Centrin is essential for the activity of the ciliary reversal-coupled voltage-gated Ca2+ channels

Gonda, Kohsuke; Yoshida, Akiko; Oami, Kazunori; Takahashi, Mihoko

doi:10.1016/j.bbrc.2004.08.172

Cited by 33 publications

(29 citation statements)

References 37 publications

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“…Intraflagellar transport (IFT) is required for the assembly and maintenance of flagella and involves the transport of non-membrane-bound macromolecular protein complexes (IFT particles) from the cell body to the tip of the flagellum and back (reviewed in references 56 and 66). Interestingly, centrin is known as a light chain associated with one type of inner dynein arm in axonemes of C. reinhardtii (33,52) and has been implicated in different ciliary functions (14,15). Here, we have shown specific centrin labeling of outer axonemal doublets consistent with the biochemical evidence.…”

Section: Discussionsupporting

confidence: 88%

“…(3,50,69). More recently, novel centrin functions have been discovered such as involvement in recombinational DNA repair through modulation of the nucleotide excision repair pathway in humans and plants (2,47), a role in the nuclear mRNA export machinery in yeast (11), regulation of calcium-dependent ciliary activities in ciliates (14,15), and signal transduction in vertebrate photoreceptors (53). How centrin exerts these different functions at the molecular level is, however, still unknown although considerable progress has recently been made through in vitro studies of centrin and its interaction with target peptides (8,19,20,40,75).…”

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confidence: 99%

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Centrin Scaffold in Chlamydomonas reinhardtii Revealed by Immunoelectron Microscopy

Geimer

Melkonian

2005

Eukaryot Cell

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In the flagellate green alga Chlamydomonas reinhardtii the Ca 2؉ -binding EF-hand protein centrin is encoded by a single-copy gene. Previous studies have localized the protein to four distinct structures in the flagellar apparatus: the nucleus-basal body connector, the distal connecting fiber, the flagellar transitional region, and the axoneme. To explain the disjunctive distribution of centrin, the interaction of centrin with as yet unknown specific centrin-binding proteins has been implied. Here, we demonstrate using serial section postembedding immunoelectron microscopy of isolated cytoskeletons that centrin is located in additional structures (transitional fibers and basal body lumen) and that the centrin-containing structures of the basal apparatus are likely part of a continuous filamentous scaffold that extends from the nucleus to the flagellar bases. In addition, we show that centrin is located in the distal lumen of the basal body in a rotationally asymmetric structure, the V-shaped filament system. This novel centrin-containing structure has also been detected near the distal end of the probasal bodies. Taken together, these results suggest a role for a rotationally asymmetric centrin "seed" in the growth and development of the centrin scaffold following replication of the basal apparatus.Centrin (also known as caltractin) is a member of the highly conserved superfamily of calcium-binding EF-hand proteins and occurs in all eukaryotic cells, being mostly associated with centrosomes (58, 64). It was first discovered in flagellate green algae, where it is located in the basal apparatus (the part of the cytoskeleton anchoring the flagella) and involved in the contraction of calcium-sensitive filaments (42, 60) which, in general, play an important role in the dynamic behavior of centrosomes by controlling the position and orientation of centrosomal structures (58, 64). Analysis of centrin mutants and RNA interference strains deficient in centrin in the green algal model system Chlamydomonas reinhardtii suggested that centrin is essential for basal body duplication and segregation during cell division (28,39,73), functions also deduced for centrin homologues in vertebrates (46, 62) and yeast spp. (3,50,69). More recently, novel centrin functions have been discovered such as involvement in recombinational DNA repair through modulation of the nucleotide excision repair pathway in humans and plants (2, 47), a role in the nuclear mRNA export machinery in yeast (11), regulation of calcium-dependent ciliary activities in ciliates (14, 15), and signal transduction in vertebrate photoreceptors (53). How centrin exerts these different functions at the molecular level is, however, still unknown although considerable progress has recently been made through in vitro studies of centrin and its interaction with target peptides (8,19,20,40,75).In some organisms, the functional diversity of centrin may be related to the presence of different centrin isotypes, e.g., four centrin proteins (centrin1p to centrin4p), which are d...

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Section: Discussionsupporting

confidence: 88%

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confidence: 99%

Centrin Scaffold in Chlamydomonas reinhardtii Revealed by Immunoelectron Microscopy

Geimer

Melkonian

2005

Eukaryot Cell

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“…Several further discrete localisations have also been identified, in cilia (Gonda et al, 2004;Guerra et al, 2003;LeDizet and Piperno, 1995) and ciliary-derived organelles of sensory cells (Giessl et al, 2006), at the contractile vacuole pores in Tetrahymena (Stemm-Wolf et al, 2005) and at the Golgi in Trypanosoma (He et al, 2005;Selvapandiyan et al, 2007). Interestingly, if species differ widely in their number of centrin genes (one in yeast, four in mammals, seven in Leishmania, at least ten in Tetrahymena and 49 in Paramecium), when more than a single gene is present, a particular localisation or function may involve either a single or different centrin isotypes and conversely, a particular isotype may show different localisations or functions.…”

Section: +mentioning

confidence: 88%

“…In view of the diverse cellular functions of centrins, it can be envisaged that isotype diversification is favoured in unicellular organisms. Paramecium possesses 48 centrins, four are basal body specific (Ruiz et al, 2005), two are orthologues of P. caudatum centrins involved in a ciliary Ca 2+ channel (Gonda et al, 2004), 35 are found in the ICL and seven have no known function. However, on the basis of their sequence identity, the 35 ICL centrin genes belong to ten subfamilies.…”

Section: Molecular Diversity and Icl Biogenesismentioning

confidence: 99%

Functional diversification of centrins and cell morphological complexity

Gogendeau

Klotz

Arnaiz

et al. 2008

Journal of Cell Science

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In addition to their key role in the duplication of microtubule organising centres (MTOCs), centrins are major constituents of diverse MTOC-associated contractile arrays. A centrin partner, Sfi1p, has been characterised in yeast as a large protein carrying multiple centrin-binding sites, suggesting a model for centrin-mediated Ca2+-induced contractility and for the duplication of MTOCs. In vivo validation of this model has been obtained in Paramecium, which possesses an extended contractile array – the infraciliary lattice (ICL) – essentially composed of centrins and a huge Sfi1p-like protein, PtCenBP1p, which is essential for ICL assembly and contractility. The high molecular diversity revealed here by the proteomic analysis of the ICL, including ten subfamilies of centrins and two subfamilies of Sf1p-like proteins, led us to address the question of the functional redundancy, either between the centrin-binding proteins or between the centrin subfamilies. We show that all are essential for ICL biogenesis. The two centrin-binding protein subfamilies and nine of the centrin subfamilies are ICL specific and play a role in its molecular and supramolecular architecture. The tenth and most conserved centrin subfamily is present at three cortical locations (ICL, basal bodies and contractile vacuole pores) and might play a role in coordinating duplication and positioning of cortical organelles.

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“…24 Therefore, most visible event with involvement of calcium signaling in Paramecium species is ciliary reversal which depends on the intracellular increase in Ca 2C concentration. 25 It has long been known that members of Paramecium species including P. bursaria exhibit galvanotaxis, a directed swimming of cells toward the electrode, induced in response to an applied voltage.…”

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confidence: 99%