2
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Pericentrin-mediated SAS-6 recruitment promotes centriole assembly

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The centrosome is composed of two centrioles surrounded by a microtubule-nucleating pericentriolar material (PCM). Although centrioles are known to regulate PCM assembly, it is less known whether and how the PCM contributes to centriole assembly. Here we investigate the interaction between centriole components and the PCM by taking advantage of fission yeast, which has a centriole-free, PCM-containing centrosome, the SPB. Surprisingly, we observed that several ectopically-expressed animal centriole components such as SAS-6 are recruited to the SPB. We revealed that a conserved PCM component, Pcp1/pericentrin, interacts with and recruits SAS-6. This interaction is conserved and important for centriole assembly, particularly its elongation. We further explored how yeasts kept this interaction even after centriole loss and showed that the conserved calmodulin-binding region of Pcp1/pericentrin is critical for SAS-6 interaction. Our work suggests that the PCM not only recruits and concentrates microtubule-nucleators, but also the centriole assembly machinery, promoting biogenesis close by.

          Related collections

          Most cited references106

          • Record: found
          • Abstract: found
          • Article: found
          Is Open Access

          HMMER web server: 2015 update

          The HMMER website, available at http://www.ebi.ac.uk/Tools/hmmer/, provides access to the protein homology search algorithms found in the HMMER software suite. Since the first release of the website in 2011, the search repertoire has been expanded to include the iterative search algorithm, jackhmmer. The continued growth of the target sequence databases means that traditional tabular representations of significant sequence hits can be overwhelming to the user. Consequently, additional ways of presenting homology search results have been developed, allowing them to be summarised according to taxonomic distribution or domain architecture. The taxonomy and domain architecture representations can be used in combination to filter the results according to the needs of a user. Searches can also be restricted prior to submission using a new taxonomic filter, which not only ensures that the results are specific to the requested taxonomic group, but also improves search performance. The repertoire of profile hidden Markov model libraries, which are used for annotation of query sequences with protein families and domains, has been expanded to include the libraries from CATH-Gene3D, PIRSF, Superfamily and TIGRFAMs. Finally, we discuss the relocation of the HMMER webserver to the European Bioinformatics Institute and the potential impact that this will have.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Estimating the timing of early eukaryotic diversification with multigene molecular clocks.

            Although macroscopic plants, animals, and fungi are the most familiar eukaryotes, the bulk of eukaryotic diversity is microbial. Elucidating the timing of diversification among the more than 70 lineages is key to understanding the evolution of eukaryotes. Here, we use taxon-rich multigene data combined with diverse fossils and a relaxed molecular clock framework to estimate the timing of the last common ancestor of extant eukaryotes and the divergence of major clades. Overall, these analyses suggest that the last common ancestor lived between 1866 and 1679 Ma, consistent with the earliest microfossils interpreted with confidence as eukaryotic. During this interval, the Earth's surface differed markedly from today; for example, the oceans were incompletely ventilated, with ferruginous and, after about 1800 Ma, sulfidic water masses commonly lying beneath moderately oxygenated surface waters. Our time estimates also indicate that the major clades of eukaryotes diverged before 1000 Ma, with most or all probably diverging before 1200 Ma. Fossils, however, suggest that diversity within major extant clades expanded later, beginning about 800 Ma, when the oceans began their transition to a more modern chemical state. In combination, paleontological and molecular approaches indicate that long stems preceded diversification in the major eukaryotic lineages.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              SAK/PLK4 is required for centriole duplication and flagella development.

              SAK/PLK4 is a distinct member of the polo-like kinase family. SAK-/- mice die during embryogenesis, whereas SAK+/- mice develop liver and lung tumors and SAK+/- MEFs show mitotic abnormalities. However, the mechanism underlying these phenotypes is still not known. Here, we show that downregulation of SAK in Drosophila cells, by mutation or RNAi, leads to loss of centrioles, the core structures of centrosomes. Such cells are able to undergo repeated rounds of cell division, but display broad disorganized mitotic spindle poles. We also show that SAK mutants lose their centrioles during the mitotic divisions preceding male meiosis but still produce cysts of 16 primary spermatocytes as in the wild-type. Mathematical modeling of the stereotyped cell divisions of spermatogenesis can account for such loss by defective centriole duplication. The majority of spermatids in SAK mutants lack centrioles and so are unable to make sperm axonemes. Finally, we show that depletion of SAK in human cells also prevents centriole duplication and gives rise to mitotic abnormalities. SAK/PLK4 is necessary for centriole duplication both in Drosophila and human cells. Drosophila cells tolerate the lack of centrioles and undertake mitosis but cannot form basal bodies and hence flagella. Human cells depleted of SAK show error-prone mitosis, likely to underlie its tumor-suppressor role.
                Bookmark

                Author and article information

                Contributors
                Role: Reviewing Editor
                Role: Senior Editor
                Journal
                eLife
                Elife
                eLife
                eLife
                eLife Sciences Publications, Ltd
                2050-084X
                11 June 2019
                2019
                : 8
                : e41418
                Affiliations
                [1 ]Instituto Gulbenkian de Ciência OeirasPortugal
                [2 ]deptOphiomics Precision Medicine LisboaPortugal
                [3 ]Institute for Research on Cancer and Aging of Nice (IRCAN), INSERM U1081 UMR7284 CNRS NiceFrance
                Max Planck Institute of Molecular Cell Biology and Genetics Germany
                Utrecht University Netherlands
                Max Planck Institute of Molecular Cell Biology and Genetics Germany
                Author notes
                [‡]

                Champalimaud Centre for the Unknown, Lisbon, Portugal.

                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0002-6759-0901
                https://orcid.org/0000-0002-8311-3849
                https://orcid.org/0000-0002-8363-7183
                https://orcid.org/0000-0003-1987-5598
                Article
                41418
                10.7554/eLife.41418
                6559791
                31182187
                a2b0f2f8-2b5b-46eb-b094-8bd721033180
                © 2019, Ito et al

                This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

                History
                : 29 August 2018
                : 14 May 2019
                Funding
                Funded by: FundRef http://dx.doi.org/10.13039/501100000854, Human Frontier Science Program;
                Award ID: LT000344/2013
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/100008732, Uehara Memorial Foundation;
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/501100001871, Fundação para a Ciência e a Tecnologia;
                Award ID: 195/BPD/17
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/501100001871, Fundação para a Ciência e a Tecnologia;
                Award ID: SFRH/BPD/87479/2012
                Award Recipient :
                Funded by: Fundação para a Ciência e a Tecnologia;
                Award ID: PTDC/BIM-ONC/6858/2014
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/501100000781, European Research Council;
                Award ID: CoG683528
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/501100000348, Calouste Gulbenkian Foundation;
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/501100001871, Fundação para a Ciência e a Tecnologia;
                Award ID: FCT Investigator Grant
                Award Recipient :
                The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
                Categories
                Research Article
                Cell Biology
                Custom metadata
                Newly discovered interaction between fission yeast SPB and animal centriole components reveals that pericentrin not only functions as a microtubule-nucleator, but also promotes centriole assembly in animals.

                Life sciences
                centrosome,centriole,pericentrin,sas-6,spb,evolution,d. melanogaster,s. pombe
                Life sciences
                centrosome, centriole, pericentrin, sas-6, spb, evolution, d. melanogaster, s. pombe

                Comments

                Comment on this article