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1.
Nat Commun ; 15(1): 2687, 2024 Mar 27.
Artigo em Inglês | MEDLINE | ID: mdl-38538594

RESUMO

Centrosomes and cilia are microtubule-based superstructures vital for cell division, signaling, and motility. The once thought hollow lumen of their microtubule core structures was recently found to hold a rich meshwork of microtubule inner proteins (MIPs). To address the outstanding question of how distinct MIPs evolved to recognize microtubule inner surfaces, we applied computational sequence analyses, structure predictions, and experimental validation to uncover evolutionarily conserved microtubule- and MIP-binding modules named NWE, SNYG, and ELLEn, and PYG and GFG-repeat by their signature motifs. These modules intermix with MT-binding DM10-modules and Mn-repeats in 24 Chlamydomonas and 33 human proteins. The modules molecular characteristics provided keys to identify elusive cross-species homologs, hitherto unknown human MIP candidates, and functional properties for seven protein subfamilies, including the microtubule seam-binding NWE and ELLEn families. Our work defines structural innovations that underpin centriole and axoneme assembly and demonstrates that MIPs co-evolved with centrosomes and cilia.


Assuntos
Cílios , Proteínas dos Microtúbulos , Humanos , Cílios/metabolismo , Proteínas dos Microtúbulos/metabolismo , Axonema/metabolismo , Microtúbulos/metabolismo , Centríolos/metabolismo
2.
Cell Rep ; 43(2): 113713, 2024 Feb 27.
Artigo em Inglês | MEDLINE | ID: mdl-38306274

RESUMO

R2TP is a chaperone complex consisting of the AAA+ ATPases RUVBL1 and RUVBL2, as well as RPAP3 and PIH1D1 proteins. R2TP is responsible for the assembly of macromolecular complexes mainly acting through different adaptors. Using proximity-labeling mass spectrometry, we identified deleted in primary ciliary dyskinesia (DPCD) as an adaptor of R2TP. Here, we demonstrate that R2TP-DPCD influences ciliogenesis initiation through a unique mechanism by interaction with Akt kinase to regulate its phosphorylation levels rather than its stability. We further show that DPCD is a heart-shaped monomeric protein with two domains. A highly conserved region in the cysteine- and histidine-rich domains-containing proteins and SGT1 (CS) domain of DPCD interacts with the RUVBL2 DII domain with high affinity to form a stable R2TP-DPCD complex both in cellulo and in vitro. Considering that DPCD is one among several CS-domain-containing proteins found to associate with RUVBL1/2, we propose that RUVBL1/2 are CS-domain-binding proteins that regulate complex assembly and downstream signaling.


Assuntos
Proteínas Proto-Oncogênicas c-akt , Transdução de Sinais , Fosforilação , ATPases Associadas a Diversas Atividades Celulares , Cognição
3.
Methods Mol Biol ; 2725: 121-129, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-37856021

RESUMO

Volume electron microscopy technologies such as serial block face scanning electron microscopy (SBF-SEM) allow the characterization of tissue organization and cellular content in three dimensions at nanoscale resolution. Here, we describe the procedure to process and image an air-liquid interface culture of human or mouse airway epithelial cells for visualization of the multiciliated epithelium by SBF-SEM in vertical or horizontal cross section.


Assuntos
Imageamento Tridimensional , Microscopia Eletrônica de Volume , Animais , Humanos , Camundongos , Imageamento Tridimensional/métodos , Microscopia Eletrônica de Varredura , Epitélio , Células Epiteliais
4.
Methods Mol Biol ; 2725: 131-146, 2024.
Artigo em Inglês | MEDLINE | ID: mdl-37856022

RESUMO

Volume electron microscopy (vEM) is a high-resolution imaging technique capable of revealing the 3D structure of cells, tissues, and model organisms. This imaging modality is gaining prominence due to its ability to provide a comprehensive view of cells at the nanometer scale. The visualization and quantitative analysis of individual subcellular structures however requires segmentation of each 2D electron micrograph slice of the 3D vEM dataset; this process is extremely laborious de facto limiting its applications and throughput. To address these limitations, deep learning approaches have been recently developed including Empanada-Napari plugin, an open-source tool for automated segmentation based on a Panoptic-DeepLab (PDL) architecture. In this chapter, we provide a step-by-step protocol describing the process of manual segmentation using 3dMOD within the IMOD package and the process of automated segmentation using Empanada-Napari plugins for the 3D reconstruction of airway cellular structures.


Assuntos
Imageamento Tridimensional , Microscopia Eletrônica de Volume , Imageamento Tridimensional/métodos , Aprendizado de Máquina , Tórax , Processamento de Imagem Assistida por Computador/métodos
5.
Methods Mol Biol ; 2440: 305-326, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35218547

RESUMO

The structural organization of macromolecules and their association in assemblies and organelles is key to understand cellular function. Super-resolution fluorescence microscopy has expanded our toolbox for examining such nanometer-scale cellular structures, by enabling positional mapping of proteins in situ. Here, we detail the workflow to build nanometer-scale maps focusing on two complementary super-resolution modalities: structured illumination microscopy (SIM) and stochastic optical reconstruction microscopy (STORM).


Assuntos
Organelas , Substâncias Macromoleculares , Microscopia de Fluorescência
6.
Am J Respir Crit Care Med ; 205(7): 761-768, 2022 04 01.
Artigo em Inglês | MEDLINE | ID: mdl-35023825

RESUMO

Rationale: Mucin homeostasis is fundamental to airway health. Upregulation of airway mucus glycoprotein MUC5B is observed in diverse common lung diseases and represents a potential therapeutic target. In mice, Muc5b is required for mucociliary clearance and for controlling inflammation after microbial exposure. The consequences of its loss in humans are unclear. Objectives: The goal of this study was to identify and characterize a family with congenital absence of MUC5B protein. Methods: We performed whole-genome sequencing in an adult proband with unexplained bronchiectasis, impaired pulmonary function, and repeated Staphylococcus aureus infection. Deep phenotyping over a 12-year period included assessments of pulmonary radioaerosol mucociliary clearance. Genotyping with reverse phenotyping was organized for eight family members. Extensive experiments, including immunofluorescence staining and mass spectrometry for mucins, were performed across accessible sample types. Measurements and Main Results: The proband, and her symptomatic sibling who also had extensive sinus disease with nasal polyps, were homozygous for a novel splicing variant in the MUC5B gene (NM_002458.2: c.1938 + 1G>A). MUC5B was absent from saliva, sputum, and nasal samples. Mucociliary clearance was impaired in the proband, and large numbers of apoptotic macrophages were present in sputum. Three siblings heterozygous for the familial MUC5B variant were asymptomatic but had a shared pattern of mild lung function impairments. Conclusions: Congenital absence of MUC5B defines a new category of genetic respiratory disease. The human phenotype is highly concordant with that of the Muc5b-/- murine model. Further study of individuals with decreased MUC5B production could provide unique mechanistic insights into airway mucus biology.


Assuntos
Pneumopatias , Mucinas , Adulto , Animais , Feminino , Humanos , Pulmão/metabolismo , Pneumopatias/metabolismo , Camundongos , Mucina-5AC/genética , Mucina-5B/genética , Mucinas/metabolismo , Depuração Mucociliar/genética , Muco/metabolismo
7.
BMC Med Genomics ; 14(1): 234, 2021 09 23.
Artigo em Inglês | MEDLINE | ID: mdl-34556108

RESUMO

BACKGROUND: It is estimated that 1-13% of cases of bronchiectasis in adults globally are attributable to primary ciliary dyskinesia (PCD) but many adult patients with bronchiectasis have not been investigated for PCD. PCD is a disorder caused by mutations in genes required for motile cilium structure or function, resulting in impaired mucociliary clearance. Symptoms appear in infancy but diagnosis is often late or missed, often due to the lack of a "gold standard" diagnostic tool and non-specific symptoms. Mutations in > 50 genes account for around 70% of cases, with additional genes, and non-coding, synonymous, missense changes or structural variants (SVs) in known genes presumed to account for the missing heritability. METHODS: UK patients with no identified genetic confirmation for the cause of their PCD or bronchiectasis were eligible for whole genome sequencing (WGS) in the Genomics England Ltd 100,000 Genomes Project. 21 PCD probands and 52 non-cystic fibrosis (CF) bronchiectasis probands were recruited in Wessex Genome Medicine Centre (GMC). We carried out analysis of single nucleotide variants (SNVs) and SVs in all families recruited in Wessex GMC. RESULTS: 16/21 probands in the PCD cohort received confirmed (n = 9), probable (n = 4) or possible (n = 3) diagnosis from WGS, although 13/16 of these could have been picked up by current standard of care gene panel testing. In the other cases, SVs were identified which were missed by panel testing. We identified variants in novel PCD candidate genes (IFT140 and PLK4) in 2 probands in the PCD cohort. 3/52 probands in the non-CF bronchiectasis cohort received a confirmed (n = 2) or possible (n = 1) diagnosis of PCD. We identified variants in novel PCD candidate genes (CFAP53 and CEP164) in 2 further probands in the non-CF bronchiectasis cohort. CONCLUSIONS: Genetic testing is an important component of diagnosing PCD, especially in cases of atypical disease history. WGS is effective in cases where prior gene panel testing has found no variants or only heterozygous variants. In these cases it may detect SVs and is a powerful tool for novel gene discovery.


Assuntos
Transtornos da Motilidade Ciliar
8.
Nat Genet ; 53(2): 205-214, 2021 02.
Artigo em Inglês | MEDLINE | ID: mdl-33432184

RESUMO

Angiotensin-converting enzyme 2 (ACE2) is the main entry point in airway epithelial cells for SARS-CoV-2. ACE2 binding to the SARS-CoV-2 protein spike triggers viral fusion with the cell plasma membrane, resulting in viral RNA genome delivery into the host. Despite ACE2's critical role in SARS-CoV-2 infection, full understanding of ACE2 expression, including in response to viral infection, remains unclear. ACE2 was thought to encode five transcripts and one protein of 805 amino acids. In the present study, we identify a novel short isoform of ACE2 expressed in the airway epithelium, the main site of SARS-CoV-2 infection. Short ACE2 is substantially upregulated in response to interferon stimulation and rhinovirus infection, but not SARS-CoV-2 infection. This short isoform lacks SARS-CoV-2 spike high-affinity binding sites and, altogether, our data are consistent with a model where short ACE2 is unlikely to directly contribute to host susceptibility to SARS-CoV-2 infection.


Assuntos
Enzima de Conversão de Angiotensina 2/genética , COVID-19/genética , Células Epiteliais/metabolismo , Animais , Sítios de Ligação , Células Cultivadas , Chlorocebus aethiops , Éxons , Células HEK293 , Humanos , Interferons/imunologia , Ligação Proteica , Isoformas de Proteínas/genética , Sítios de Splice de RNA , RNA-Seq , Sistema Respiratório/citologia , Glicoproteína da Espícula de Coronavírus/metabolismo , Transcriptoma , Regulação para Cima , Células Vero
9.
Dev Cell ; 55(2): 224-236.e6, 2020 10 26.
Artigo em Inglês | MEDLINE | ID: mdl-33038333

RESUMO

Motile cilia are cellular beating machines that play a critical role in mucociliary clearance, cerebrospinal fluid movement, and fertility. In the airways, hundreds of motile cilia present on the surface of a multiciliated epithelia cell beat coordinately to protect the epithelium from bacteria, viruses, and harmful particulates. During multiciliated cell differentiation, motile cilia are templated from basal bodies, each extending a basal foot-an appendage linking motile cilia together to ensure coordinated beating. Here, we demonstrate that among the many motile cilia of a multiciliated cell, a hybrid cilium with structural features of both primary and motile cilia is harbored. The hybrid cilium is conserved in mammalian multiciliated cells, originates from parental centrioles, and its cellular position is biased and dependent on ciliary beating. Furthermore, we show that the hybrid cilium emerges independently of other motile cilia and functions in regulating basal body alignment.


Assuntos
Corpos Basais/patologia , Diferenciação Celular/fisiologia , Centríolos/patologia , Cílios/patologia , Células Cultivadas , Centríolos/fisiologia , Cílios/fisiologia , Células Epiteliais/patologia , Epitélio/patologia , Humanos , Microscopia/métodos
10.
Dev Cell ; 55(2): 209-223.e7, 2020 10 26.
Artigo em Inglês | MEDLINE | ID: mdl-33038334

RESUMO

In situ molecular architecture analysis of organelles and protein assemblies is essential to understanding the role of individual components and their cellular function, and to engineering new molecular functionalities. Through a super-resolution-driven approach, here we characterize the organization of the ciliary basal foot, an appendage of basal bodies whose main role is to provide a point of anchoring to the microtubule cytoskeleton. Quantitative image analysis shows that the basal foot is organized into three main regions linked by elongated coiled-coil proteins, revealing a conserved modular architecture in primary and motile cilia, but showing distinct features reflecting its specialized functions. Using domain-specific BioID proximity labeling and super-resolution imaging, we identify CEP112 as a basal foot protein and other candidate components of this assembly, aiding future investigations on the role of basal foot across different cilia systems.


Assuntos
Corpos Basais/metabolismo , Centríolos/metabolismo , Cílios/metabolismo , Microtúbulos/metabolismo , Animais , Transtornos da Motilidade Ciliar/metabolismo , Humanos , Microscopia Eletrônica/métodos , Proteínas/metabolismo
11.
Nat Commun ; 11(1): 1862, 2020 Apr 15.
Artigo em Inglês | MEDLINE | ID: mdl-32296038

RESUMO

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

12.
Sci Transl Med ; 12(535)2020 03 18.
Artigo em Inglês | MEDLINE | ID: mdl-32188719

RESUMO

Airway clearance of pathogens and particulates relies on motile cilia. Impaired cilia motility can lead to reduction in lung function, lung transplant, or death in some cases. More than 50 proteins regulating cilia motility are linked to primary ciliary dyskinesia (PCD), a heterogeneous, mainly recessive genetic lung disease. Accurate PCD molecular diagnosis is essential for identifying therapeutic targets and for initiating therapies that can stabilize lung function, thereby reducing socioeconomic impact of the disease. To date, PCD diagnosis has mainly relied on nonquantitative methods that have limited sensitivity or require a priori knowledge of the genes involved. Here, we developed a quantitative super-resolution microscopy workflow: (i) to increase sensitivity and throughput, (ii) to detect structural defects in PCD patients' cells, and (iii) to quantify motility defects caused by yet to be found PCD genes. Toward these goals, we built a localization map of PCD proteins by three-dimensional structured illumination microscopy and implemented quantitative image analysis and machine learning to detect protein mislocalization, we analyzed axonemal structure by stochastic optical reconstruction microscopy, and we developed a high-throughput method for detecting motile cilia uncoordination by rotational polarity. Together, our data show that super-resolution methods are powerful tools for improving diagnosis of motile ciliopathies.


Assuntos
Transtornos da Motilidade Ciliar , Ciliopatias , Síndrome de Kartagener , Cílios , Transtornos da Motilidade Ciliar/diagnóstico , Humanos , Mutação , Proteínas/genética
13.
Science ; 367(6483)2020 03 13.
Artigo em Inglês | MEDLINE | ID: mdl-32165559

RESUMO

The measured nitrogen-to-carbon ratio in comets is lower than for the Sun, a discrepancy which could be alleviated if there is an unknown reservoir of nitrogen in comets. The nucleus of comet 67P/Churyumov-Gerasimenko exhibits an unidentified broad spectral reflectance feature around 3.2 micrometers, which is ubiquitous across its surface. On the basis of laboratory experiments, we attribute this absorption band to ammonium salts mixed with dust on the surface. The depth of the band indicates that semivolatile ammonium salts are a substantial reservoir of nitrogen in the comet, potentially dominating over refractory organic matter and more volatile species. Similar absorption features appear in the spectra of some asteroids, implying a compositional link between asteroids, comets, and the parent interstellar cloud.

14.
Nature ; 578(7793): 49-52, 2020 02.
Artigo em Inglês | MEDLINE | ID: mdl-32025011

RESUMO

Solar heating of a cometary surface provides the energy necessary to sustain gaseous activity, through which dust is removed1,2. In this dynamical environment, both the coma3,4 and the nucleus5,6 evolve during the orbit, changing their physical and compositional properties. The environment around an active nucleus is populated by dust grains with complex and variegated shapes7, lifted and diffused by gases freed from the sublimation of surface ices8,9. The visible colour of dust particles is highly variable: carbonaceous organic material-rich grains10 appear red while magnesium silicate-rich11,12 and water-ice-rich13,14 grains appear blue, with some dependence on grain size distribution, viewing geometry, activity level and comet family type. We know that local colour changes are associated with grain size variations, such as in the bluer jets made of submicrometre grains on comet Hale-Bopp15 or in the fragmented grains in the coma16 of C/1999 S4 (LINEAR). Apart from grain size, composition also influences the coma's colour response, because transparent volatiles can introduce a substantial blueing in scattered light, as observed in the dust particles ejected after the collision of the Deep Impact probe with comet 9P/Tempel 117. Here we report observations of two opposite seasonal colour cycles in the coma and on the surface of comet 67P/Churyumov-Gerasimenko through its perihelion passage18. Spectral analysis indicates an enrichment of submicrometre grains made of organic material and amorphous carbon in the coma, causing reddening during the passage. At the same time, the progressive removal of dust from the nucleus causes the exposure of more pristine and bluish icy layers on the surface. Far from the Sun, we find that the abundance of water ice on the nucleus is reduced owing to redeposition of dust and dehydration of the surface layer while the coma becomes less red.

16.
Elife ; 72018 08 31.
Artigo em Inglês | MEDLINE | ID: mdl-30168418

RESUMO

Centrosome structure, function, and number are finely regulated at the cellular level to ensure normal mammalian development. Here, we characterize PPP1R35 as a novel bona fide centrosomal protein and demonstrate that it is critical for centriole elongation. Using quantitative super-resolution microscopy mapping and live-cell imaging we show that PPP1R35 is a resident centrosomal protein located in the proximal lumen above the cartwheel, a region of the centriole that has eluded detailed characterization. Loss of PPP1R35 function results in decreased centrosome number and shortened centrioles that lack centriolar distal and microtubule wall associated proteins required for centriole elongation. We further demonstrate that PPP1R35 acts downstream of, and forms a complex with, RTTN, a microcephaly protein required for distal centriole elongation. Altogether, our study identifies a novel step in the centriole elongation pathway centered on PPP1R35 and elucidates downstream partners of the microcephaly protein RTTN.


Assuntos
Proteínas de Transporte/metabolismo , Proteínas de Ciclo Celular/metabolismo , Centríolos/metabolismo , Centrossomo/metabolismo , Proteínas de Transporte/genética , Proteínas de Ciclo Celular/genética , Linhagem Celular Tumoral , Proteínas de Fluorescência Verde/genética , Proteínas de Fluorescência Verde/metabolismo , Células HEK293 , Humanos , Microscopia Confocal , Ligação Proteica , Interferência de RNA
17.
Cell Chem Biol ; 25(8): 1017-1030.e9, 2018 08 16.
Artigo em Inglês | MEDLINE | ID: mdl-30126533

RESUMO

Acyldepsipeptides (ADEPs) are potential antibiotics that dysregulate the activity of the highly conserved tetradecameric bacterial ClpP protease, leading to bacterial cell death. Here, we identified ADEP analogs that are potent dysregulators of the human mitochondrial ClpP (HsClpP). These ADEPs interact tightly with HsClpP, causing the protease to non-specifically degrade model substrates. Dysregulation of HsClpP activity by ADEP was found to induce cytotoxic effects via activation of the intrinsic, caspase-dependent apoptosis. ADEP-HsClpP co-crystal structure was solved for one of the analogs revealing a highly complementary binding interface formed by two HsClpP neighboring subunits but, unexpectedly, with HsClpP in the compact conformation. Given that HsClpP is highly expressed in multiple cancers and has important roles in cell metastasis, our findings suggest a therapeutic potential for ADEPs in cancer treatment.


Assuntos
Antibacterianos/efeitos adversos , Antibacterianos/química , Apoptose/efeitos dos fármacos , Depsipeptídeos/efeitos adversos , Depsipeptídeos/química , Endopeptidase Clp/metabolismo , Mitocôndrias/efeitos dos fármacos , Acilação , Antibacterianos/farmacologia , Infecções Bacterianas/tratamento farmacológico , Infecções Bacterianas/microbiologia , Linhagem Celular Tumoral , Depsipeptídeos/farmacologia , Endopeptidase Clp/química , Células HEK293 , Humanos , Mitocôndrias/enzimologia , Simulação de Acoplamento Molecular , Neoplasias/tratamento farmacológico , Neoplasias/enzimologia
18.
Nat Commun ; 9(1): 2800, 2018 07 13.
Artigo em Inglês | MEDLINE | ID: mdl-30006521

RESUMO

In the original version of this Article, the affiliation details for Jadranka Loncarek and Vito Mennella were incorrectly given as 'Cell Biology Program, The Hospital for Sick Children, Department of Biochemistry, University of Toronto, 555 University Avenue, Toronto, ON, M5G 1X8, Canada' and 'Laboratory of Protein Dynamics and Signaling, Center for Cancer Research, National Cancer Institute, 1050 Boyles Street, Frederick, MD, 21702, USA', respectively. This has now been corrected in both the PDF and HTML versions of the Article.

19.
Nat Commun ; 9(1): 2210, 2018 06 07.
Artigo em Inglês | MEDLINE | ID: mdl-29880810

RESUMO

The inheritance of the centrosome during human fertilization remains mysterious. Here we show that the sperm centrosome contains, in addition to the known typical barrel-shaped centriole (the proximal centriole, PC), a surrounding matrix (pericentriolar material, PCM), and an atypical centriole (distal centriole, DC) composed of splayed microtubules surrounding previously undescribed rods of centriole luminal proteins. The sperm centrosome is remodeled by both reduction and enrichment of specific proteins and the formation of these rods during spermatogenesis. In vivo and in vitro investigations show that the flagellum-attached, atypical DC is capable of recruiting PCM, forming a daughter centriole, and localizing to the spindle pole during mitosis. Altogether, we show that the DC is compositionally and structurally remodeled into an atypical centriole, which functions as the zygote's second centriole. These findings now provide novel avenues for diagnostics and therapeutic strategies for male infertility, and insights into early embryo developmental defects.


Assuntos
Centríolos/fisiologia , Fertilização/fisiologia , Espermatogênese/fisiologia , Espermatozoides/citologia , Animais , Bovinos , Proteínas de Ciclo Celular/metabolismo , Linhagem Celular Tumoral , Centríolos/ultraestrutura , Anormalidades Congênitas/etiologia , Desenvolvimento Embrionário/fisiologia , Feminino , Fertilização in vitro , Flagelos/fisiologia , Humanos , Infertilidade Masculina/etiologia , Masculino , Microscopia Eletrônica , Microtúbulos/fisiologia , Microtúbulos/ultraestrutura , Mitose/fisiologia , Espermatozoides/fisiologia , Espermatozoides/ultraestrutura , Testículo/citologia , Tubulina (Proteína)/metabolismo , Xenopus laevis , Zigoto/citologia
20.
Mol Biol Cell ; 27(11): 1740-52, 2016 06 01.
Artigo em Inglês | MEDLINE | ID: mdl-27053665

RESUMO

Ninein (Nin) is a centrosomal protein whose gene is mutated in Seckel syndrome (SCKL, MIM 210600), an inherited recessive disease that results in primordial dwarfism, cognitive deficiencies, and increased sensitivity to genotoxic stress. Nin regulates neural stem cell self-renewal, interkinetic nuclear migration, and microtubule assembly in mammals. Nin is evolutionarily conserved, yet its role in cell division and development has not been investigated in a model organism. Here we characterize the single Nin orthologue in Drosophila Drosophila Nin localizes to the periphery of the centrosome but not at centriolar structures as in mammals. However, Nin shares the property of its mammalian orthologue of promoting microtubule assembly. In neural and germline stem cells, Nin localizes asymmetrically to the younger (daughter) centrosome, yet it is not required for the asymmetric division of stem cells. In wing epithelia and muscle, Nin localizes to noncentrosomal microtubule-organizing centers. Surprisingly, loss of nin expression from a nin mutant does not significantly affect embryonic and brain development, fertility, or locomotor performance of mutant flies or their survival upon exposure to DNA-damaging agents. Although it is not essential, our data suggest that Nin plays a supportive role in centrosomal and extracentrosomal microtubule organization and asymmetric stem cell division.


Assuntos
Centrossomo/metabolismo , Dano ao DNA , Proteínas de Drosophila/genética , Proteínas de Drosophila/metabolismo , Animais , Divisão Celular , Centríolos/metabolismo , Centrossomo/fisiologia , Proteínas do Citoesqueleto/metabolismo , Drosophila/metabolismo , Centro Organizador dos Microtúbulos/metabolismo , Microtúbulos/metabolismo , Proteínas Nucleares/metabolismo , Células-Tronco/metabolismo
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