ArticleMolecular biology of the cell2004
IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Article
- Consensus nomenclature for dyneins and associated assembly factors.The Journal of cell biology · 2022Article
- Structure of Motile Cilia.Sub-cellular biochemistry · 2022Article
- Structural organization of the intermediate and light chain complex of Chlamydomonas ciliary I1 dynein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Composition and function of ciliary inner-dynein-arm subunits studied in Chlamydomonas reinhardtii.Cytoskeleton (Hoboken, N.J.) · 2021Review
- A dynein-associated photoreceptor protein prevents ciliary acclimation to blue light.Science advances · 2021Article
- Mutations in PIH proteins MOT48, TWI1 and PF13 define common and unique steps for preassembly of each, different ciliary dynein.PLoS genetics · 2020Article
- LAX28 is required for the stable assembly of the inner dynein arm f complex, and the tether and tether head complex inJournal of cell science · 2020Article
- FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia.Molecular biology of the cell · 2019Article
- Vertebrate Dynein-f depends on Wdr78 for axonemal localization and is essential for ciliary beat.Journal of molecular cell biology · 2019Article
- WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions.The protein journal · 2018Review
- Turning dyneins off bends cilia.Cytoskeleton (Hoboken, N.J.) · 2018Article
- The I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility.Molecular biology of the cell · 2018Article
- A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1).Molecular biology of the cell · 2018Article
- The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length.Molecular biology of the cell · 2018Article
- Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.PLoS genetics · 2017Article
- Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017Review
- Knockdown of Inner Arm Protein IC138 in Trypanosoma brucei Causes Defective Motility and Flagellar Detachment.PloS one · 2015Article
- The ciliary inner dynein arm, I1 dynein, is assembled in the cytoplasm and transported by IFT before axonemal docking.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Slow axonemal dynein e facilitates the motility of faster dynein c.Biophysical journal · 2014Article
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8 authors.
Funding
Abstract
Increased phosphorylation of dynein IC IC138 correlates with decreases in flagellar microtubule sliding and phototaxis defects. To test the hypothesis that regulation of IC138 phosphorylation controls flagellar bending, we cloned the IC138 gene. IC138 encodes a novel protein with a calculated mass of 111 kDa and is predicted to form seven WD-repeats at the C terminus. IC138 maps near the BOP5 locus, and bop5-1 contains a point mutation resulting in a truncated IC138 lacking the C terminus, including the seventh WD-repeat. bop5-1 cells display wild-type flagellar beat frequency but swim slower than wild-type cells, suggesting that bop5-1 is altered in its ability to control flagellar waveform. Swimming speed is rescued in bop5-1 transformants containing the wild-type IC138, confirming that BOP5 encodes IC138. With the exception of the roadblock-related light chain, LC7b, all the other known components of the I1 complex, including the truncated IC138, are assembled in bop5-1 axonemes. Thus, the bop5-1 motility phenotype reveals a role for IC138 and LC7b in the control of flagellar bending. IC138 is hyperphosphorylated in paralyzed flagellar mutants lacking radial spoke and central pair components, further indicating a role for the radial spokes and central pair apparatus in control of IC138 phosphorylation and regulation of flagellar waveform.
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