this machinery, not the processive motor. Supporting Evidence: PMID:24302887 Wdpcp is localized to the 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. |
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