Results 31 to 40 of about 16,625 (265)

A novel role of centrin in flagellar motility: stabilizing an inner-arm dynein motor in the flagellar axoneme

Microbial Cell, 2014
Centrin is an evolutionarily conserved EF-hand calcium-binding protein found in the centriole of animals and the basal body of flagellated organisms. It was originally discovered in the flagellated unicellular green alga Chlamydomonas reinhardtii, where ...
Ziyin Li
doaj   +1 more source

The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length [PDF]

, 2018
Axonemal dyneins, including inner dynein arm I1, assemble in the cytoplasm prior to transport into cilia by intraflagellar transport (IFT). How I1 dynein interacts with IFT is not understood.
Alford, Lea M, Dutcher, Susan K, Fu, Gang, Gokhale, Avanti, Hunter, Emily L, Hwang, Juyeon, Kamiya, Ritsu, Lechtreck, Karl, Lewis, Brian, Lin, Huawen, Nicastro, Daniela, Sale, Winfield S, Wirschell, Maureen, Yamamoto, Ryosuke, Yang, Fan   +14 more
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Axonemal Dynein Arms [PDF]

Cold Spring Harbor Perspectives in Biology, 2016
Axonemal dyneins form the inner and outer rows of arms associated with the doublet microtubules of motile cilia. These enzymes convert the chemical energy released from adenosine triphosphate (ATP) hydrolysis into mechanical work by causing the doublets to slide with respect to each other.
openaire   +2 more sources

Chlamydomonas Basal Bodies as Flagella Organizing Centers

Cells, 2018
During ciliogenesis, centrioles convert to membrane-docked basal bodies, which initiate the formation of cilia/flagella and template the nine doublet microtubules of the flagellar axoneme.
Jenna Lynne Wingfield, Karl-Ferdinand Lechtreck   +1 more
doaj   +1 more source

Mechanisms of Regulation in Intraflagellar Transport

Cells, 2022
Cilia are eukaryotic organelles essential for movement, signaling or sensing. Primary cilia act as antennae to sense a cell’s environment and are involved in a wide range of signaling pathways essential for development. Motile cilia drive cell locomotion
Wouter Mul, Aniruddha Mitra, Erwin J. G. Peterman   +2 more
doaj   +1 more source

Combined exome and whole-genome sequencing identifies mutations in ARMC4 as a cause of primary ciliary dyskinesia with defects in the outer dynein arm [PDF]

, 2013
Primary ciliary dyskinesia (PCD) is a rare, genetically heterogeneous ciliopathy disorder affecting cilia and sperm motility. A range of ultrastructural defects of the axoneme underlie the disease, which is characterised by chronic respiratory symptoms ...
Alexandros Onoufriadis, Amelia Shoemark, Anthony T Moore, Antony, Bush, Chela T James, Chiara Bacchelli, Claire Hogg, Eddie M K Chung, Elisabeth M Rosser, Fliegauf, Gerard Pals, Gherman, Hannah M Mitchison, Hirst, Hjeij, Hozumi, Jeannette E Danke-Roelse, John J Sloper, Kennedy, Knowles, Loges, Lonergan, Miriam Schmidts, Mitali Patel, Mustafa M Munye, O'Toole, Olbrich, Ong, Onoufriadis, Papon, Peter J Scambler, Philip L Beales, Plagnol, Richard D Emes, Roy, Sarah Hull, Schultz, Shoemark, Speder, Stephen L Hart, Tarkar, Tewari, Xu, Yang, Zhang   +45 more
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Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule

eLife, 2019
Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk.
Samuel E Lacey, Shaoda He, Sjors HW Scheres, Andrew P Carter   +3 more
doaj   +1 more source

Cfap91-Dependent Stability of the RS2 and RS3 Base Proteins and Adjacent Inner Dynein Arms in Tetrahymena Cilia

Cells, 2022
Motile cilia and eukaryotic flagella are specific cell protrusions that are conserved from protists to humans. They are supported by a skeleton composed of uniquely organized microtubules—nine peripheral doublets and two central singlets (9 × 2 + 2 ...
Marta Bicka, Ewa Joachimiak, Paulina Urbanska, Anna Osinka, Anna Konopka, Ewa Bulska, Dorota Wloga   +6 more
doaj   +1 more source

A Flagellar A-Kinase Anchoring Protein with Two Amphipathic Helices Forms a Structural Scaffold in the Radial Spoke Complex [PDF]

, 2012
A-kinase anchoring proteins (AKAPs) contain an amphipathic helix (AH) that binds the dimerization and docking (D/D) domain, RIIa, in cAMP-dependent protein kinase A (PKA). Many AKAPs were discovered solely based on the AH–RIIa interaction in vitro.
Alto, Angelo, Banky, Barber, Brokaw, Burns-Hamuro, Cao, Carr, Carr, Carr, Chen, Cho, Diener, Diener, Fujita, Gaillard, Gaillard, Gold, Greengard, Gupta, Habermacher, Habermacher, Herberg, Hirsch, Howard, Hsu, Huang, Jarnaess, Jennifer M. Dienes, Jiang, Kammerer, Kinderman, Kindle, Klauck, Kohno, Li, Martin St. Maurice, Mastronarde, Mauban, Means, Mitchell, Morikis, Newell, Nicastro, Omoto, Patel, Patel-King, Pauling, Pigino, Pinfen Yang, Priyanka Sivadas, Roguev, Rual, Sarma, Satir, Scott, Silflow, South, Wang, Warner, Wei, Welch, William D. Meek, Williams, Wirschell, Witman, Xia, Xu, Yang, Yang, Yang, Yang   +71 more
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Axonemal radial spokes [PDF]

BioArchitecture, 2012
The radial spoke (RS) is a complex of at least 23 proteins that works as a mechanochemical transducer between the central-pair apparatus and the peripheral microtubule doublets in eukaryotic flagella and motile cilia. The RS contributes to the regulation of the activity of dynein motors, and thus to flagellar motility.
Gaia, Pigino, Takashi, Ishikawa
openaire   +2 more sources