Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules

Linck, Richard W.; Stephens, R. E.

doi:10.1002/cm.20202

Cited by 42 publications

(41 citation statements)

References 66 publications

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“…Although there is general agreement that the A-tubules of most species are formed by 13 PFs (15), the number of PFs within the B-tubule has been controversial, being either 10 or 11 PFs (16). Our data clearly show a B-tubule with 10 PFs, of which at least PFs B2 to B10 † appear to be identical ( Fig.…”

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confidence: 50%

“…However, few axonemal structures have attracted more controversy about their architecture than the DMTs. First, whereas the A-tubules are composed of 13 protofilaments (PFs) (15) similar to native cytoplasmic MTs, the number of PFs in the B-tubules, 10 or 11, has been the subject of ongoing debate (16). Second, the nature of the junctions that the B-tubule makes with the A-tubule is unknown.…”

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confidence: 99%

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Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Nicastro¹,

Heuser³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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The axoneme forms the essential and conserved core of cilia and flagella. We have used cryo-electron tomography of Chlamydomonas and sea urchin flagella to answer long-standing questions and to provide information about the structure of axonemal doublet microtubules (DMTs). Solving an ongoing controversy, we show that B-tubules of DMTs contain exactly 10 protofilaments (PFs) and that the inner junction (IJ) and outer junction between the A-and B-tubules are fundamentally different. The outer junction, crucial for the initiation of doublet formation, appears to be formed by close interactions between the tubulin subunits of three PFs with unusual tubulin interfaces; other investigators have reported that this junction is weakened by mutations affecting posttranslational modifications of tubulin. The IJ consists of an axially periodic ladder-like structure connecting tubulin PFs of the A-and B-tubules. The recently discovered microtubule inner proteins (MIPs) on the inside of the A-and B-tubules are more complex than previously thought. They are composed of alternating small and large subunits with periodicities of 16 and/or 48 nm. MIP3 forms arches connecting B-tubule PFs, contrary to an earlier report that MIP3 forms the IJ. Finally, the "beak" structures within the B-tubules of Chlamydomonas DMT1, DMT5, and DMT6 are clearly composed of a longitudinal band of proteins repeating with a periodicity of 16 nm. These findings, discussed in relation to genetic and biochemical data, provide a critical foundation for future work on the molecular assembly and stability of the axoneme, as well as its function in motility and sensory transduction.microtubule stability | cilia | axoneme | ciliopathies | cytoskeleton

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Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Nicastro¹,

Heuser³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

136

208

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“…1 (11, 12, 15, 27, 32, 44, 58–63). Here, using biochemical fractionation techniques, proteomics, immunoelectron microscopy, cryo-electron tomography (cryo-EM), and a new, integrative approach of immuno-cryo-EM/ET, we have localized Sp Rib74 and Sp Rib85.5, resolved the location of the Ribbon of four stable protofilaments in flagellar DMTs, and furthered our understanding of tektin filament structure and location.…”

Section: Introductionmentioning

confidence: 99%

Insights into the Structure and Function of Ciliary and Flagellar Doublet Microtubules

Linck

Lin

et al. 2014

Journal of Biological Chemistry

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Background: Ciliary microtubules contain hyperstable Ribbons of adjoining protofilaments.Results: Using echinoderm flagella, the locations of Ribbons, tektins, and Ca2+-binding proteins (related to human epilepsy) are studied biochemically and by immuno-cryo-electron tomography.Conclusion: The locations of these proteins create a biochemically, structurally unique region of ciliary A-microtubules.Significance: The results indicate specialized functions for Ribbons, with potential roles in assembly, motility, and/or signal transduction.

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“…At the same time, they also give rise to the poles of the mitotic spindle. Centrioles may function as a signaling platform, through proteins that promote the transition from one phase to another in mitosis [18].  Apc2, anaphase promoting complex protein 2  Platelet-derived growth factor receptors (Pdgfr) The Centrosome is an organelle located in the center of eukaryotic cells, and acts as an organizing center rather than a microtubule [19].…”

Section: Cell Cycle: Centriole Union Linkmentioning

confidence: 99%

Ciliopathies: Primary Cilia and Signaling Pathways in Mammalian Development

Romero¹,

Solano²,

Cabo³

2011

Neuroimaging for Clinicians - Combining Research and Practice

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Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules

Abstract: This article discusses the current state of knowledge about the evolutionarily conserved structure of ciliary, flagellar and centriolar microtubules, and formally proposes a functional numbering convention for their protofilaments. Cell Motil. Cytoskeleton 64: 489-495, 2007

Cited by 42 publications

References 66 publications

Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Insights into the Structure and Function of Ciliary and Flagellar Doublet Microtubules

Ciliopathies: Primary Cilia and Signaling Pathways in Mammalian Development

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