scholarly journals Proteins that control the geometry of microtubules at the ends of cilia

2018 ◽  
Vol 217 (12) ◽  
pp. 4298-4313 ◽  
Author(s):  
Panagiota Louka ◽  
Krishna Kumar Vasudevan ◽  
Mayukh Guha ◽  
Ewa Joachimiak ◽  
Dorota Wloga ◽  
...  
Keyword(s):  
Transition Zone ◽  
Basal Body ◽  
Distal Segment ◽  
Joubert Syndrome ◽  
Nanometer Scale ◽  
Negative Regulators ◽  
Middle Segment ◽  
Sensory Activities

Cilia, essential motile and sensory organelles, have several compartments: the basal body, transition zone, and the middle and distal axoneme segments. The distal segment accommodates key functions, including cilium assembly and sensory activities. While the middle segment contains doublet microtubules (incomplete B-tubules fused to complete A-tubules), the distal segment contains only A-tubule extensions, and its existence requires coordination of microtubule length at the nanometer scale. We show that three conserved proteins, two of which are mutated in the ciliopathy Joubert syndrome, determine the geometry of the distal segment, by controlling the positions of specific microtubule ends. FAP256/CEP104 promotes A-tubule elongation. CHE-12/Crescerin and ARMC9 act as positive and negative regulators of B-tubule length, respectively. We show that defects in the distal segment dimensions are associated with motile and sensory deficiencies of cilia. Our observations suggest that abnormalities in distal segment organization cause a subset of Joubert syndrome cases.

scholarly journals Super-resolution microscopy reveals that disruption of ciliary transition-zone architecture causes Joubert syndrome

2017 ◽  
Vol 19 (10) ◽  
pp. 1178-1188 ◽  
Author(s):  
Xiaoyu Shi ◽  
Galo Garcia ◽  
Julie C. Van De Weghe ◽  
Ryan McGorty ◽  
Gregory J. Pazour ◽  
...  
Keyword(s):  
Transition Zone ◽  
Super Resolution ◽  
Joubert Syndrome ◽  
Super Resolution Microscopy

scholarly journals Erratum: Super-resolution microscopy reveals that disruption of ciliary transition-zone architecture causes Joubert syndrome

2017 ◽  
Vol 19 (11) ◽  
pp. 1379-1379 ◽  
Author(s):  
Xiaoyu Shi ◽  
Galo Garcia ◽  
Julie C. Van De Weghe ◽  
Ryan McGorty ◽  
Gregory J. Pazour ◽  
...  
Keyword(s):  
Transition Zone ◽  
Super Resolution ◽  
Joubert Syndrome ◽  
Super Resolution Microscopy

scholarly journals The conserved centrosomal protein FOR20 is required for assembly of the transition zone and basal body docking at the cell surface

2012 ◽  
Vol 125 (18) ◽  
pp. 4395-4404 ◽  
Author(s):  
A. Aubusson-Fleury ◽  
M. Lemullois ◽  
N. G. de Loubresse ◽  
C. Laligne ◽  
J. Cohen ◽  
...  
Keyword(s):  
Cell Surface ◽  
Transition Zone ◽  
Basal Body ◽  
Centrosomal Protein

scholarly journals Bacterial Flagellum versus Carbon Nanotube: A Review Article on the Potential of Bacterial Flagellum as a Sustainable and Green Substance for the Synthesis of Nanotubes

2020 ◽  
Vol 13 (1) ◽  
pp. 21
Author(s):  
Charles Ng Wai Chun ◽  
Husnul Azan Tajarudin ◽  
Norli Ismail ◽  
Baharin Azahari ◽  
Muaz Mohd Zaini Makhtar ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Carbon Nanotubes ◽  
Carbon Nanotube ◽  
Basal Body ◽  
Research Area ◽  
Review Article ◽  
Nanometer Scale ◽  
Structural Components ◽  
Bacterial Flagellum ◽  
Bacterial Flagella

Bacterial flagella are complex multicomponent structures that help in cell locomotion. It is composed of three major structural components: the hook, the filament and basal body. The special mechanical properties of flagellar components make them useful for the applications in nanotechnology especially in nanotube formation. Carbon nanotubes (CNTs) are nanometer scale tube-shaped material and it is very useful in many applications. However, the production of CNTs is costly and detrimental to the environment as it pollutes the environment. Therefore, bacterial flagella have become a highly interesting research area especially in producing bacterial nanotubes that could replace CNTs. In this review article, we will discuss about bacterial flagellum and carbon nanotubes in the context of their types and applications. Then, we will focus and review on the characteristics of bacterial flagellum in comparison to carbon nanotubes and subsequently, the advantages of bacterial flagellum as nanotubes in comparison with carbon nanotubes.

scholarly journals Mutations in ARMC9 , which Encodes a Basal Body Protein, Cause Joubert Syndrome in Humans and Ciliopathy Phenotypes in Zebrafish

2017 ◽  
Vol 101 (1) ◽  
pp. 23-36 ◽  
Author(s):  
Julie C. Van De Weghe ◽  
Tamara D.S. Rusterholz ◽  
Brooke Latour ◽  
Megan E. Grout ◽  
Kimberly A. Aldinger ◽  
...  
Keyword(s):  
Basal Body ◽  
Joubert Syndrome ◽  
Body Protein

scholarly journals Novel Jbts17 mutant mouse model of Joubert syndrome with cilia transition zone defects and cerebellar and other ciliopathy related anomalies

2015 ◽  
Vol 24 (14) ◽  
pp. 3994-4005 ◽  
Author(s):  
Rama Rao Damerla ◽  
Cheng Cui ◽  
George C. Gabriel ◽  
Xiaoqin Liu ◽  
Branch Craige ◽  
...  
Keyword(s):  
Mouse Model ◽  
Transition Zone ◽  
Mutant Mouse ◽  
Joubert Syndrome

scholarly journals The ternary complex CEP90, FOPNL and OFD1 specifies the future location of centriolar distal appendages, and promotes their assembly

2021 ◽  
Author(s):  
Pierrick Le Borgne ◽  
Marine Hélène Laporte ◽  
Logan Greibill ◽  
Michel Lemullois ◽  
Mebarek Temagoult ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Plasma Membrane ◽  
Transition Zone ◽  
Basal Body ◽  
Mammalian Cells ◽  
Ternary Complex ◽  
Basal Bodies ◽  
Sequence Of Events ◽  
The Future ◽  
High Conservation

Cilia assembly starts with centriole to basal body maturation, migration to the cell surface and docking to the plasma membrane. The basal body docking process involves the interaction of both the distal end of the basal body and the transition fibers (or mature distal appendages), with the plasma membrane. During this process, the transition zone assembles and forms the structural junction between the basal body and the nascent cilium. Mutations in numerous genes involved in basal body docking and transition zone assembly are associated with the most severe ciliopathies, highlighting the importance of these events in cilium biogenesis. The conservation of this sequence of events across phyla is paralleled by a high conservation of the proteins involved. We identified CEP90 by BioID using FOPNL as a bait. Ultrastructure expansion microscopy showed that CEP90, FOPNL and OFD1 localized at the distal end of both centrioles/basal bodies in Paramecium and mammalian cells. These proteins are recruited early after duplication on the procentriole. Finally, functional analysis performed both in Paramecium and mammalian cells demonstrate the requirement of this complex for distal appendage assembly and basal body docking. Altogether, we propose that this ternary complex is required to determine the future position of distal appendages

scholarly journals Ciliogenesis in Caenorhabditis elegans requires genetic interactions between ciliary middle segment localized NPHP-2 (inversin) and transition zone-associated proteins

Development ◽  
2012 ◽  
Vol 139 (16) ◽  
pp. e1607-e1607
Author(s):  
S. R. F. Warburton-Pitt ◽  
A. R. Jauregui ◽  
C. Li ◽  
J. Wang ◽  
M. R. Leroux ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Transition Zone ◽  
Genetic Interactions ◽  
Middle Segment ◽  
Associated Proteins

scholarly journals Hook-length of the bacterial flagellum is optimized for maximal stability of the flagellar bundle

2018 ◽  
Author(s):  
Imke Spöring ◽  
Vincent A. Martinez ◽  
Christian Hotz ◽  
Jana Schwarz-Linek ◽  
Keara L. Grady ◽  
...  
Keyword(s):  
Basal Body ◽  
Swimming Speed ◽  
Self Assembly ◽  
Nanometer Scale ◽  
Hook Length ◽  
Optimal Length ◽  
Directed Movement ◽  
Bacterial Flagellum ◽  
Evolutionary Forces ◽  
Molecular Ruler

AbstractMost bacteria swim in liquid environments by rotating one or several flagella. The long external filament of the flagellum is connected to a membrane-embedded basal-body by a flexible universal joint, the hook, which allows the transmission of motor torque to the filament. The length of the hook is controlled on a nanometer-scale by a sophisticated molecular ruler mechanism. However, why its length is stringently controlled has remained elusive. We engineered and studied a diverse set of hook-length variants ofSalmonella enterica. Measurements of plate-assay motility, single-cell swimming speed and directional persistence in quasi 2D and population-averaged swimming speed and body angular velocity in 3D revealed that the motility performance is optimal around the wild type hook-length. We conclude that too short hooks may be too stiff to function as a junction and too long hooks may buckle and create instability in the flagellar bundle. Accordingly, peritrichously flagellated bacteria move most efficiently as the distance travelled per body rotation is maximal and body wobbling is minimized. Thus, our results suggest that the molecular ruler mechanism evolved to control flagellar hook growth to the optimal length consistent with efficient bundle formation. The hook-length control mechanism is therefore a prime example of how bacteria evolved elegant, but robust mechanisms to maximize their fitness under specific environmental constraints.Author summaryMany bacteria use flagella for directed movement in liquid environments. The flexible hook connects the membrane-embedded basal-body of the flagellum to the long, external filament. Flagellar function relies on self-assembly processes that define or self-limit the lengths of major parts. The length of the hook is precisely controlled on a nanometer-scale by a molecular ruler mechanism. However, the physiological benefit of tight hook-length control remains unclear. Here, we show that the molecular ruler mechanism evolved to control the optimal length of the flagellar hook, which is consistent with efficient motility performance. These results highlight the evolutionary forces that enable flagellated bacteria to optimize their fitness in diverse environments and might have important implications for the design of swimming micro-robots.

Role of DZIP1–CBY–FAM92 transition zone complex in the basal body to membrane attachment and ciliary budding

2020 ◽  
Vol 48 (3) ◽  
pp. 1067-1075
Author(s):  
Jean-André Lapart ◽  
Amélie Billon ◽  
Jean-Luc Duteyrat ◽  
Joëlle Thomas ◽  
Bénédicte Durand
Keyword(s):  
Transition Zone ◽  
Basal Body ◽  
Cell Types ◽  
Molecular Assembly ◽  
Bud Formation ◽  
Wide Range ◽  
Membrane Attachment ◽  
Functional Hierarchy ◽  
Complex Architecture ◽  
Different Cell Types

Cilia play important signaling or motile functions in various organisms. In Human, cilia dysfunctions are responsible for a wide range of diseases, called ciliopathies. Cilia assembly is a tightly controlled process, which starts with the conversion of the centriole into a basal body, leading to the formation of the ciliary bud that protrudes inside a ciliary vesicle and/or ultimately at the cell surface. Ciliary bud formation is associated with the assembly of the transition zone (TZ), a complex architecture of proteins of the ciliary base which plays critical functions in gating proteins in and out of the ciliary compartment. Many proteins are involved in the assembly of the TZ, which shows structural and functional variations in different cell types or organisms. In this review, we discuss how a particular complex, composed of members of the DZIP1, CBY and FAM92 families of proteins, is required for the initial stages of cilia assembly leading to ciliary bud formation and how their functional hierarchy contributes to TZ assembly. Moreover, we summarize how evidences in Drosophila reveal functional differences of the DZIP1–CBY–FAM92 complex in the different ciliated tissues of this organism. Whereas it is essential for proper TZ assembly in the two types of ciliated tissues, it is involved in stable anchoring of basal bodies to the plasma membrane in male germ cells. Overall, the DZIP1–CBY–FAM92 complex reveals a molecular assembly pathway required for the initial stages of ciliary bud formation and that is conserved from Drosophila to Human.

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