ArticleMolecular biology of the cell2011
Distinct roles of 1alpha and 1beta heavy chains of the inner arm dynein I1 of Chlamydomonas flagella.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Structure and Mechanics of Dynein Motors.Annual review of biophysics · 2021Review
- 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
- 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
- Ciliary proteins Fap43 and Fap44 interact with each other and are essential for proper cilia and flagella beating.Cellular and molecular life sciences : CMLS · 2018Article
- A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1).Molecular biology of the cell · 2018Article
- The I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility.Molecular biology of the cell · 2018Article
- Asymmetric distribution and spatial switching of dynein activity generates ciliary motility.Science (New York, N.Y.) · 2018Article
- Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017Review
- 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
- The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility.The Journal of cell biology · 2013Article
- Integrated control of axonemal dynein AAA(+) motors.Journal of structural biology · 2012Review
- Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- bop5 Mutations reveal new roles for the IC138 phosphoprotein in the regulation of flagellar motility and asymmetric waveforms.Molecular biology of the cell · 2011Article
- An axonemal PP2A B-subunit is required for PP2A localization and flagellar motility.Cytoskeleton (Hoboken, N.J.) · 2011Article
- Regulation of ciliary motility: conserved protein kinases and phosphatases are targeted and anchored in the ciliary axoneme.Archives of biochemistry and biophysics · 2011Review
- IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility.Molecular biology of the cell · 2009Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
Abstract
The Chlamydomonas I1 dynein is a two-headed inner dynein arm important for the regulation of flagellar bending. Here we took advantage of mutant strains lacking either the 1α or 1β motor domain to distinguish the functional role of each motor domain. Single- particle electronic microscopic analysis confirmed that both the I1α and I1β complexes are single headed with similar ringlike, motor domain structures. Despite similarity in structure, however, the I1β complex has severalfold higher ATPase activity and microtubule gliding motility compared to the I1α complex. Moreover, in vivo measurement of microtubule sliding in axonemes revealed that the loss of the 1β motor results in a more severe impairment in motility and failure in regulation of microtubule sliding by the I1 dynein phosphoregulatory mechanism. The data indicate that each I1 motor domain is distinct in function: The I1β motor domain is an effective motor required for wild-type microtubule sliding, whereas the I1α motor domain may be responsible for local restraint of microtubule sliding.
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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.