Bld10p, a novel protein essential for basal body assembly in <i>Chlamydomonas </i>

Matsuura, Kazuki; Lefebvre, Paul; Kamiya, Ritsu; Hirono, Masafumi

doi:10.1083/jcb.200402022

Cited by 132 publications

(88 citation statements)

References 41 publications

(38 reference statements)

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“…It is also remarkable that Cep135 is much more abundant at purified centrosomes than either STIL or Sas‐6 (Fig 2C). Although this result may appear surprising when considering the striking association of the Cep135 homolog Bld10 with the centriolar cartwheel in Chlamydomonas (Matsuura et al , 2004; Hiraki et al , 2007), it falls in line with the observation that the bulk of human Cep135 associates with the proximal ends of mother centrioles rather than the cartwheels of daughter centrioles (Sonnen et al , 2012). Finally, and most interestingly, our data predict that Sas‐6 is about twice as abundant as STIL.…”

Section: Resultsmentioning

confidence: 86%

Quantitative analysis of human centrosome architecture by targeted proteomics and fluorescence imaging

et al. 2016

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Centrioles are essential for the formation of centrosomes and cilia. While numerical and/or structural centrosomes aberrations are implicated in cancer, mutations in centriolar and centrosomal proteins are genetically linked to ciliopathies, microcephaly, and dwarfism. The evolutionarily conserved mechanisms underlying centrosome biogenesis are centered on a set of key proteins, including Plk4, Sas‐6, and STIL, whose exact levels are critical to ensure accurate reproduction of centrioles during cell cycle progression. However, neither the intracellular levels of centrosomal proteins nor their stoichiometry within centrosomes is presently known. Here, we have used two complementary approaches, targeted proteomics and EGFP‐tagging of centrosomal proteins at endogenous loci, to measure protein abundance in cultured human cells and purified centrosomes. Our results provide a first assessment of the absolute and relative amounts of major components of the human centrosome. Specifically, they predict that human centriolar cartwheels comprise up to 16 stacked hubs and 1 molecule of STIL for every dimer of Sas‐6. This type of quantitative information will help guide future studies of the molecular basis of centrosome assembly and function.

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Section: Resultsmentioning

confidence: 86%

Quantitative analysis of human centrosome architecture by targeted proteomics and fluorescence imaging

et al. 2016

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“…Cep135 is a microcephaly associated (MCPH8), cartwheel protein that promotes centriole assembly and stability [9, 13, 15–19]. The protein contains a coiled-coil domain and conserved regions near the N-terminus and the C-terminus, respectively (Figure 1A).…”

Section: Resultsmentioning

confidence: 99%

A Short CEP135 Splice Isoform Controls Centriole Duplication

et al. 2015

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Summary Centriole duplication is coordinated such that a single round of duplication occurs during each cell cycle. Disruption of this synchrony causes defects including supernumerary centrosomes in cancer and perturbed ciliary signaling [1–5]. To preserve the normal number of centrioles, the level, localization, and post-translational modification of centriole proteins is regulated so that when centriole protein expression and/or activity is increased, centrioles self-assemble. Assembly is initiated by the formation of the cartwheel structure that comprises the base of centrioles [6–11]. SAS-6 constitutes the cartwheel and SAS-6 levels remain low until centriole assembly is initiated at S-phase onset [3, 12, 13]. Cep135 physically links to SAS-6 near the site of microtubule nucleation and binds to CPAP for triplet microtubule formation [13, 14]. We identify two distinct protein isoforms of Cep135 that antagonize each other to modulate centriole duplication: full length Cep135 (Cep135full) promotes new assembly while a short isoform, Cep135mini, represses it. Cep135mini represses centriole duplication by limiting the centriolar localization of Cep135full binding proteins (SAS-6 and CPAP) and the pericentriolar localization of γ-tubulin. The Cep135 isoforms exhibit distinct and complementary centrosomal localization during the cell cycle. Cep135mini protein decreases from centrosomes upon anaphase onset. We suggest that the decrease in Cep135mini from centrosomes promotes centriole assembly. The repression of centriole duplication by a splice isoform of a protein that normally promotes it serves as a novel mechanism to limit centriole duplication.

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“…The centriolar components SAS-4/CPAP, SAS-6 and BLD10/Cep135 belong to a universal module of functionally conserved proteins involved in the early steps of centrosome/basal body assembly and establishment of their nine-fold symmetry (Salisbury, 2003; Matsuura et al, 2004; Nakazawa et al, 2007; Culver et al, 2009; Carvalho-Santos et al, 2010). We confirmed the presence of a Giardia SAS-4 homolog (Hodges et al, 2010) and identified a SAS-6 but not a BLD-10 homolog.…”

Section: Resultsmentioning

confidence: 99%

Mining the Giardia genome and proteome for conserved and unique basal body proteins

Lauwaet

Smith

Reiner

et al. 2011

International Journal for Parasitology

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Giardia lamblia is a flagellated protozoan parasite and a major cause of diarrhea in humans. Its microtubular cytoskeleton mediates trophozoite motility, attachment and cytokinesis, and is characterized by an attachment disk and eight flagella that are each nucleated in a basal body. To date, only 10 giardial basal body proteins have been identified, including universal signaling proteins that are important for regulating mitosis or differentiation. In this study, we have exploited bioinformatics and proteomic approaches to identify new Giardia basal body proteins and confocal microscopy to confirm their localization in interphase trophozoites. This approach identified 75 homologs of conserved basal body proteins in the genome including 65 not previously known to be associated with Giardia basal bodies. Thirteen proteins were confirmed to co-localize with centrin to the Giardia basal bodies. We also demonstrate that most basal body proteins localize to additional cytoskeletal structures in interphase trophozoites. This might help to explain the roles of the four pairs of flagella and Giardia-specific organelles in motility and differentiation. A deeper understanding of the composition of the Giardia basal bodies will contribute insights into the complex signaling pathways that regulate its unique cytoskeleton and the biological divergence of these conserved organelles.

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Bld10p, a novel protein essential for basal body assembly in Chlamydomonas

Cited by 132 publications

References 41 publications

Quantitative analysis of human centrosome architecture by targeted proteomics and fluorescence imaging

Quantitative analysis of human centrosome architecture by targeted proteomics and fluorescence imaging

A Short CEP135 Splice Isoform Controls Centriole Duplication

Mining the Giardia genome and proteome for conserved and unique basal body proteins

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