ArticleProceedings of the National Academy of Sciences of the United States of America2013
Activation loop phosphorylation of a protein kinase is a molecular marker of organelle size that dynamically reports flagellar length.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed.
- Precise subcellular organelle-targeted analyses of hepatotoxicity ofChinese herbal medicines · 2026Article
- The flagellar length control system: exploring the physical biology of organelle size.Physical biology · 2023Review
- Identification and Functional Analysis of Key Autophosphorylation Residues of Arabidopsis Senescence Associated Receptor-like Kinase.International journal of molecular sciences · 2022Article
- Review
- Nanobody-directed targeting of optogenetic tools to study signaling in the primary cilium.eLife · 2020Article
- FLS2 is a CDK-like kinase that directly binds IFT70 and is required for proper ciliary disassembly in Chlamydomonas.PLoS genetics · 2020Article
- Potassium channel KCN11 is required for maintaining cellular osmolarity during nitrogen starvation to control proper cell physiology and TAG accumulation inBiotechnology for biofuels · 2020Article
- Length regulation of multiple flagella that self-assemble from a shared pool of components.eLife · 2019Article
- A CCRK and a MAK Kinase Modulate Cilia Branching and Length via Regulation of Axonemal Microtubule Dynamics in Caenorhabditis elegans.Current biology : CB · 2019Article
- Rapid and high efficiency transformation ofBioscience reports · 2019Article
- Diffusion as a Ruler: Modeling Kinesin Diffusion as a Length Sensor for Intraflagellar Transport.Biophysical journal · 2018Article
- A novel interaction between kinase activities in regulation of cilia formation.BMC cell biology · 2017Article
- Testing the time-of-flight model for flagellar length sensing.Molecular biology of the cell · 2017Article
- Protein transport in growing and steady-state cilia.Traffic (Copenhagen, Denmark) · 2017Review
- Intraflagellar Transport and Ciliary Dynamics.Cold Spring Harbor perspectives in biology · 2017Review
- Two classes of short intraflagellar transport train with different 3D structures are present in Chlamydomonas flagella.Journal of cell science · 2016Article
- Mechanism of ciliary disassembly.Cellular and molecular life sciences : CMLS · 2016Review
- A NIMA-related kinase, CNK4, regulates ciliary stability and length.Molecular biology of the cell · 2016Article
- Regulation of Chlamydomonas flagella and ependymal cell motile cilia by ceramide-mediated translocation of GSK3.Molecular biology of the cell · 2015Article
- Ciliary/Flagellar Protein Ubiquitination.Cells · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Specification of organelle size is crucial for cell function, yet we know little about the molecular mechanisms that report and regulate organelle growth and steady-state dimensions. The biflagellated green alga Chlamydomonas requires continuous-length feedback to integrate the multiple events that support flagellar assembly and disassembly and at the same time maintain the sensory and motility functions of the organelle. Although several length mutants have been characterized, the requisite molecular reporter of length has not been identified. Previously, we showed that depletion of Chlamydomonas aurora-like protein kinase CALK inhibited flagellar disassembly and that a gel-shift-associated phosphorylation of CALK marked half-length flagella during flagellar assembly. Here, we show that phosphorylation of CALK on T193, a consensus phosphorylation site on the activation loop required for kinase activity, is distinct from the gel-shift-associated phosphorylation and is triggered when flagellar shortening is induced, thereby implicating CALK protein kinase activity in the shortening arm of length control. Moreover, CALK phosphorylation on T193 is dynamically related to flagellar length. It is reduced in cells with short flagella, elevated in the long flagella mutant, lf4, and dynamically tracks length during both flagellar assembly and flagellar disassembly in WT, but not in lf4. Thus, phosphorylation of CALK in its activation loop is implicated in the disassembly arm of a length feedback mechanism and is a continuous and dynamic molecular marker of flagellar length during both assembly and disassembly.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.