Proteomic Analysis of Isolated Chlamydomonas Centrioles Reveals Orthologs of Ciliary-Disease Genes

Keller, Lani C.; Romijn, Edwin P.; Zamora, Ivan; Yates, John R.; Marshall, Wallace F.

doi:10.1016/j.cub.2005.05.024

Cited by 300 publications

(280 citation statements)

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“…Mutations in the VFL1 gene encoding a basal body protein (Silflow et al, 2001) and in the VFL2 gene encoding centrin (Taillon et al, 1992) show the roles of these gene products in basal body positioning and segregation. Genomic and proteomic approaches have provided information on the protein composition of the flagella and basal bodies (Li et al, 2004;Keller et al, 2005;Pazour et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…The bld2 mutation in the gene encoding -tubulin (Dutcher et al, 2002) and the uni3 mutation in the gene encoding ␦-tubulin (Dutcher and Trabuco, 1998) (Silflow et al, 2001) and in the VFL2 gene encoding centrin (Taillon et al, 1992) show the roles of these gene products in basal body positioning and segregation. Genomic and proteomic approaches have provided information on the protein composition of the flagella and basal bodies (Li et al, 2004;Keller et al, 2005;Pazour et al, 2005). Genetic studies of basal body function in Chlamydomonas are supported by detailed ultrastructural characterization of the basal bodies and associated fibers (Ringo, 1967; CavalierSmith, 1974;O'Toole et al, 2003;Geimer and Melkonian, 2004).…”

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confidence: 99%

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The Uni2 Phosphoprotein is a Cell Cycle–regulated Component of the Basal Body Maturation Pathway inChlamydomonas reinhardtii

Piasecki

LaVoie

Tam

et al. 2008

MBoC

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Mutations in the UNI2 locus in Chlamydomonas reinhardtii result in a "uniflagellar" phenotype in which flagellar assembly occurs preferentially from the older basal body and ultrastructural defects reside in the transition zones. The UNI2 gene encodes a protein of 134 kDa that shares 20.5% homology with a human protein. Immunofluorescence microscopy localized the protein on both basal bodies and probasal bodies. The protein is present as at least two molecular-weight variants that can be converted to a single form with phosphatase treatment. Synthesis of Uni2 protein is induced during cell division cycles; accumulation of the phosphorylated form coincides with assembly of transition zones and flagella at the end of the division cycle. Using the Uni2 protein as a cell cycle marker of basal bodies, we observed migration of basal bodies before flagellar resorption in some cells, indicating that flagellar resorption is not required for mitotic progression. We observed the sequential assembly of new probasal bodies beginning at prophase. The uni2 mutants may be defective in the pathways leading to flagellar assembly and to basal body maturation. INTRODUCTIONCentrioles are evolutionarily ancient organelles, possibly extant in a common ancestor of all eukaryotic cells (CavalierSmith, 2002). They are required for the organization of interphase and mitotic microtubule arrays and as basal bodies they serve as templates for the growth of nine doublet microtubules in axonemes of cilia and flagella (for review see Marshall, 2007). Although flowering plants and more derived fungi have reduced or eliminated centrioles and cilia, metazoans have diversified their functions in numerous sensory and developmental processes (for reviews see Singla and Reiter, 2006;Dawe et al., 2007). Several mammalian genetic disorders have been linked to defects in centrioles or cilia (for review see Afzelius, 2004;Pan et al., 2005). For example, the proteins associated with Bardet-Biedl syndrome, a debilitating pleiotropic human disorder characterized by obesity, renal abnormalities, polydactyly, retinal degeneration, and genitourinary tract malformations have been shown to localize to or around centrioles and cilia (for review see Beales, 2005;Blacque and Leroux, 2006).Centrioles in actively dividing cells show conservative replication and semiconservative segregation during division (for review see Dawe et al., 2007). As a result, each pair of centrioles consists of an older and a younger centriole that differ in age by at least one cell generation. The "mother" centriole differs both in structure and function from the "daughter" centriole. For example, in the single pair of centrioles found in most types of mammalian cells, the mother centriole nucleates the growth of the primary cilium and contains proteins not present in the daughter centriole. The daughter centriole becomes competent for ciliary assembly only in the ensuing cell cycle (for review see Bornens, 2002). Extension of the pathway for sequential maturation of basal bodies has been ...

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

The Uni2 Phosphoprotein is a Cell Cycle–regulated Component of the Basal Body Maturation Pathway inChlamydomonas reinhardtii

Piasecki

LaVoie

Tam

et al. 2008

MBoC

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“…Centrioles, in their capacity as basal bodies, nucleate the extension of their A-and Btubules to become ciliary/flagellar doublet microtubules, with the centriolar C-tubules remaining quiescent. The wide-ranging and essential functions of these organelles help to explain the prevalence of the many varied diseases and developmental disorders that arise from mutations in ciliary, flagellar and centriolar genes [Afzelius, 2004;Eley et al, 2005;Keller et al, 2005;Pazour et al, 2005]. Several recent studies have now highlighted the importance of the underlying arrangement and composition of the microtubule protofilaments (PFs) and their associated proteins in ciliary/flagellar assembly and their motile/sensory functions [Marshall and Nonaka, 2006 -for review;Rupp and Porter, 2003;Nicastro et al, 2006;Ralston and Hill, 2006;Setter et al, 2006;Sui and Downing, 2006;Wirschell et al, in press].…”

Section: Introductionmentioning

confidence: 99%

Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules

Linck

Stephens

2007

Cell Motil. Cytoskeleton

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“…A recent report suggested that JME may be caused by mutations in the EFHC1 gene [Suzuki et al, 2004]. Here I will discuss the evidence supporting a role for Efhc1 in JME and detail recent analyses [Ikeda et al, 2005] that demonstrate that this protein is the mammalian orthologue of Chlamydomonas Rib72 and as such is likely an integral axonemal component [Patel-King et al, 2002;Ikeda et al, 2003] located within the protofilament ribbons [Ikeda et al, 2003] and, potentially, is also present in basal bodies/centrioles [Hinchcliffe and Linck, 1998;Keller et al, 2005]. These studies have raised the exciting possibility that alterations in ciliary function due to mutations in Efhc1/Rib72 provide the underlying basis for this inherited neural disorder.…”

Section: Introductionmentioning

confidence: 99%

“…1a). Although no staining was observed in the basal body region using an anti-Rib72 antibody [Ikeda et al, 2003], recent proteomic studies suggest that this protein may be a component of the Chlamydomonas basal body/centriole [Keller et al, 2005].…”

Section: Introductionmentioning

confidence: 99%

Axonemal protofilament ribbons, DM10 domains, and the link to juvenile myoclonic epilepsy

King

2006

Cell Motil. Cytoskeleton

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Juvenile myoclonic epilepsy (JME) is a common neurological disorder that results in short uncontrolled muscle contractions and sometimes more severe seizures. Genetic studies have suggested that JME may be caused by mutations in EFHC1. The Efhc1 protein consists of three DM10 domains and a C-terminal region containing a potential Ca 2þ -binding motif. In Chlamydomonas, a protein (Rib72) of almost identical domain structure is a component of the protofilament ribbons within the doublet microtubules of the flagellar axoneme. Here I discuss recent work that supports assignment of human Efhc1 as a ciliary component and the resulting implications for the mechanism of disease causation. Cell Motil.

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Proteomic Analysis of Isolated Chlamydomonas Centrioles Reveals Orthologs of Ciliary-Disease Genes

Abstract: By analyzing isolated Chlamydomonas basal bodies, we have been able to obtain the first reported proteomic analysis of the centriole.

Cited by 300 publications

References 43 publications

The Uni2 Phosphoprotein is a Cell Cycle–regulated Component of the Basal Body Maturation Pathway inChlamydomonas reinhardtii

The Uni2 Phosphoprotein is a Cell Cycle–regulated Component of the Basal Body Maturation Pathway inChlamydomonas reinhardtii

Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules

Axonemal protofilament ribbons, DM10 domains, and the link to juvenile myoclonic epilepsy

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