Affinage

CILK1

Serine/threonine-protein kinase ICK · UniProt Q9UPZ9

Length
632 aa
Mass
71.4 kDa
Annotated
2026-06-09
37 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CILK1 (ICK) is a conserved serine/threonine kinase of the MAP kinase-like family that localizes to the tip of cilia and governs intraflagellar transport (IFT) train turnaround during ciliogenesis (PMID:24797473, PMID:25243405). It is delivered anterogradely to the ciliary tip through direct binding of its C-terminal non-catalytic region to the IFT-B complex, moving bidirectionally at IFT-particle velocities; loss of CILK1 impairs retrograde IFT and causes IFT-A, IFT-B, and BBSome components to accumulate at a bulged ciliary tip, with kinase activity, TDY-motif phosphorylation, and IFT-dependent transport all required for function (PMID:24797473, PMID:32732286). CILK1 directly phosphorylates KIF3A (at Thr672/Thr674), but ablating this single site is insufficient to reproduce CILK1-loss developmental defects, indicating additional substrates mediate ciliopathy phenotypes (PMID:24797473, PMID:32178256, PMID:32935890); it also phosphorylates Raptor at Thr908 to activate mTORC1, and its control of cilia length acts through the mTORC1 pathway (PMID:22356909, PMID:25243405). CILK1 activity is set by an upstream CCRK/CDK20 axis—scaffolded by BROMI/TBC1D32—that phosphorylates and activates the kinase, and is further potentiated by KATNIP, which binds the CILK1 C-terminal intrinsically disordered region to elevate CILK1 protein levels, TDY-motif phosphorylation, substrate phosphorylation, and cilia-length restriction (PMID:35609210, PMID:37665596, PMID:40621737). Through these activities CILK1 is essential for Hedgehog signaling, planar cell polarity, and skeletal and sensory development (PMID:27466187, PMID:28115485, PMID:39120290). Loss-of-function and C-terminal variants of CILK1 cause multiple human ciliopathies, including a skeletal/Hedgehog disorder, ECO syndrome, juvenile myoclonic epilepsy, and cranioectodermal dysplasia (PMID:27466187, PMID:27069622, PMID:32178256, PMID:40615527).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2000 Medium

    Established CILK1/ICK as a distinct serine/threonine kinase carrying a MAP-kinase-type dual-phosphorylation (TXY) activation motif, defining the molecular class of the enzyme before any cellular role was known.

    Evidence PCR cloning from intestinal crypt cDNA, Northern blot, in situ hybridization

    PMID:10699974

    Open questions at the time
    • No substrate or pathway identified
    • Ciliary role not yet recognized
    • Activation mechanism of the TXY/TDY motif unresolved
  2. 2012 High

    Identified the first direct substrate, showing CILK1 phosphorylates Raptor at Thr908 to enable mTORC1 activation, linking the kinase to nutrient/growth signaling.

    Evidence In vitro kinase assay, mass spectrometry, phospho-specific antibody, T908A mutagenesis rescue

    PMID:22356909

    Open questions at the time
    • Connection between mTORC1 regulation and cilia not yet drawn
    • Physiological context of Raptor phosphorylation in vivo unclear
  3. 2014 High

    Defined CILK1's core cellular role: it localizes to the ciliary tip, is required for IFT, and phosphorylates KIF3A, with loss causing accumulation of IFT-A, IFT-B, and BBSome at tips—and showed its ciliary effects involve the mTORC1 pathway.

    Evidence ICK-deficient mouse, immunolocalization, live imaging, in vitro KIF3A kinase assay; separate live IFT velocity imaging with rapamycin suppression

    PMID:24797473 PMID:25243405

    Open questions at the time
    • Mechanism of tip recruitment not yet defined
    • Whether KIF3A phosphorylation is the relevant in vivo substrate untested
    • How mTORC1 and IFT control intersect mechanistically unclear
  4. 2016 High

    Connected CILK1 kinase activity to human disease and developmental signaling, showing kinase-dead mutations alter ciliary localization, lengthen cilia, and disrupt Hedgehog signaling and skeletogenesis, and that distinct mutations cause ECO syndrome with ciliogenesis defects.

    Evidence Exome sequencing of patients, in vitro kinase assays of E80K, patient fibroblast localization; homozygosity mapping and WT/mutant mRFP-ICK localization for ECO syndrome

    PMID:27069622 PMID:27466187

    Open questions at the time
    • Hedgehog defect downstream effectors not identified
    • Relationship between localization shift and signaling loss not mechanistically resolved
  5. 2017 High

    Extended CILK1's IFT-regulatory role to sensory tissue and planar cell polarity, showing kinocilia of hair cells require Ick for correct IFT88 localization, stereocilia orientation, and hearing.

    Evidence Conditional Ick knockout mice, IFT88 immunofluorescence, ABR auditory tests, confocal stereocilia imaging

    PMID:28115485

    Open questions at the time
    • Molecular link between IFT regulation and PCP unestablished
    • Substrate mediating PCP effects unknown
  6. 2019 Medium

    Dissected the domain architecture, demonstrating the C-terminal non-catalytic domain is required for KIF3A substrate recognition, ciliary localization, and negative regulation of ciliogenesis—separating catalysis from targeting.

    Evidence CTD truncation mutants, in vitro KIF3A kinase assay, immunofluorescence, ciliation quantification

    PMID:31277411

    Open questions at the time
    • Binding partner mediating CTD-dependent localization not yet identified
    • Single-lab construct study
  7. 2020 High

    Resolved how CILK1 reaches and acts at the tip: its C-terminal region binds IFT-B for anterograde delivery, and its kinase activity is needed for retrograde IFT turnaround—while a KIF3A phospho-site knock-in showed that single substrate is not sufficient to explain developmental phenotypes, and JME mutations split into kinase-dead versus localization/length-control classes.

    Evidence Co-IP of CILK1 CTD with IFT-B, TIRF live imaging, KO rescue; Kif3a T674A knock-in mouse; in vitro KIF3A-Thr672 assays with JME mutants

    PMID:32178256 PMID:32732286 PMID:32935890

    Open questions at the time
    • Identity of the additional CILK1 substrates driving development unknown
    • Direct IFT-B subunit contacted not pinpointed
    • How CTD mutations alter axonemal distribution mechanistically unclear
  8. 2022 High

    Placed CILK1 within an upstream activation axis and identified additional partners, showing CCRK/CDK20 (scaffolded by BROMI/TBC1D32) phosphorylates and activates CILK1 to control tip IFT turnaround, and that KLC3 binds CILK1 at cilia bases to modulate IFT-B/EGFR recruitment in kidney; pharmacological inhibition (Alvocidib) confirmed CILK1-dependent cilia elongation.

    Evidence Reciprocal Co-IP and multiple KO cell lines (CCRK, BROMI, FAM149B1); yeast two-hybrid + Co-IP and conditional Cilk1 KO mice for KLC3; in vitro IC50 kinase inhibition assay

    PMID:35609210 PMID:35897693 PMID:35961787

    Open questions at the time
    • Direct CCRK phosphosite on CILK1 within this axis not mapped here
    • Whether KLC3 effects are kinase-dependent unclear
    • Off-target profile of Alvocidib not addressed
  9. 2023 High

    Identified KATNIP as a regulatory scaffold that potentiates CILK1, showing its binding to the CILK1 C-terminal IDR elevates CILK1 levels, TDY-motif and substrate phosphorylation, and restricts cilia length.

    Evidence Co-IP, reciprocal domain deletion of CILK1 IDR and KATNIP DUF domains, TDY/substrate phosphorylation assays, cilia length measurement

    PMID:37665596

    Open questions at the time
    • Whether KATNIP stabilizes CILK1 directly or via reduced turnover unclear
    • Relationship between KATNIP and CCRK activation pathways unresolved
  10. 2024 High

    Demonstrated functional cooperation and disease relevance: CCRK activates both Mak and Ick to co-regulate photoreceptor tip IFT with FGF receptors as negative regulators, and a JME-associated IDR variant (A615T) selectively impairs KATNIP-mediated CILK1 regulation, deregulating Hedgehog signaling.

    Evidence Conditional Mak/Ick double-KO mice with AAV-Ick rescue and FGFR inhibition; A612T knock-in MEF analysis with KATNIP co-expression and Hedgehog readouts

    PMID:39120290 PMID:39293864

    Open questions at the time
    • Mechanism of FGFR-mediated negative regulation unmapped
    • How A615T alters KATNIP binding versus stabilization not fully resolved
  11. 2025 Medium

    Refined the KATNIP activation mechanism and broadened the disease spectrum, showing a C-terminal KATNIP residue stretch (1524-1573) is required to activate CILK1 (separating binding from activation), and a C-terminal frameshift CILK1 variant causes cranioectodermal dysplasia with rescuable ciliary defects.

    Evidence KATNIP deletion constructs with TDY/substrate phosphorylation and cilia assays; patient-derived cells, C. elegans model, and CILK1 re-expression rescue

    PMID:40615527 PMID:40621737

    Open questions at the time
    • Structural basis of KATNIP-mediated activation not solved
    • Single-lab disease cohorts

Open questions

Synthesis pass · forward-looking unresolved questions
  • The full set of physiologically relevant CILK1 substrates beyond KIF3A and Raptor that drive Hedgehog, PCP, and developmental phenotypes remains unidentified.
  • No substrate proven to mediate the developmental ciliopathy phenotypes
  • Direct molecular mechanism converting tip kinase activity into IFT turnaround unresolved
  • No structure of CILK1 in complex with KATNIP or IFT-B

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 4 GO:0016740 transferase activity 3
Localization
GO:0005929 cilium 4 GO:0005815 microtubule organizing center 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-1852241 Organelle biogenesis and maintenance 3 R-HSA-5653656 Vesicle-mediated transport 3
Partners
CCRKIFT-BKATNIPKIF3AKLC3RPTORTBC1D32

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 ICK (intestinal cell kinase) was cloned and identified as a novel serine/threonine kinase harboring a dual phosphorylation site (TXY motif) found in MAP kinases, which is important for kinase activity; it localizes to the intestinal crypt region. PCR cloning from intestinal crypt cDNA library, Northern blot, RNA in situ hybridization Journal of cellular physiology Medium 10699974
2012 ICK promotes activation of mTOR complex 1 (mTORC1) by directly phosphorylating Raptor at Thr-908; ICK can phosphorylate Raptor both in vitro and in vivo, and expression of Raptor T908A mutant markedly impairs mTORC1 activation by insulin or RheB under nutrient starvation. In vitro kinase assay, mass spectrometry, phospho-specific antibody, co-immunoprecipitation, site-directed mutagenesis (T908A) The Journal of biological chemistry High 22356909
2014 ICK localizes to the tip of cilia and is essential for ciliary transport; loss of ICK in mice causes accumulation of IFT-A, IFT-B, and BBSome components at ciliary tips, while overexpression induces IFT-B (but not IFT-A or BBSome) accumulation at tips; ICK directly phosphorylates Kif3a, and inhibition of this phosphorylation affects ciliary formation. ICK-deficient mouse model, immunolocalization, live imaging, in vitro kinase assay (Kif3a phosphorylation), overexpression experiments The EMBO journal High 24797473
2014 ICK and MOK localize to cilia of renal epithelial cells and negatively regulate cilium length; ICK is transported as part of or by the IFT machinery (moves at ~0.45 µm/s similar to IFT proteins); ICK knockdown increases anterograde IFT velocities while overexpression reduces retrograde IFT speed; effects on cilia length and IFT are suppressed by rapamycin, implicating the mTORC1 pathway. Live fluorescence imaging of GFP-tagged IFT proteins, siRNA knockdown, overexpression, rapamycin treatment, velocity measurements PloS one High 25243405
2016 A missense mutation p.E80K in ICK abolishes serine/threonine kinase activity, resulting in altered ICK subcellular and ciliary localization, increased cilia length, aberrant cartilage growth plate structure, and defective Hedgehog and altered ERK signaling; ICK kinase activity is thus required for normal Hedgehog signaling and skeletogenesis. Exome sequencing of patient cohort, in vitro kinase activity assay of E80K mutant, immunofluorescence localization, patient fibroblast analysis Human molecular genetics High 27466187
2016 ICK mutations (p.R272Q and p.G120C) cause ECO syndrome; mutant ICK proteins mislocalize to the ciliary tip rather than distributing along the axoneme/ciliary base as wild-type ICK does; cells from affected individuals show decreased ciliation, confirming ICK regulates ciliogenesis. Homozygosity mapping, whole-exome sequencing, mRFP-ICK expression (wild-type and mutant), immunocytochemistry of patient fibroblasts Cilia Medium 27069622
2017 ICK regulates intraflagellar transport (IFT) at the tip of kinocilia in inner ear hair cells; loss of Ick leads to abnormal ciliary localization of IFT component Ift88, planar cell polarity (PCP) defects including misorientation of stereocilia and aberrant kinocilium localization, and auditory dysfunction. Conditional Ick knockout mice, immunofluorescence (Ift88 localization), auditory function tests (ABR), confocal microscopy of stereocilia The Journal of neuroscience High 28115485
2019 The C-terminal non-catalytic domain (CTD) of ICK/CAPK is required for substrate recognition and phosphorylation of KIF3A; CTD truncation impairs both KIF3A phosphorylation and localization of ICK to the primary cilium, and eliminates negative regulation of ciliogenesis. CTD truncation mutants, in vitro kinase assay (KIF3A phosphorylation), immunofluorescence localization, ciliation rate quantification Cells Medium 31277411
2020 ICK/CILK1 is transported anterogradely to the ciliary tip via direct interaction of its C-terminal non-catalytic region with the IFT-B complex; ICK undergoes bidirectional movement within cilia at velocities similar to IFT particles; ICK deficiency severely impairs retrograde IFT trafficking and causes ciliary proteins and IFT components to accumulate at the bulged ciliary tip, which can be released as extracellular vesicles; IFT-dependent transport of ICK, its kinase activity, and TDY motif phosphorylation are all required for ICK function. Co-immunoprecipitation (ICK C-terminal domain with IFT-B complex), total internal reflection fluorescence (TIRF) microscopy of ICK movement, ICK knockout cell analysis, exogenous expression of ICK constructs in KO cells The Journal of biological chemistry High 32732286
2020 JME pathogenic mutations in the CILK1 N-terminal kinase domain abolish kinase activity and eliminate phosphorylation of KIF3A at Thr672; JME mutations in the C-terminal non-catalytic domain (CTD) retain kinase activity but lose ability to restrict cilia length, promote ciliogenesis, and shift localization from the ciliary base to the entire axoneme. In vitro kinase assay (KIF3A-Thr672 phosphorylation), immunofluorescence localization, cilia length measurements, ciliation rate quantification Cells Medium 32178256
2020 Eliminating Kif3a Thr674 phosphorylation by Cilk1 (via T674A knock-in mouse) is insufficient to reproduce the severe developmental defects caused by Cilk1 loss of function, indicating that KIF3A-Thr672 phosphorylation is not essential for tissue development and that other CILK1 substrates mediate ciliopathy phenotypes. Kif3a T674A knock-in mouse model, skeletal analysis, MEF ciliation assay, cilia length measurement Developmental dynamics Medium 32935890
2022 BROMI/TBC1D32 interacts with CCRK/CDK20, which phosphorylates and activates ICK/CILK1; BROMI also interacts with FAM149B1/JBTS36 and CFAP20; CCRK-KO, BROMI-KO, and FAM149B1-KO cells all show abnormally long cilia and accumulation of IFT machinery and ICK at the ciliary tip, placing CCRK upstream of ICK in a signaling axis that regulates IFT turnaround at the ciliary tip. Co-immunoprecipitation, knockout cell analysis (CCRK-KO, BROMI-KO, FAM149B1-KO), rescue experiments with BROMI mutants defective in CCRK binding, immunofluorescence Molecular biology of the cell High 35609210
2022 Alvocidib potently inhibits CILK1 kinase activity (IC50 = 20 nM) and induces CILK1-dependent cilia elongation, demonstrating pharmacological inhibition of CILK1 modulates primary cilia length. In vitro kinase inhibition assay (IC50 determination), cilia length measurements in cells treated with Alvocidib vs. CILK1 KO cells International journal of molecular sciences Medium 35897693
2022 KLC3 (kinesin light chain-3) interacts with CILK1 at cilia bases; in CILK1-deficient cells, KLC3 is upregulated and its overexpression promotes ciliary recruitment of IFT-B and EGFR, contributing to cystic defects; reduction of KLC3 rescues ciliary defects and inhibits cyst progression in CILK1-deficient kidneys. Yeast two-hybrid, co-immunoprecipitation, immunocytochemistry, conditional Cilk1 KO mice, KLC3 knockdown rescue experiments Journal of the American Society of Nephrology Medium 35961787
2023 KATNIP (katanin-interacting protein/KIAA0556) co-localizes with CILK1 at the basal body; the CILK1 C-terminal intrinsically disordered region (IDR) mediates binding to KATNIP; KATNIP binding drastically elevates CILK1 protein levels and TDY motif phosphorylation (activation), increases phosphorylation of CILK1 substrates, and suppresses cilia length, establishing KATNIP as a regulatory scaffold that potentiates CILK1 function. Co-immunoprecipitation, deletion analysis of CILK1 IDR and KATNIP DUF domains, immunofluorescence colocalization, CILK1 substrate phosphorylation assays, cilia length measurement Molecular and cellular biology High 37665596
2024 CCRK kinase is an upstream activator of both Mak and Ick in retinal photoreceptor cells; Mak and Ick cooperatively regulate IFT at ciliary tips; simultaneous disruption of Mak and Ick causes loss of photoreceptor ciliary axonemes and severe retinal degeneration; gene delivery of Ick ameliorates retinal degeneration in Mak-deficient mice; FGF receptors act as negative regulators of Ick. Conditional double-KO mouse model (Mak and Ick), AAV-mediated Ick gene delivery rescue, FGF receptor inhibitor treatment, retinal histology, in vivo epistasis analysis Life science alliance High 39293864
2024 A JME-associated CILK1 A615T variant (in the C-terminal IDR) compromises KATNIP-mediated regulation of CILK1; MEFs with the A612T knock-in allele (heterozygous or homozygous) show higher ciliation rate, shorter cilia, and upregulation of ciliary Hedgehog signaling; the CILK1 A615T mutant protein is not elevated by KATNIP co-expression to the same extent as wild-type CILK1. Knock-in mouse model (A612T), MEF analysis, immunofluorescence (ciliation rate, cilia length), Hedgehog signaling readout, co-expression with KATNIP Cells Medium 39120290
2025 KATNIP disease variants that truncate near the C-terminus (M1474C) bind to CILK1 but do not support TDY activating phosphorylation in CILK1, phosphorylation of CILK1 substrates, or restriction of cilia length and ciliation rate; residues 1524-1573 of KATNIP (predicted β-sheets and α-helix) are essential for CILK1 activation, separating KATNIP's binding and activation functions for CILK1. KATNIP deletion constructs, Co-immunoprecipitation, TDY phosphorylation assay, CILK1 substrate phosphorylation assay, cilia length and ciliation rate quantification Journal of cell science Medium 40621737
2025 A homozygous frameshift variant in the CILK1 non-catalytic C-terminal domain causes cranioectodermal dysplasia; patient-derived cells show reduced cilia number, increased cilia length, and disrupted IFT component localization; the CILK1 variant protein retains correct ciliary localization; reintroduction of wild-type CILK1 rescues the majority of ciliary defects. Patient-derived cell analysis, C. elegans model, immunofluorescence (cilia number/length, IFT localization), rescue by CILK1 re-expression European journal of human genetics Medium 40615527
2024 In C. elegans, absence of DYF-5 (CILK1 homolog) causes accumulation of IFT components at the ciliary tip, loss of restriction of kinesin-II to the proximal ciliary segment, reduced IFT train frequency (especially retrograde trains), and impaired retrograde transport leading to depletion of IFT components at the ciliary base and impeded anterograde train assembly; DYF-5/CILK1 thus regulates IFT train turnaround at the ciliary tip. Fluorescence imaging and single-molecule tracking in live C. elegans phasmid cilia, IFT velocity and frequency measurements in dyf-5 null mutants bioRxivpreprint Medium bio_10.1101_2024.09.11.612404

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 ICK is essential for cell type-specific ciliogenesis and the regulation of ciliary transport. The EMBO journal 104 24797473
2014 Regulation of cilium length and intraflagellar transport by the RCK-kinases ICK and MOK in renal epithelial cells. PloS one 81 25243405
2016 An inactivating mutation in intestinal cell kinase, ICK, impairs hedgehog signalling and causes short rib-polydactyly syndrome. Human molecular genetics 46 27466187
2011 Analyses of phylogeny, evolution, conserved sequences and genome-wide expression of the ICK/KRP family of plant CDK inhibitors. Annals of botany 46 21385782
2000 Intestinal cell kinase (ICK) localizes to the crypt region and requires a dual phosphorylation site found in map kinases. Journal of cellular physiology 46 10699974
2016 A novel ICK mutation causes ciliary disruption and lethal endocrine-cerebro-osteodysplasia syndrome. Cilia 36 27069622
2013 Multiple actions of phi-LITX-Lw1a on ryanodine receptors reveal a functional link between scorpion DDH and ICK toxins. Proceedings of the National Academy of Sciences of the United States of America 34 23671114
2020 Anterograde trafficking of ciliary MAP kinase-like ICK/CILK1 by the intraflagellar transport machinery is required for intraciliary retrograde protein trafficking. The Journal of biological chemistry 33 32732286
2012 Intestinal cell kinase (ICK) promotes activation of mTOR complex 1 (mTORC1) through phosphorylation of Raptor Thr-908. The Journal of biological chemistry 31 22356909
2017 Ick Ciliary Kinase Is Essential for Planar Cell Polarity Formation in Inner Ear Hair Cells and Hearing Function. The Journal of neuroscience : the official journal of the Society for Neuroscience 28 28115485
2019 The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework. The Journal of biological chemistry 27 30975904
2019 Ciliopathy-Associated Protein Kinase ICK Requires Its Non-Catalytic Carboxyl-Terminal Domain for Regulation of Ciliogenesis. Cells 25 31277411
2013 A novel ICK peptide from the Loxosceles intermedia (brown spider) venom gland: cloning, heterologous expression and immunological cross-reactivity approaches. Toxicon : official journal of the International Society on Toxinology 23 23751278
2020 Functional Alterations in Ciliogenesis-Associated Kinase 1 (CILK1) that Result from Mutations Linked to Juvenile Myoclonic Epilepsy. Cells 16 32178256
2020 Phosphosite T674A mutation in kinesin family member 3A fails to reproduce tissue and ciliary defects characteristic of CILK1 loss of function. Developmental dynamics : an official publication of the American Association of Anatomists 16 32935890
2013 Distinct expression patterns of ICK/MAK/MOK protein kinases in the intestine implicate functional diversity. PloS one 16 24244486
2000 Association between GM3 and CD4-Ick complex in human peripheral blood lymphocytes. Glycoconjugate journal 15 11201797
2022 BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36 contributes to intraflagellar transport turnaround involving ICK/CILK1. Molecular biology of the cell 12 35609210
2018 Enriched expression of the ciliopathy gene Ick in cell proliferating regions of adult mice. Gene expression patterns : GEP 12 29635032
1998 The Ick protein tyrosine kinase is not involved in antibody-mediated CD4 (CDR3-loop) signal transduction that inhibits HIV-1 transcription. European journal of immunology 12 9603449
2020 A Chemical Biology Approach to Probing the Folding Pathways of the Inhibitory Cystine Knot (ICK) Peptide ProTx-II. Frontiers in chemistry 10 32309273
2022 Modulation of Primary Cilia by Alvocidib Inhibition of CILK1. International journal of molecular sciences 9 35897693
2021 New Insectotoxin from Tibellus Oblongus Spider Venom Presents Novel Adaptation of ICK Fold. Toxins 8 33406803
2023 The Scaffold Protein KATNIP Enhances CILK1 Control of Primary Cilia. Molecular and cellular biology 7 37665596
2022 KLC3 Regulates Ciliary Trafficking and Cyst Progression in CILK1 Deficiency-Related Polycystic Kidney Disease. Journal of the American Society of Nephrology : JASN 6 35961787
2017 Identification and functional analysis of the ICK gene family in maize. Scientific reports 6 28262730
2024 Structural analysis of a U-superfamily conotoxin containing a mini-granulin fold: Insights into key features that distinguish between the ICK and granulin folds. The Journal of biological chemistry 5 38508311
2024 Ccrk-Mak/Ick signaling is a ciliary transport regulator essential for retinal photoreceptor survival. Life science alliance 5 39293864
2013 Characterization and expression of the gene encoding En-MAPK1, an intestinal cell kinase (ICK)-like kinase activated by the autocrine pheromone-signaling loop in the Polar Ciliate, Euplotes nobilii. International journal of molecular sciences 4 23552830
2025 A homozygous frameshift variant in the CILK1 gene causes cranioectodermal dysplasia. European journal of human genetics : EJHG 2 40615527
2025 Human disease variants of KATNIP fail to support CILK1 activation and control of primary cilia. Journal of cell science 2 40621737
2024 An Epilepsy-Associated CILK1 Variant Compromises KATNIP Regulation and Impairs Primary Cilia and Hedgehog Signaling. Cells 2 39120290
2021 Mice Harboring a Non-Functional CILK1/ICK Allele Fail to Model the Epileptic Phenotype in Patients Carrying Variant CILK1/ICK. International journal of molecular sciences 2 34445580
2025 Progressive tooth pattern changes in Cilk1-deficient mice depending on Hedgehog signaling. International journal of oral science 1 41320695
2026 Use of Small-Molecule Inhibitors of CILK1 and AURKA as Cilia-Promoting Drugs to Decelerate Medulloblastoma Cell Replication. Biomedicines 0 41751164
2025 Cilk1 Is Essential for Mesenchymal Cilia Maintenance and Epithelial-mesenchymal Crosstalk in Intestinal Villus Morphogenesis. Cellular and molecular gastroenterology and hepatology 0 41192595
2024 An epilepsy-associated CILK1 variant compromises KATNIP regulation and impairs primary cilia and Hedgehog signaling. bioRxiv : the preprint server for biology 0 38798407

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