ArticleDevelopmental dynamics : an official publication of the American Association of Anatomists2021
Phosphosite T674A mutation in kinesin family member 3A fails to reproduce tissue and ciliary defects characteristic of CILK1 loss of function.
Article in Developmental dynamics : an official publication of the American Association of Anatomists, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Phosphorylation at the Helm: Kinase-Mediated Regulation of Primary Cilia Assembly and Disassembly.Cytoskeleton (Hoboken, N.J.) · 2025Review
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Kinase-dependent regulation of ciliary protein transport and its implications for therapy.Frontiers in molecular biosciences · 2025Review
- Ccrk-Mak/Ick signaling is a ciliary transport regulator essential for retinal photoreceptor survival.Life science alliance · 2024Article
- Article
- KIF3A tail domain phosphorylation is not required for ciliogenesis in mouse embryonic fibroblasts.iScience · 2024Article
- Class switching is differentially regulated in RBC alloimmunization and vaccination.Transfusion · 2023Article
- Review
- BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36 contributes to intraflagellar transport turnaround involving ICK/CILK1.Molecular biology of the cell · 2022Article
- Modulation of Primary Cilia by Alvocidib Inhibition of CILK1.International journal of molecular sciences · 2022Article
- Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport.Frontiers in cell and developmental biology · 2022Review
- CCRK/CDK20 regulates ciliary retrograde protein trafficking via interacting with BROMI/TBC1D32.PloS one · 2021Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
backgroundKinesin family member 3A (KIF3A) is a molecular motor protein in the heterotrimeric kinesin-2 complex that drives anterograde intraflagellar transport. This process plays a pivotal role in both biogenesis and maintenance of the primary cilium that supports tissue development. Ciliogenesis associated kinase 1 (CILK1) phosphorylates human KIF3A at Thr672. CILK1 loss of function causes ciliopathies that manifest profound and multiplex developmental defects, including hydrocephalus, polydactyly, shortened and hypoplastic bones and alveoli airspace deficiency, leading to perinatal lethality. Prior studies have raised the hypothesis that CILK1 phosphorylation of KIF3A is critical for its regulation of organ development.
resultsWe produced a mouse model with phosphorylation site Thr674 in mouse Kif3a mutated to Ala. Kif3a T674A homozygotes are viable and exhibit no skeletal and brain abnormalities, and only mildly reduced airspace in alveoli. Mouse embryonic fibroblasts carrying Kif3a T674A mutation show a normal rate of ciliation and a moderate increase in cilia length.
conclusionThese results indicate that eliminating Kif3a Thr674 phosphorylation by Cilk1 is insufficient to reproduce the severe developmental defects in ciliopathies caused by Cilk1 loss of function. This suggests KIF3A-Thr672 phosphorylation by CILK1 is not essential for tissue development and other substrates are involved in CILK1 ciliopathies.
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