{"gene":"CSPP1","run_date":"2026-06-09T22:57:19","timeline":{"discoveries":[{"year":2006,"finding":"CSPP and CSPP-L, two splice isoforms encoded by CSPP1, associate with centrosomes and spindle pole microtubules. The coiled-coil mid-domain insertion unique to CSPP-L is required for its differential effects on microtubule organization in mitosis (lagging chromosomes/monopolar spindles vs. multipolar spindles with CSPP). The common C-terminal domain can associate with centrosomes in a microtubule-independent manner and represses microtubule-organization activity until mitosis.","method":"Ectopic expression, domain deletion/mutagenesis, fluorescence microscopy, cell cycle analysis","journal":"Journal of cellular physiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple domain-mapping experiments and cell biological readouts in a single lab, two orthogonal approaches (localization + functional assay)","pmids":["16826565"],"is_preprint":false},{"year":2010,"finding":"CSPP isoforms localize to the ciliary axoneme in post-mitotic resting cells and are required for ciliogenesis in hTERT-RPE1 cells. CSPP isoforms interact via their common C-terminal domain with Nephrocystin 8 (NPHP8/RPGRIP1L) and form a ternary complex with NPHP8 and NPHP4. CSPP-L is required for efficient localization of NPHP8 (but not NPHP4) to the basal body, though the ciliogenesis defect is not mediated through loss of NPHP8.","method":"Endogenous protein localization (immunofluorescence), co-immunoprecipitation, siRNA knockdown, domain-mapping pulldown, in vivo tissue immunostaining","journal":"Molecular biology of the cell","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal co-IP, domain-mapping, siRNA loss-of-function with defined ciliogenesis phenotype, in vivo corroboration; multiple orthogonal methods in one focused study","pmids":["20519441"],"is_preprint":false},{"year":2013,"finding":"Biallelic truncating mutations in CSPP1 cause Joubert syndrome. Patient fibroblasts show reduced numbers and/or shortened primary cilia, reduced axonemal localization of ARL13B and adenylyl cyclase III. Morpholino knockdown of cspp1 in zebrafish reduced ciliary localization of Arl13b and produced curved body, pronephric cysts, and cerebellar abnormalities consistent with JBTS.","method":"Patient fibroblast analysis (immunofluorescence for ciliary markers), zebrafish morpholino knockdown","journal":"American journal of human genetics","confidence":"High","confidence_rationale":"Tier 2 / Strong — loss-of-function in human fibroblasts and zebrafish model, replicated across independent labs in same issue","pmids":["24360808"],"is_preprint":false},{"year":2013,"finding":"CSPP1 mutations cause ciliopathy phenotypes ranging from Joubert syndrome to Meckel-Gruber syndrome. Mutant patient fibroblasts display severely impaired ciliogenesis with concomitant defects in sonic hedgehog (SHH) signaling, placing CSPP1 upstream of or at the level of SHH pathway transduction in cilia.","method":"Patient fibroblast ciliogenesis assay, SHH signaling reporter assay","journal":"American journal of human genetics","confidence":"High","confidence_rationale":"Tier 2 / Strong — loss-of-function in patient fibroblasts with two orthogonal readouts (ciliogenesis + SHH signaling), independent lab replication","pmids":["24360803"],"is_preprint":false},{"year":2013,"finding":"CSPP1 protein localizes to the primary cilium in an in vitro model of human neurogenesis, in addition to centrosomes and spindle poles. CSPP1-mutant fibroblasts from affected individuals show abrogated protein levels and defective ciliogenesis, supporting a neural-specific ciliary function. No CSPP1 mutations were found in a nephronophthisis cohort, indicating tissue-specific ciliary roles.","method":"Immunofluorescence localization in human neurogenesis model, patient fibroblast analysis, cohort mutation screening","journal":"American journal of human genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization with functional consequence (ciliogenesis defect), single lab, multiple methods","pmids":["24360807"],"is_preprint":false},{"year":2015,"finding":"CSPP1 localizes to kinetochores during mitosis and directly binds CENP-H both in vitro and in vivo. CSPP1 depletion perturbs mitotic progression, compromises spindle assembly checkpoint satisfaction, attenuates chromosome oscillation, and enhances kinetochore movement velocity; CSPP1 overexpression decreases kinetochore movement speed, indicating CSPP1 promotes kinetochore microtubule (kMT) stability. Disruption of CENP-H/CSPP1 interaction with a membrane-permeable competing peptide causes mitotic arrest and chromosome segregation defects.","method":"Co-immunoprecipitation, in vitro pulldown/binding assay, siRNA depletion, live-cell imaging of kinetochore movements, competing peptide perturbation","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP, in vitro binding, live-cell functional readout, competing peptide mechanistic dissection, multiple orthogonal methods","pmids":["26378239"],"is_preprint":false},{"year":2015,"finding":"CSPP-L localizes to desmosomes in apical-basal polarized epithelial cells in a microtubule-independent but Desmoplakin-dependent manner. siRNA depletion of CSPP-L or Desmoplakin promotes multi-lumen spheroid formation in 3D cultures of non-ciliated Caco-2 cells. CSPP-L-depleted multi-lumen spheroids show disrupted apical localization of the cytoskeleton-organizing RhoGEF ECT2, revealing a non-ciliary role in epithelial morphogenesis.","method":"siRNA knockdown, immunofluorescence, 3D spheroid culture, subcellular fractionation/localization","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization with mechanistic perturbation (Desmoplakin dependency), defined phenotypic readout in 3D culture, single lab","pmids":["26241740"],"is_preprint":false},{"year":2019,"finding":"CSPP1 interacts with the Joubert syndrome ciliary tip protein CEP104 at microtubules to regulate axoneme length. Both CSPP1 and CEP104 are required for ciliary translocation of Smoothened in response to Hedgehog pathway stimulation in hTERT-RPE1 cells. CEP104 is not required for ciliary recruitment of CSPP1, indicating that an intra-ciliary CEP104-CSPP1 complex controls axoneme length and Hedgehog signaling competence.","method":"Co-immunoprecipitation, siRNA knockdown, immunofluorescence (Smoothened translocation assay), zebrafish cep104 morpholino knockdown","journal":"Cell reports","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal interaction, loss-of-function in human cells and zebrafish, multiple orthogonal functional readouts (axoneme length + Hh signaling)","pmids":["31412255"],"is_preprint":false},{"year":2023,"finding":"In vitro reconstitution showed that CSPP1 preferentially binds to polymerizing microtubule ends growing slowly or undergoing perturbations, stabilizing them similarly to taxane-class compounds. Cryo-electron tomography and fluorescence microscopy demonstrated that CSPP1 is deposited in the microtubule lumen. CSPP1 inhibits microtubule growth and shortening through two separate domains and specifically recognizes and stabilizes damaged microtubule lattices.","method":"In vitro microtubule reconstitution assay, fluorescence microscopy, cryo-electron tomography, domain-deletion analysis","journal":"The Journal of cell biology","confidence":"High","confidence_rationale":"Tier 1 / Strong — in vitro reconstitution combined with cryo-ET structural analysis and domain mutagenesis, multiple orthogonal methods in one study","pmids":["36752787"],"is_preprint":false},{"year":2024,"finding":"CSPP1 caps and stabilizes both plus and minus ends of static microtubules in live cells. Real-time imaging of laser-ablated microtubules showed deposition of CSPP1 at newly generated ends with concomitant suppression of dynamic instability. CSPP1 suppresses intrinsic microtubule catastrophe and restricts polymerization at free ends. CSPP1-bound microtubules are resistant to MCAK (mitotic centromere-associated kinesin)-mediated depolymerization.","method":"Live-cell imaging, laser ablation of microtubules, CSPP1 overexpression/depletion, functional depolymerization resistance assay","journal":"Journal of molecular cell biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — live-cell real-time imaging with laser ablation, gain- and loss-of-function, MCAK resistance assay; multiple orthogonal methods in one study","pmids":["38389254"],"is_preprint":false}],"current_model":"CSPP1 encodes two major isoforms (CSPP and CSPP-L) that associate with centrosomes, spindle microtubules, kinetochores, and the ciliary axoneme: at microtubules, CSPP1 stabilizes both plus and minus ends by capping them from the lumen, suppressing catastrophe and resisting MCAK-mediated depolymerization via two separate domains; at kinetochores it binds CENP-H to regulate kMT dynamics and chromosome oscillation; in post-mitotic cells it extends into the ciliary axoneme where, in complex with CEP104, it controls axoneme length and Hedgehog signaling competence; it also interacts with NPHP8/RPGRIP1L and NPHP4 via its C-terminal domain to support basal body organization and ciliogenesis; and in polarized epithelial cells CSPP-L localizes to desmosomes in a Desmoplakin-dependent manner to maintain epithelial architecture, with loss-of-function mutations in humans causing Joubert syndrome through defective primary cilia formation and impaired SHH signaling."},"narrative":{"mechanistic_narrative":"CSPP1 encodes centrosome and spindle pole–associated isoforms (CSPP and CSPP-L) that function as microtubule-stabilizing factors deployed across mitotic and post-mitotic contexts [PMID:16826565, PMID:36752787]. Mechanistically, CSPP1 is deposited within the microtubule lumen, where it preferentially recognizes slowly polymerizing or damaged lattices and caps both plus and minus ends, suppressing intrinsic catastrophe and restricting end dynamics through two separable domains; CSPP1-bound microtubules become resistant to MCAK-mediated depolymerization [PMID:36752787, PMID:38389254]. During mitosis CSPP1 localizes to kinetochores and directly binds CENP-H, promoting kinetochore-microtubule stability, damping chromosome oscillation, and supporting spindle assembly checkpoint satisfaction [PMID:26378239]. In post-mitotic cells CSPP1 extends into the ciliary axoneme and is required for ciliogenesis, acting through a C-terminal interaction with NPHP8/RPGRIP1L and a ternary complex with NPHP4 at the basal body, and through an intra-ciliary complex with CEP104 that sets axoneme length and licenses Hedgehog signaling competence via Smoothened translocation [PMID:20519441, PMID:31412255]. Biallelic truncating mutations in CSPP1 cause Joubert syndrome and related ciliopathies, with patient cells showing reduced and shortened cilia, loss of axonemal ARL13B and adenylyl cyclase III, and impaired SHH signaling [PMID:24360808, PMID:24360803]. CSPP-L additionally has a non-ciliary role, localizing to desmosomes in a Desmoplakin-dependent manner to maintain polarized epithelial architecture [PMID:26241740].","teleology":[{"year":2006,"claim":"Established that CSPP1 produces two isoforms targeting centrosomes and spindle poles, with distinct domains controlling microtubule organization and a C-terminal domain mediating centrosome association independent of microtubules.","evidence":"Ectopic expression, domain deletion/mutagenesis, and fluorescence microscopy with cell cycle analysis","pmids":["16826565"],"confidence":"Medium","gaps":["Did not define the biochemical basis of microtubule binding","Endogenous localization and physiological partners not established"]},{"year":2010,"claim":"Showed CSPP1 has a ciliary function, localizing to the axoneme and required for ciliogenesis, and physically linking to the NPHP module via its C-terminal domain.","evidence":"Endogenous immunofluorescence, reciprocal co-IP, domain-mapping pulldowns, and siRNA loss-of-function in hTERT-RPE1 cells","pmids":["20519441"],"confidence":"High","gaps":["Ciliogenesis defect was not attributable to NPHP8 loss, leaving the effector mechanism undefined","Did not establish how CSPP1 is recruited to the axoneme"]},{"year":2013,"claim":"Demonstrated that CSPP1 loss-of-function causes human ciliopathy, connecting its ciliary role to disease and to SHH signaling competence.","evidence":"Biallelic truncating mutations identified in Joubert/Meckel-Gruber patients, patient fibroblast ciliary marker and SHH reporter assays, zebrafish morpholino knockdown","pmids":["24360808","24360803","24360807"],"confidence":"High","gaps":["Molecular step at which CSPP1 acts in SHH transduction not pinpointed","Tissue-specificity of phenotypes (e.g. absence in nephronophthisis cohort) unexplained"]},{"year":2015,"claim":"Defined a mitotic kinetochore function, showing CSPP1 directly binds CENP-H to stabilize kinetochore microtubules and regulate chromosome dynamics.","evidence":"Reciprocal co-IP, in vitro binding, siRNA depletion, live-cell kinetochore tracking, and competing-peptide perturbation","pmids":["26378239"],"confidence":"High","gaps":["Structural basis of CENP-H/CSPP1 binding not resolved","Relationship between mitotic and ciliary pools of CSPP1 unclear"]},{"year":2015,"claim":"Revealed a non-ciliary role in epithelial morphogenesis, with CSPP-L localizing to desmosomes to maintain single-lumen architecture.","evidence":"siRNA knockdown, immunofluorescence, and 3D spheroid culture in non-ciliated Caco-2 cells showing Desmoplakin dependence","pmids":["26241740"],"confidence":"Medium","gaps":["Direct CSPP-L/Desmoplakin interaction not biochemically validated","Mechanism linking desmosomal CSPP-L to ECT2 apical localization unresolved"]},{"year":2019,"claim":"Identified the CEP104-CSPP1 ciliary-tip complex as the module controlling axoneme length and Hedgehog signaling competence.","evidence":"Co-IP, siRNA knockdown, Smoothened translocation assay in hTERT-RPE1 cells, and zebrafish cep104 morpholino knockdown","pmids":["31412255"],"confidence":"High","gaps":["How the complex couples length control to Smoothened trafficking not defined","CSPP1 recruitment mechanism (CEP104-independent) not identified"]},{"year":2023,"claim":"Provided the biochemical and structural mechanism, showing CSPP1 acts from within the microtubule lumen to recognize and stabilize damaged lattices and growing ends through two separate domains.","evidence":"In vitro microtubule reconstitution, fluorescence microscopy, cryo-electron tomography, and domain-deletion analysis","pmids":["36752787"],"confidence":"High","gaps":["Atomic-resolution binding mode within the lumen not resolved","How luminal deposition occurs in cells not established"]},{"year":2024,"claim":"Extended the stabilization mechanism in cells, showing CSPP1 caps both microtubule ends, suppresses catastrophe, and confers resistance to MCAK depolymerization.","evidence":"Live-cell imaging with laser ablation, gain- and loss-of-function, and a MCAK depolymerization-resistance assay","pmids":["38389254"],"confidence":"High","gaps":["Regulation of CSPP1 end-capping across the cell cycle not defined","Interplay with other end-binding/depolymerizing factors not mapped"]},{"year":null,"claim":"How CSPP1's intrinsic microtubule-stabilizing activity is selectively targeted and regulated across its mitotic (kinetochore), ciliary (axoneme), and epithelial (desmosome) contexts remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No unifying mechanism linking luminal microtubule stabilization to context-specific recruitment","Isoform-specific functional partitioning (CSPP vs CSPP-L) not fully mapped"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[8,9,0]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[9,8]}],"localization":[{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[0]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[8,9]},{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[1,4,7]},{"term_id":"GO:0005694","term_label":"chromosome","supporting_discovery_ids":[5]}],"pathway":[{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[5]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[3,7]},{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[1,7]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[2,3]}],"complexes":["CEP104-CSPP1 ciliary tip complex","CSPP1-NPHP8-NPHP4 ternary complex"],"partners":["CEP104","RPGRIP1L","NPHP4","CENP-H","DSP"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q1MSJ5","full_name":"Centrosome and spindle pole-associated protein 1","aliases":[],"length_aa":1256,"mass_kda":145.5,"function":"May play a role in cell-cycle-dependent microtubule organization","subcellular_location":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Cytoplasm, cytoskeleton, spindle; Cytoplasm, cytoskeleton, spindle pole; Cell projection, cilium","url":"https://www.uniprot.org/uniprotkb/Q1MSJ5/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CSPP1","classification":"Not Classified","n_dependent_lines":4,"n_total_lines":1208,"dependency_fraction":0.0033112582781456954},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"MIF","stoichiometry":0.2},{"gene":"VPS35","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/CSPP1","total_profiled":1310},"omim":[{"mim_id":"615636","title":"JOUBERT SYNDROME 21; JBTS21","url":"https://www.omim.org/entry/615636"},{"mim_id":"611654","title":"CENTROSOME SPINDLE POLE-ASSOCIATED PROTEIN 1; CSPP1","url":"https://www.omim.org/entry/611654"},{"mim_id":"611395","title":"FAMILY WITH SEQUENCE SIMILARITY 110, MEMBER C; FAM110C","url":"https://www.omim.org/entry/611395"},{"mim_id":"611394","title":"FAMILY WITH SEQUENCE SIMILARITY 110, MEMBER B; FAM110B","url":"https://www.omim.org/entry/611394"},{"mim_id":"611393","title":"FAMILY WITH SEQUENCE SIMILARITY 110, MEMBER A; FAM110A","url":"https://www.omim.org/entry/611393"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Centriolar satellite","reliability":"Approved"},{"location":"Centrosome","reliability":"Approved"},{"location":"Basal body","reliability":"Approved"},{"location":"Vesicles","reliability":"Additional"},{"location":"Primary cilium","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in many","driving_tissues":[],"url":"https://www.proteinatlas.org/search/CSPP1"},"hgnc":{"alias_symbol":["FLJ22490","CSPP","JBTS21","CSPP-L"],"prev_symbol":[]},"alphafold":{"accession":"Q1MSJ5","domains":[{"cath_id":"1.20.5","chopping":"1021-1062","consensus_level":"medium","plddt":83.6671,"start":1021,"end":1062}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q1MSJ5","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q1MSJ5-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q1MSJ5-F1-predicted_aligned_error_v6.png","plddt_mean":55.94},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CSPP1","jax_strain_url":"https://www.jax.org/strain/search?query=CSPP1"},"sequence":{"accession":"Q1MSJ5","fasta_url":"https://rest.uniprot.org/uniprotkb/Q1MSJ5.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q1MSJ5/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q1MSJ5"}},"corpus_meta":[{"pmid":"24360808","id":"PMC_24360808","title":"Mutations 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The coiled-coil mid-domain insertion unique to CSPP-L is required for its differential effects on microtubule organization in mitosis (lagging chromosomes/monopolar spindles vs. multipolar spindles with CSPP). The common C-terminal domain can associate with centrosomes in a microtubule-independent manner and represses microtubule-organization activity until mitosis.\",\n      \"method\": \"Ectopic expression, domain deletion/mutagenesis, fluorescence microscopy, cell cycle analysis\",\n      \"journal\": \"Journal of cellular physiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple domain-mapping experiments and cell biological readouts in a single lab, two orthogonal approaches (localization + functional assay)\",\n      \"pmids\": [\"16826565\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"CSPP isoforms localize to the ciliary axoneme in post-mitotic resting cells and are required for ciliogenesis in hTERT-RPE1 cells. CSPP isoforms interact via their common C-terminal domain with Nephrocystin 8 (NPHP8/RPGRIP1L) and form a ternary complex with NPHP8 and NPHP4. CSPP-L is required for efficient localization of NPHP8 (but not NPHP4) to the basal body, though the ciliogenesis defect is not mediated through loss of NPHP8.\",\n      \"method\": \"Endogenous protein localization (immunofluorescence), co-immunoprecipitation, siRNA knockdown, domain-mapping pulldown, in vivo tissue immunostaining\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal co-IP, domain-mapping, siRNA loss-of-function with defined ciliogenesis phenotype, in vivo corroboration; multiple orthogonal methods in one focused study\",\n      \"pmids\": [\"20519441\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"Biallelic truncating mutations in CSPP1 cause Joubert syndrome. Patient fibroblasts show reduced numbers and/or shortened primary cilia, reduced axonemal localization of ARL13B and adenylyl cyclase III. Morpholino knockdown of cspp1 in zebrafish reduced ciliary localization of Arl13b and produced curved body, pronephric cysts, and cerebellar abnormalities consistent with JBTS.\",\n      \"method\": \"Patient fibroblast analysis (immunofluorescence for ciliary markers), zebrafish morpholino knockdown\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — loss-of-function in human fibroblasts and zebrafish model, replicated across independent labs in same issue\",\n      \"pmids\": [\"24360808\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"CSPP1 mutations cause ciliopathy phenotypes ranging from Joubert syndrome to Meckel-Gruber syndrome. Mutant patient fibroblasts display severely impaired ciliogenesis with concomitant defects in sonic hedgehog (SHH) signaling, placing CSPP1 upstream of or at the level of SHH pathway transduction in cilia.\",\n      \"method\": \"Patient fibroblast ciliogenesis assay, SHH signaling reporter assay\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — loss-of-function in patient fibroblasts with two orthogonal readouts (ciliogenesis + SHH signaling), independent lab replication\",\n      \"pmids\": [\"24360803\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"CSPP1 protein localizes to the primary cilium in an in vitro model of human neurogenesis, in addition to centrosomes and spindle poles. CSPP1-mutant fibroblasts from affected individuals show abrogated protein levels and defective ciliogenesis, supporting a neural-specific ciliary function. No CSPP1 mutations were found in a nephronophthisis cohort, indicating tissue-specific ciliary roles.\",\n      \"method\": \"Immunofluorescence localization in human neurogenesis model, patient fibroblast analysis, cohort mutation screening\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization with functional consequence (ciliogenesis defect), single lab, multiple methods\",\n      \"pmids\": [\"24360807\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"CSPP1 localizes to kinetochores during mitosis and directly binds CENP-H both in vitro and in vivo. CSPP1 depletion perturbs mitotic progression, compromises spindle assembly checkpoint satisfaction, attenuates chromosome oscillation, and enhances kinetochore movement velocity; CSPP1 overexpression decreases kinetochore movement speed, indicating CSPP1 promotes kinetochore microtubule (kMT) stability. Disruption of CENP-H/CSPP1 interaction with a membrane-permeable competing peptide causes mitotic arrest and chromosome segregation defects.\",\n      \"method\": \"Co-immunoprecipitation, in vitro pulldown/binding assay, siRNA depletion, live-cell imaging of kinetochore movements, competing peptide perturbation\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP, in vitro binding, live-cell functional readout, competing peptide mechanistic dissection, multiple orthogonal methods\",\n      \"pmids\": [\"26378239\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"CSPP-L localizes to desmosomes in apical-basal polarized epithelial cells in a microtubule-independent but Desmoplakin-dependent manner. siRNA depletion of CSPP-L or Desmoplakin promotes multi-lumen spheroid formation in 3D cultures of non-ciliated Caco-2 cells. CSPP-L-depleted multi-lumen spheroids show disrupted apical localization of the cytoskeleton-organizing RhoGEF ECT2, revealing a non-ciliary role in epithelial morphogenesis.\",\n      \"method\": \"siRNA knockdown, immunofluorescence, 3D spheroid culture, subcellular fractionation/localization\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization with mechanistic perturbation (Desmoplakin dependency), defined phenotypic readout in 3D culture, single lab\",\n      \"pmids\": [\"26241740\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"CSPP1 interacts with the Joubert syndrome ciliary tip protein CEP104 at microtubules to regulate axoneme length. Both CSPP1 and CEP104 are required for ciliary translocation of Smoothened in response to Hedgehog pathway stimulation in hTERT-RPE1 cells. CEP104 is not required for ciliary recruitment of CSPP1, indicating that an intra-ciliary CEP104-CSPP1 complex controls axoneme length and Hedgehog signaling competence.\",\n      \"method\": \"Co-immunoprecipitation, siRNA knockdown, immunofluorescence (Smoothened translocation assay), zebrafish cep104 morpholino knockdown\",\n      \"journal\": \"Cell reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal interaction, loss-of-function in human cells and zebrafish, multiple orthogonal functional readouts (axoneme length + Hh signaling)\",\n      \"pmids\": [\"31412255\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"In vitro reconstitution showed that CSPP1 preferentially binds to polymerizing microtubule ends growing slowly or undergoing perturbations, stabilizing them similarly to taxane-class compounds. Cryo-electron tomography and fluorescence microscopy demonstrated that CSPP1 is deposited in the microtubule lumen. CSPP1 inhibits microtubule growth and shortening through two separate domains and specifically recognizes and stabilizes damaged microtubule lattices.\",\n      \"method\": \"In vitro microtubule reconstitution assay, fluorescence microscopy, cryo-electron tomography, domain-deletion analysis\",\n      \"journal\": \"The Journal of cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro reconstitution combined with cryo-ET structural analysis and domain mutagenesis, multiple orthogonal methods in one study\",\n      \"pmids\": [\"36752787\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"CSPP1 caps and stabilizes both plus and minus ends of static microtubules in live cells. Real-time imaging of laser-ablated microtubules showed deposition of CSPP1 at newly generated ends with concomitant suppression of dynamic instability. CSPP1 suppresses intrinsic microtubule catastrophe and restricts polymerization at free ends. CSPP1-bound microtubules are resistant to MCAK (mitotic centromere-associated kinesin)-mediated depolymerization.\",\n      \"method\": \"Live-cell imaging, laser ablation of microtubules, CSPP1 overexpression/depletion, functional depolymerization resistance assay\",\n      \"journal\": \"Journal of molecular cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — live-cell real-time imaging with laser ablation, gain- and loss-of-function, MCAK resistance assay; multiple orthogonal methods in one study\",\n      \"pmids\": [\"38389254\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CSPP1 encodes two major isoforms (CSPP and CSPP-L) that associate with centrosomes, spindle microtubules, kinetochores, and the ciliary axoneme: at microtubules, CSPP1 stabilizes both plus and minus ends by capping them from the lumen, suppressing catastrophe and resisting MCAK-mediated depolymerization via two separate domains; at kinetochores it binds CENP-H to regulate kMT dynamics and chromosome oscillation; in post-mitotic cells it extends into the ciliary axoneme where, in complex with CEP104, it controls axoneme length and Hedgehog signaling competence; it also interacts with NPHP8/RPGRIP1L and NPHP4 via its C-terminal domain to support basal body organization and ciliogenesis; and in polarized epithelial cells CSPP-L localizes to desmosomes in a Desmoplakin-dependent manner to maintain epithelial architecture, with loss-of-function mutations in humans causing Joubert syndrome through defective primary cilia formation and impaired SHH signaling.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"CSPP1 encodes centrosome and spindle pole–associated isoforms (CSPP and CSPP-L) that function as microtubule-stabilizing factors deployed across mitotic and post-mitotic contexts [#0, #8]. Mechanistically, CSPP1 is deposited within the microtubule lumen, where it preferentially recognizes slowly polymerizing or damaged lattices and caps both plus and minus ends, suppressing intrinsic catastrophe and restricting end dynamics through two separable domains; CSPP1-bound microtubules become resistant to MCAK-mediated depolymerization [#8, #9]. During mitosis CSPP1 localizes to kinetochores and directly binds CENP-H, promoting kinetochore-microtubule stability, damping chromosome oscillation, and supporting spindle assembly checkpoint satisfaction [#5]. In post-mitotic cells CSPP1 extends into the ciliary axoneme and is required for ciliogenesis, acting through a C-terminal interaction with NPHP8/RPGRIP1L and a ternary complex with NPHP4 at the basal body, and through an intra-ciliary complex with CEP104 that sets axoneme length and licenses Hedgehog signaling competence via Smoothened translocation [#1, #7]. Biallelic truncating mutations in CSPP1 cause Joubert syndrome and related ciliopathies, with patient cells showing reduced and shortened cilia, loss of axonemal ARL13B and adenylyl cyclase III, and impaired SHH signaling [#2, #3]. CSPP-L additionally has a non-ciliary role, localizing to desmosomes in a Desmoplakin-dependent manner to maintain polarized epithelial architecture [#6].\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"Established that CSPP1 produces two isoforms targeting centrosomes and spindle poles, with distinct domains controlling microtubule organization and a C-terminal domain mediating centrosome association independent of microtubules.\",\n      \"evidence\": \"Ectopic expression, domain deletion/mutagenesis, and fluorescence microscopy with cell cycle analysis\",\n      \"pmids\": [\"16826565\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Did not define the biochemical basis of microtubule binding\", \"Endogenous localization and physiological partners not established\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Showed CSPP1 has a ciliary function, localizing to the axoneme and required for ciliogenesis, and physically linking to the NPHP module via its C-terminal domain.\",\n      \"evidence\": \"Endogenous immunofluorescence, reciprocal co-IP, domain-mapping pulldowns, and siRNA loss-of-function in hTERT-RPE1 cells\",\n      \"pmids\": [\"20519441\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Ciliogenesis defect was not attributable to NPHP8 loss, leaving the effector mechanism undefined\", \"Did not establish how CSPP1 is recruited to the axoneme\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Demonstrated that CSPP1 loss-of-function causes human ciliopathy, connecting its ciliary role to disease and to SHH signaling competence.\",\n      \"evidence\": \"Biallelic truncating mutations identified in Joubert/Meckel-Gruber patients, patient fibroblast ciliary marker and SHH reporter assays, zebrafish morpholino knockdown\",\n      \"pmids\": [\"24360808\", \"24360803\", \"24360807\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular step at which CSPP1 acts in SHH transduction not pinpointed\", \"Tissue-specificity of phenotypes (e.g. absence in nephronophthisis cohort) unexplained\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Defined a mitotic kinetochore function, showing CSPP1 directly binds CENP-H to stabilize kinetochore microtubules and regulate chromosome dynamics.\",\n      \"evidence\": \"Reciprocal co-IP, in vitro binding, siRNA depletion, live-cell kinetochore tracking, and competing-peptide perturbation\",\n      \"pmids\": [\"26378239\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of CENP-H/CSPP1 binding not resolved\", \"Relationship between mitotic and ciliary pools of CSPP1 unclear\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Revealed a non-ciliary role in epithelial morphogenesis, with CSPP-L localizing to desmosomes to maintain single-lumen architecture.\",\n      \"evidence\": \"siRNA knockdown, immunofluorescence, and 3D spheroid culture in non-ciliated Caco-2 cells showing Desmoplakin dependence\",\n      \"pmids\": [\"26241740\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct CSPP-L/Desmoplakin interaction not biochemically validated\", \"Mechanism linking desmosomal CSPP-L to ECT2 apical localization unresolved\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Identified the CEP104-CSPP1 ciliary-tip complex as the module controlling axoneme length and Hedgehog signaling competence.\",\n      \"evidence\": \"Co-IP, siRNA knockdown, Smoothened translocation assay in hTERT-RPE1 cells, and zebrafish cep104 morpholino knockdown\",\n      \"pmids\": [\"31412255\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How the complex couples length control to Smoothened trafficking not defined\", \"CSPP1 recruitment mechanism (CEP104-independent) not identified\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Provided the biochemical and structural mechanism, showing CSPP1 acts from within the microtubule lumen to recognize and stabilize damaged lattices and growing ends through two separate domains.\",\n      \"evidence\": \"In vitro microtubule reconstitution, fluorescence microscopy, cryo-electron tomography, and domain-deletion analysis\",\n      \"pmids\": [\"36752787\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Atomic-resolution binding mode within the lumen not resolved\", \"How luminal deposition occurs in cells not established\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Extended the stabilization mechanism in cells, showing CSPP1 caps both microtubule ends, suppresses catastrophe, and confers resistance to MCAK depolymerization.\",\n      \"evidence\": \"Live-cell imaging with laser ablation, gain- and loss-of-function, and a MCAK depolymerization-resistance assay\",\n      \"pmids\": [\"38389254\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Regulation of CSPP1 end-capping across the cell cycle not defined\", \"Interplay with other end-binding/depolymerizing factors not mapped\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How CSPP1's intrinsic microtubule-stabilizing activity is selectively targeted and regulated across its mitotic (kinetochore), ciliary (axoneme), and epithelial (desmosome) contexts remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No unifying mechanism linking luminal microtubule stabilization to context-specific recruitment\", \"Isoform-specific functional partitioning (CSPP vs CSPP-L) not fully mapped\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [8, 9, 0]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [9, 8]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [8, 9]},\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [1, 4, 7]},\n      {\"term_id\": \"GO:0005694\", \"supporting_discovery_ids\": [5]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [5]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [3, 7]},\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [1, 7]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"complexes\": [\"CEP104-CSPP1 ciliary tip complex\", \"CSPP1-NPHP8-NPHP4 ternary complex\"],\n    \"partners\": [\"CEP104\", \"RPGRIP1L\", \"NPHP4\", \"CENP-H\", \"DSP\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}