FAP20 is an inner junction protein of doublet microtubules essential for both the planar asymmetrical waveform and stability of flagella in<i>Chlamydomonas</i>

Yanagisawa, Haruaki; Mathis, Garrison; Oda, Toshiyuki; Hirono, Masafumi; Richey, Elizabeth A.; Ishikawa, Hiroaki; Marshall, Wallace F.; Kikkawa, Masahide; Qin, Hongmin

doi:10.1091/mbc.e13-08-0464

Cited by 82 publications

(163 citation statements)

References 67 publications

(113 reference statements)

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“…FAP20 was proposed to be a candidate for the non-tubulin continuous density by cryo-electron tomography combined with protein tagging9. In our structure, we were not able to observe this density (Fig.…”

Section: Resultsmentioning

confidence: 57%

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Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins

et al. 2017

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Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign α- and β-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule.

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Section: Resultsmentioning

confidence: 57%

“…4d). Second, Yanagisawa et al 9. recently proposed that in Chlamydomonas , tektin forms the inner junction non-tubulin structure together with FAP20 and PACRG.…”

Section: Discussionmentioning

confidence: 99%

Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins

et al. 2017

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“…Previous studies have suggested that PACRG interacts with the axonemal protein FAP20, localized at the inner junction of doublet microtubules (Yanagisawa et al ., 2014). This location is near the root of the RSs on the A2 and A3 protofilaments (Nicastro et al ., 2006; Barber et al ., 2012); therefore, it is possible that PACRG and its interactors are involved in relaying signals from the CA and RSs to the inner dynein arms.…”

Section: Resultsmentioning

confidence: 99%

“…Additional studies have suggested that Rib72, PACRG (the Parkin co-regulated gene product), FAP252, and FAP20 form a complex which is anchored to the doublet microtubules (Ikeda et al ., 2007; Yanagisawa et al ., 2014). Rib72 was simultaneously discovered by three different labs.…”

Section: Introductionmentioning

confidence: 99%

“…In addition Ikeda has shown that PACRG binds directly to tubulin and microtubules (Ikeda, 2008). More recently, Yanagisawa et al have shown that FAP20 is an inner junction protein of the doublets, and that PACRG, but not Rib72, is reduced in FAP20 mutants (Yanagisawa et al ., 2014) indicating that FAP20 may also interact with PACRG. FAP20 mutants, like PACRG mutants, have cilia with abnormal motility.…”

Section: Introductionmentioning

confidence: 99%

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Microtubule binding protein PACRG plays a role in regulating specific ciliary dyneins during microtubule sliding

Mizuno¹,

Dymek

Smith

2016

Cytoskeleton

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The complex waveforms characteristic of motile eukaryotic cilia and flagella are produced by the temporally and spatially regulated action of multiple dynein subforms generating sliding between subsets of axonemal microtubules. Multiple protein complexes have been identified that are associated with the doublet microtubules and that mediate regulatory signals between key axonemal structures, such as the radial spokes and central apparatus, and the dynein arm motors; these complexes include the N-DRC, MIA, and CSC complexes. Previous studies have shown that PACRG (parkin co-regulated gene) forms a complex that is anchored to the axonemal doublet microtubules. Loss of PACRG causes defects in ciliary motility and cilia related diseases. Here, we use an in vitro microtubule sliding assay to demonstrate that PACRG and its interactors are part of a signaling pathway that includes the central apparatus, radial spokes and specific inner dynein arm subforms to control dynein-driven microtubule sliding. Using a biochemical approach, our studies also indicate that PACRG interacts with the radial spokes.

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Microtubule Inner Proteins: A Meshwork of Luminal Proteins Stabilizing the Doublet Microtubule

Ichikawa

Bui

2018

BioEssays

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Motile eukaryotic cilia and flagella are hair-like organelles responsible for cell motility and mucociliary clearance. Using cryo-electron tomography, it has been shown that the doublet microtubule, the cytoskeleton core of the cilia and flagella, has microtubule inner protein structures binding periodically inside its lumen. More recently, single-particle cryo-electron microscopy analyses of isolated doublet microtubules have shown that microtubule inner proteins form a meshwork inside the doublet microtubule. High-resolution structures revealed new types of interactions between the microtubule inner proteins and the tubulin lattice. In addition, they offered insights into the potential roles of microtubule inner proteins in the stabilization and assembly of the doublet microtubule. Herein, we review our new insights into microtubule inner proteins from the doublet microtubule together with the current body of literature on microtubule inner proteins.

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FAP20 is an inner junction protein of doublet microtubules essential for both the planar asymmetrical waveform and stability of flagella inChlamydomonas

Cited by 82 publications

References 67 publications

Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins

Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins

Microtubule binding protein PACRG plays a role in regulating specific ciliary dyneins during microtubule sliding

Microtubule Inner Proteins: A Meshwork of Luminal Proteins Stabilizing the Doublet Microtubule

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