Comparative structural analysis of eukaryotic flagella and cilia from Chlamydomonas, Tetrahymena, and sea urchins

Pigino, Gaia; Maheshwari, Aditi; Bui, Khanh Huy; Shingyoji, Chikako; Kamimura, Shinji; Ishikawa, Takashi

doi:10.1016/j.jsb.2012.02.012

Cited by 89 publications

(141 citation statements)

References 30 publications

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“…In addition, MIP1a of Chlamydomonas flagella has three slightly different structures that repeat with a 48-nm periodicity (Pigino et al, 2012). This feature has also been observed in sea urchin sperm, but not in Tetrahymena.…”

Section: Fap85 Is a Component Of Mip1a Characteristic Of Chlamydomonasmentioning

confidence: 72%

“…Various types of MIPs have been described in a variety of organisms, and the divergence in their molecular architecture as well as their structural similarities have been revealed. Specifically, the divergence of these MIPs may contribute to differences in the bending patterns of these organisms, as pointed out by Pigino and colleagues (Pigino et al, 2012).…”

Section: Introductionmentioning

confidence: 92%

“…Comparison of the axonemes from various types of organisms has enabled the categorization of MIPs into several types such as MIP1a, MIP1b, MIP2a, MIP2b, MIP3a, MIP3b and MIP4 (Pigino et al, 2012). Numerous MIPs are well conserved in different organisms; however, organismsspecific MIPs have also been reported.…”

Section: Fap85 Is a Component Of Mip1a Characteristic Of Chlamydomonasmentioning

confidence: 99%

“…On the basis of the observation on the Sarkosyl-treated A-tubule in (A), the position of FAP85 overlapped with MIP1a (the yellow blob) but not MIP1b (the green blob). Modified after Pigino et al, 2012. structure bridging protofilaments 5th to 7th of A-tubules (these correspond to protofilaments 10th to 8th in the study from Pigino and colleagues [Pigino et al, 2012]). Therefore, comparing the localization and the periodicity of FAP85 on the A-tubule with that of the previously described MIP1a, we concluded that FAP85 is a component of MIP1a.…”

Section: Fap85 Is a Component Of Mip1a Characteristic Of Chlamydomonasmentioning

confidence: 99%

“…Only a small number of FAPs have been characterized biochemically and/or biophysically. Recent progress in electron tomography has enabled the elucidation of minor flagellar structures such as proteins within the DMTs, known as microtubule inner proteins (MIPs) (Heuser et al, 2012;Ichikawa et al, 2017;Maheshwari et al, 2015;Nicastro et al, 2011Nicastro et al, , 2006Pigino et al, 2012;Sui and Downing, 2006). However, the composition, biochemical properties, and functions of these MIPs have not been well characterized.…”

Section: Introductionmentioning

confidence: 99%

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Flagellar-associated Protein FAP85 Is a Microtubule Inner Protein That Stabilizes Microtubules

Kirima

Oiwa

2018

Cell Struct. Funct.

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Section: Fap85 Is a Component Of Mip1a Characteristic Of Chlamydomonasmentioning

confidence: 72%

Section: Introductionmentioning

confidence: 92%

Section: Fap85 Is a Component Of Mip1a Characteristic Of Chlamydomonasmentioning

confidence: 99%

Section: Fap85 Is a Component Of Mip1a Characteristic Of Chlamydomonasmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Flagellar-associated Protein FAP85 Is a Microtubule Inner Protein That Stabilizes Microtubules

Kirima

Oiwa

2018

Cell Struct. Funct.

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Tubulin and Microtubules

Amos

2015

Encyclopedia of Life Sciences

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Microtubules are found in almost all types of eukaryotic cell. Their principal constituents are the highly conserved proteins of the tubulin family, in the form of longitudinal protofilaments of tubulin heterodimers. The conserved lateral interactions produce a characteristic 2D lattice. Tubulin structure and conformational changes are now known to atomic resolution. Its GTP‐dependent dynamic self‐assembly and disassembly is modulated by a host of other proteins. This dynamic activity and a more passive role as tracks for interaction with motor proteins, kinesin and dynein, allow microtubules to perform vital roles in various forms of cell motility. They are an essential component of cell division, provide oriented tracks for the transport of cellular organelles and vesicles and are responsible for the relative positioning of cellular compartments. Thus, they are important targets in the control of cancer cells, as their essential activity is severely affected by a variety of drugs. Key Concepts Tubulin heterodimers, consisting of highly homologous α‐ and β‐tubulin monomers, self‐assemble into a unique lattice with polar longitudinal ‘protofilaments’ The assembled sheet has a slightly variable curvature, producing microtubules, with around 13 protofilaments but not strictly defined unless they are grown from a γ‐tubulin template or given a curvature appropriate to exactly 13 protofilaments by accessory proteins The structure of microtubules has been solved to near‐atomic level both with GTP homologues bound to β‐tubulin and with GDP bound; also a depolymerised protofilament structure in a longitudinally curved conformation is known Hydrolysis of bound GTP enables microtubules to assemble with ‘dynamic instability’, behaviour that depends on stochastic disassembly when the GTP ‘cap’ is lost from a growing end Microtubule behaviour is modified by many different accessory proteins that may act just at the tips or everywhere on the lattice wall To play different roles according to their positions in cells, the properties of microtubules may vary owing to different tubulin isotypes and be modified by a wide range of associated proteins Changes can also vary with time (‘ageing’) as a result of post‐translational modification of tubulin and of some accessory proteins Microtubules are employed in axonemes of cilia and flagella, where the motor protein dynein interacts with them to produce beating while other linking components help control the wave‐form Cytoplasmic microtubules provide tracks for vesicles and other cargoes driven by kinesins and cytoplasmic dynein Mitotic and meiotic spindles are assembled from microtubules, which interact with kinetochores and with multiple motor proteins Microtubules are susceptible to many small molecules that depolymerise or hyperstabilise them and thus serve as anti‐cancer drugs.

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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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Comparative structural analysis of eukaryotic flagella and cilia from Chlamydomonas, Tetrahymena, and sea urchins

Cited by 89 publications

References 30 publications

Flagellar-associated Protein FAP85 Is a Microtubule Inner Protein That Stabilizes Microtubules

Flagellar-associated Protein FAP85 Is a Microtubule Inner Protein That Stabilizes Microtubules

Tubulin and Microtubules

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

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