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1.
J Dev Biol ; 8(3)2020 Sep 07.
Artigo em Inglês | MEDLINE | ID: mdl-32906663

RESUMO

Formation and regulation of properly sized epithelial tubes is essential for multicellular life. The excretory canal cell of C. elegans provides a powerful model for investigating the integration of the cytoskeleton, intracellular transport, and organismal physiology to regulate the developmental processes of tube extension, lumen formation, and lumen diameter regulation in a narrow single cell. Multiple studies have provided new understanding of actin and intermediate filament cytoskeletal elements, vesicle transport, and the role of vacuolar ATPase in determining tube size. Most of the genes discovered have clear homologues in humans, with implications for understanding these processes in mammalian tissues such as Schwann cells, renal tubules, and brain vasculature. The results of several new genetic screens are described that provide a host of new targets for future studies in this informative structure.

2.
J Cell Biol ; 219(11)2020 11 02.
Artigo em Inglês | MEDLINE | ID: mdl-32860501

RESUMO

Single-celled tubules represent a complicated structure that forms during development, requiring extension of a narrow cytoplasm surrounding a lumen exerting osmotic pressure that can burst the luminal membrane. Genetic studies on the excretory canal cell of Caenorhabditis elegans have revealed many proteins that regulate the cytoskeleton, vesicular transport, and physiology of the narrow canals. Here, we show that ßH-spectrin regulates the placement of intermediate filament proteins forming a terminal web around the lumen, and that the terminal web in turn retains a highly conserved protein (EXC-9/CRIP1) that regulates apical endosomal trafficking. EXC-1/IRG, the binding partner of EXC-9, is also localized to the apical membrane and affects apical actin placement and RAB-8-mediated vesicular transport. The results suggest that an intermediate filament protein acts in a novel pathway to direct the traffic of vesicles to locations of lengthening apical surface during single-celled tubule development.


Assuntos
Proteínas de Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/crescimento & desenvolvimento , Exocitose , Proteínas de Filamentos Intermediários/metabolismo , Organogênese , Vesículas Transportadoras/fisiologia , Proteínas de Transporte Vesicular/metabolismo , Animais , Caenorhabditis elegans/genética , Caenorhabditis elegans/metabolismo , Proteínas de Caenorhabditis elegans/genética , Proteínas de Filamentos Intermediários/genética , Análise de Célula Única , Proteínas de Transporte Vesicular/genética
3.
G3 (Bethesda) ; 9(5): 1339-1353, 2019 05 07.
Artigo em Inglês | MEDLINE | ID: mdl-30885922

RESUMO

Regulation of luminal diameter is critical to the function of small single-celled tubes, of which the seamless tubular excretory canals of Caenorhabditis elegans provide a tractable genetic model. Mutations in several sets of genes exhibit the Exc phenotype, in which canal luminal growth is visibly altered. Here, a focused reverse genomic screen of genes highly expressed in the canals found 18 genes that significantly affect luminal outgrowth or diameter. These genes encode novel proteins as well as highly conserved proteins involved in processes including gene expression, cytoskeletal regulation, and vesicular and transmembrane transport. In addition, two genes act as suppressors on a pathway of conserved genes whose products mediate vesicle movement from early to recycling endosomes. The results provide new tools for understanding the integration of cytoplasmic structure and physiology in forming and maintaining the narrow diameter of single-cell tubules.


Assuntos
Proteínas de Caenorhabditis elegans/genética , Caenorhabditis elegans/genética , Caenorhabditis elegans/metabolismo , Glândulas Exócrinas/metabolismo , Animais , Transporte Biológico , Caenorhabditis elegans/ultraestrutura , Proteínas de Caenorhabditis elegans/metabolismo , Glândulas Exócrinas/ultraestrutura , Técnicas de Silenciamento de Genes , Estudos de Associação Genética , Genótipo , Mutação , Fenótipo , Interferência de RNA
4.
Genetics ; 210(2): 637-652, 2018 10.
Artigo em Inglês | MEDLINE | ID: mdl-29945901

RESUMO

The excretory canals of Caenorhabditis elegans are a model for understanding the maintenance of apical morphology in narrow single-celled tubes. Light and electron microscopy shows that mutants in exc-2 start to form canals normally, but these swell to develop large fluid-filled cysts that lack a complete terminal web at the apical surface, and accumulate filamentous material in the canal lumen. Here, whole-genome sequencing and gene rescue show that exc-2 encodes intermediate filament protein IFC-2 EXC-2/IFC-2 protein, fluorescently tagged via clustered regularly interspaced short palindromic repeats/Cas9, is located at the apical surface of the canals independently of other intermediate filament proteins. EXC-2 is also located in several other tissues, though the tagged isoforms are not seen in the larger intestinal tube. Tagged EXC-2 binds via pulldown to intermediate filament protein IFA-4, which is also shown to line the canal apical surface. Overexpression of either protein results in narrow but shortened canals. These results are consistent with a model whereby three intermediate filaments in the canals-EXC-2, IFA-4, and IFB-1-restrain swelling of narrow tubules in concert with actin filaments that guide the extension and direction of tubule outgrowth, while allowing the tube to bend as the animal moves.


Assuntos
Proteínas de Caenorhabditis elegans/metabolismo , Células Epiteliais/metabolismo , Proteínas de Filamentos Intermediários/metabolismo , Animais , Caenorhabditis elegans/citologia , Caenorhabditis elegans/genética , Caenorhabditis elegans/metabolismo , Proteínas de Caenorhabditis elegans/genética , Células Epiteliais/citologia , Proteínas de Filamentos Intermediários/genética , Ligação Proteica
5.
Genetics ; 203(4): 1789-806, 2016 08.
Artigo em Inglês | MEDLINE | ID: mdl-27334269

RESUMO

Determination of luminal diameter is critical to the function of small single-celled tubes. A series of EXC proteins, including EXC-1, prevent swelling of the tubular excretory canals in Caenorhabditis elegans In this study, cloning of exc-1 reveals it to encode a homolog of mammalian IRG proteins, which play roles in immune response and autophagy and are associated with Crohn's disease. Mutants in exc-1 accumulate early endosomes, lack recycling endosomes, and exhibit abnormal apical cytoskeletal structure in regions of enlarged tubules. EXC-1 interacts genetically with two other EXC proteins that also affect endosomal trafficking. In yeast two-hybrid assays, wild-type and putative constitutively active EXC-1 binds to the LIM-domain protein EXC-9, whose homolog, cysteine-rich intestinal protein, is enriched in mammalian intestine. These results suggest a model for IRG function in forming and maintaining apical tubule structure via regulation of endosomal recycling.


Assuntos
Proteínas de Caenorhabditis elegans/genética , Endossomos/genética , Metaloproteínas/genética , Animais , Autofagia/genética , Caenorhabditis elegans/genética , Caenorhabditis elegans/crescimento & desenvolvimento , Proteínas de Caenorhabditis elegans/metabolismo , Doença de Crohn/genética , Doença de Crohn/patologia , Citoesqueleto/genética , Citoesqueleto/metabolismo , Endossomos/metabolismo , Humanos , Túbulos Renais/crescimento & desenvolvimento , Túbulos Renais/metabolismo , Metaloproteínas/metabolismo , Transporte Proteico/genética , Técnicas do Sistema de Duplo-Híbrido
6.
Genetics ; 203(1): 35-63, 2016 05.
Artigo em Inglês | MEDLINE | ID: mdl-27183565

RESUMO

The excretory system of the nematode Caenorhabditis elegans is a superb model of tubular organogenesis involving a minimum of cells. The system consists of just three unicellular tubes (canal, duct, and pore), a secretory gland, and two associated neurons. Just as in more complex organs, cells of the excretory system must first adopt specific identities and then coordinate diverse processes to form tubes of appropriate topology, shape, connectivity, and physiological function. The unicellular topology of excretory tubes, their varied and sometimes complex shapes, and the dynamic reprogramming of cell identity and remodeling of tube connectivity that occur during larval development are particularly fascinating features of this organ. The physiological roles of the excretory system in osmoregulation and other aspects of the animal's life cycle are only beginning to be explored. The cellular mechanisms and molecular pathways used to build and shape excretory tubes appear similar to those used in both unicellular and multicellular tubes in more complex organs, such as the vertebrate vascular system and kidney, making this simple organ system a useful model for understanding disease processes.


Assuntos
Caenorhabditis elegans/citologia , Caenorhabditis elegans/fisiologia , Plasticidade Celular , Glândulas Exócrinas/citologia , Glândulas Exócrinas/fisiologia , Via Secretória , Animais , Especificidade de Órgãos
7.
Nat Cell Biol ; 15(2): 143-56, 2013 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-23334498

RESUMO

Many unicellular tubes such as capillaries form lumens intracellularly, a process that is not well understood. Here we show that the cortical membrane organizer ERM-1 is required to expand the intracellular apical/lumenal membrane and its actin undercoat during single-cell Caenorhabditis elegans excretory canal morphogenesis. We characterize AQP-8, identified in an ERM-1-overexpression (ERM-1[++]) suppressor screen, as a canalicular aquaporin that interacts with ERM-1 in lumen extension in a mercury-sensitive manner, implicating water-channel activity. AQP-8 is transiently recruited to the lumen by ERM-1, co-localizing in peri-lumenal cuffs interspaced along expanding canals. An ERM-1[++]-mediated increase in the number of lumen-associated canaliculi is reversed by AQP-8 depletion. We propose that the ERM-1/AQP-8 interaction propels lumen extension by translumenal flux, suggesting a direct morphogenetic effect of water-channel-regulated fluid pressure.


Assuntos
Aquaporinas/metabolismo , Proteínas de Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/metabolismo , Membrana Celular/metabolismo , Proteínas do Citoesqueleto/metabolismo , Citoesqueleto de Actina/metabolismo , Animais , Animais Geneticamente Modificados , Aquaporinas/genética , Caenorhabditis elegans/efeitos dos fármacos , Caenorhabditis elegans/embriologia , Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/genética , Membrana Celular/efeitos dos fármacos , Permeabilidade da Membrana Celular , Proteínas do Citoesqueleto/genética , Regulação da Expressão Gênica no Desenvolvimento , Genótipo , Cloreto de Mercúrio/farmacologia , Morfogênese , Mutação , Pressão Osmótica , Fenótipo , Ligação Proteica , Transporte Proteico , Interferência de RNA , Fatores de Tempo , Água/metabolismo , Equilíbrio Hidroeletrolítico
8.
Dev Biol ; 359(1): 59-72, 2011 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-21889936

RESUMO

Maintenance of the shape of biological tubules is critical for development and physiology of metazoan organisms. Loss of function of the Caenorhabditis elegans FGD protein EXC-5 allows large fluid-filled cysts to form in the lumen of the single-cell excretory canal tubules, while overexpression of exc-5 causes defects at the tubule's basolateral surface. We have examined the effects of altering expression levels of exc-5 on the distribution of fluorescently-marked subcellular organelles. In exc-5 mutants, early endosomes build up in the cell, especially in areas close to cysts, while recycling endosomes are depleted. Endosome morphology changes prior to cyst formation. Conversely, when exc-5 is overexpressed, recycling endosomes are enriched. Since FGD proteins activate the small GTPases CDC42 and Rac, these results support the hypothesis that EXC-5 acts through small GTPases to move material from apical early endosomes to recycling endosomes, and that loss of such movement is likely the cause of tubule deformation both in nematodes and in tissues affected by FGD dysfunction such as Charcot-Marie-Tooth Syndrome type 4H.


Assuntos
Proteínas de Caenorhabditis elegans/fisiologia , Caenorhabditis elegans/metabolismo , Fatores de Troca do Nucleotídeo Guanina/fisiologia , Animais , Transporte Biológico , Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/metabolismo , Fatores de Troca do Nucleotídeo Guanina/metabolismo , Microinjeções , Frações Subcelulares/metabolismo
9.
BMC Dev Biol ; 8: 110, 2008 Nov 17.
Artigo em Inglês | MEDLINE | ID: mdl-19014691

RESUMO

BACKGROUND: The founding member of the EMAP-like protein family is the Echinoderm Microtubule-Associated Protein (EMAP), so-named for its abundance in sea urchin, starfish, and sand dollar eggs. The EMAP-like protein family has five members in mammals (EML1 through EML5) and only one in both Drosophila (ELP-1) and C. elegans (ELP-1). Biochemical studies of sea urchin EMAP and vertebrate EMLs implicate these proteins in the regulation of microtubule stability. So far, however, the physiological function of this protein family remains unknown. RESULTS: We examined the expression pattern of C. elegans ELP-1 by means of transgenic gene expression in living embryos and adults, and by immunolocalization with an ELP-1-specific antibody in fixed tissues. In embryos, ELP-1 is expressed in the hypodermis. In larvae and adults, ELP-1 is expressed in the body wall, spermatheca and vulval muscles, intestine, and hypodermal seam cells. In muscle, ELP-1 is associated with adhesion complexes near the cell surface and is bound to a criss-crossing network of microtubules in the cytoplasm. ELP-1 is also expressed in a subset of mechanoreceptor neurons, including the ray neurons in the male tail, microtubule-rich touch receptor neurons, and the six ciliated IL1 neurons. This restricted localization in the nervous system implies that ELP-1 plays a role in mechanotransmission. Consistent with this idea, decreasing ELP-1 expression decreases sensitivity to gentle touch applied to the body wall. CONCLUSION: These data imply that ELP-1 may play an important role during the transmission of forces and signals between the body surface and both muscle cells and touch receptor neurons.


Assuntos
Proteínas de Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/metabolismo , Proteínas Associadas aos Microtúbulos/metabolismo , Microtúbulos/metabolismo , Sequência de Aminoácidos , Animais , Western Blotting , Caenorhabditis elegans/embriologia , Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/fisiologia , Embrião não Mamífero/embriologia , Embrião não Mamífero/metabolismo , Proteínas de Fluorescência Verde/genética , Proteínas de Fluorescência Verde/metabolismo , Microscopia de Fluorescência , Proteínas Associadas aos Microtúbulos/genética , Proteínas Associadas aos Microtúbulos/fisiologia , Dados de Sequência Molecular , Neurônios/metabolismo , Ligação Proteica
10.
Dev Biol ; 317(1): 225-33, 2008 May 01.
Artigo em Inglês | MEDLINE | ID: mdl-18384766

RESUMO

Maintenance of the shape and diameter of biological tubules is a critical task in the development and physiology of all metazoan organisms. We have cloned the exc-9 gene of Caenorhabditis elegans, which regulates the diameter of the single-cell excretory canal tubules. exc-9 encodes a homologue of the highly expressed mammalian intestinal LIM-domain protein CRIP, whose function has not previously been determined. A second well-conserved CRIP homologue functions in multiple valves of C. elegans. EXC-9 shows genetic interactions with other EXC proteins, including the EXC-5 guanine exchange factor that regulates CDC-42 activity. EXC-9 and its nematode homologue act in polarized epithelial cells that must maintain great flexibility at their apical surface; our results suggest that CRIPs function to maintain cytoskeletal flexibility at the apical surface.


Assuntos
Proteínas de Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/metabolismo , Metaloproteínas/metabolismo , Sequência de Aminoácidos , Animais , Caenorhabditis elegans/citologia , Proteínas de Caenorhabditis elegans/química , Proteínas de Caenorhabditis elegans/genética , Proteínas de Transporte/química , Proteínas de Transporte/metabolismo , Citoesqueleto/química , Citoesqueleto/metabolismo , Regulação da Expressão Gênica , Mamíferos , Metaloproteínas/química , Metaloproteínas/genética , Dados de Sequência Molecular , Estrutura Terciária de Proteína , Alinhamento de Sequência
11.
Cell Calcium ; 37(6): 593-601, 2005 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-15862350

RESUMO

Polycystin-2, a member of the TRP family of calcium channels, is encoded by the human PKD2 gene. Mutations in that gene can lead to swelling of nephrons into the fluid-filled cysts of polycystic kidney disease. In addition to expression in tubular epithelial cells, human polycystin-2 is found in muscle and neuronal cells, but its cell biological function has been unclear. A homologue in Caenorhabditis elegans is necessary for male mating behavior. We compared the behavior, calcium signaling mechanisms, and electrophysiology of wild-type and pkd-2 knockout C. elegans. In addition to characterizing PKD-2-mediated aggregation and mating behaviors, we found that polycystin-2 is an intracellular Ca(2+) release channel that is required for the normal pattern of Ca(2+) responses involving IP(3) and ryanodine receptor-mediated Ca(2+) release from intracellular stores. Activity of polycystin-2 creates brief cytosolic Ca(2+) transients with increased amplitude and decreased duration. Polycystin-2, along with the IP(3) and ryanodine receptors, acts as a major calcium-release channel in the endoplasmic reticulum in cells where rapid calcium signaling is required, and polycystin-2 activity is essential in those excitable cells for rapid responses to stimuli.


Assuntos
Cálcio/metabolismo , Proteínas de Membrana/fisiologia , Sequência de Aminoácidos , Animais , Caenorhabditis elegans , Canais de Cálcio/metabolismo , Sinalização do Cálcio , Eletrofisiologia , Retículo Endoplasmático/metabolismo , Feminino , Humanos , Receptores de Inositol 1,4,5-Trifosfato , Masculino , Proteínas de Membrana/genética , Dados de Sequência Molecular , Mutação , Neurônios/metabolismo , Receptores Citoplasmáticos e Nucleares/metabolismo , Canal de Liberação de Cálcio do Receptor de Rianodina/metabolismo , Comportamento Sexual Animal/fisiologia , Canais de Cátion TRPP
12.
Dev Biol ; 256(2): 290-301, 2003 Apr 15.
Artigo em Inglês | MEDLINE | ID: mdl-12679103

RESUMO

The exc mutations of Caenorhabditis elegans alter the position and shape of the apical cytoskeleton in polarized epithelial cells. Mutants in exc-7 form small cysts throughout the tubular excretory canals that regulate organismal osmolarity. We have cloned the exc-7 gene, the closest nematode homologue to the neural RNA-binding protein ELAV. EXC-7 is expressed in the canal for a short time midway through embryogenesis. Cysts in exc-7 mutants do not develop until several hours later, beginning at the time of hatching. We find that the first larval period is when the canal completes the majority of its outgrowth, and adds new apical cytoskeleton at a rapid rate. Ultrastructural studies show that exc-7 mutant defects resemble loss of beta(H)-spectrin (encoded by sma-1) at the distal ends of the excretory canals. In addition, exc-7 mutants exhibit synergistic excretory canal defects with mutations in sma-1, and EXC-7 binds sma-1 mRNA. These data imply that EXC-7 protein may affect expression of sma-1 and other genes to effect proper development of the excretory canals.


Assuntos
Proteínas de Caenorhabditis elegans/genética , Caenorhabditis elegans/embriologia , Regulação da Expressão Gênica no Desenvolvimento , Proteínas de Ligação a RNA/genética , Ribonucleoproteínas/genética , Animais , Proteínas ELAV , Microscopia Eletrônica , Mutação , Ribonucleoproteínas/metabolismo , Sistema Urinário/embriologia , Sistema Urinário/ultraestrutura
13.
J Gen Virol ; 84(Pt 2): 375-381, 2003 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-12560570

RESUMO

Walleye dermal sarcomas are associated with the presence of a complex retrovirus, walleye dermal sarcoma virus (WDSV). These sarcomas develop and regress seasonally in naturally infected fish. In addition to gag, pol and env, WDSV contains three open reading frames (ORFs), designated orf a, orf b and orf c. orf c is located between the 5' long terminal repeat and gag. Developing tumours contain low levels of orf a and orf b transcripts, whereas regressing tumours contain high levels of genomic transcripts and virus particles. Orf C protein is encoded by the full-length, genomic transcript and can be detected in tumour extracts with anti-Orf C-specific antisera. To determine the subcellular location of WDSV Orf C, cultured cells were transfected with an expression vector encoding haemagglutinin-tagged Orf C and examined by immunofluorescence. Orf C was observed throughout the cytoplasm and accumulated in cytoplasmic organelles. Dual-antibody staining for Orf C and mitochondrial cytochrome c demonstrated colocalization of Orf C with mitochondria and loss of the normal distribution of mitochondria in the cytoplasm. Cells transiently expressing Orf C exhibited apoptotic morphology and increased levels of surface phosphatidylserine and were unable to retain MitoTracker Orange, a dye that accumulates in active mitochondria. These results imply a functional role for WDSV Orf C in an alteration of mitochondrial function that results in apoptosis contributing to tumour regression.


Assuntos
Epsilonretrovirus/patogenicidade , Doenças dos Peixes/metabolismo , Doenças dos Peixes/virologia , Mitocôndrias/metabolismo , Proteínas dos Retroviridae/metabolismo , Sarcoma/veterinária , Neoplasias Cutâneas/veterinária , Animais , Linhagem Celular , Cães , Peixes/virologia , Humanos , Camundongos , Infecções por Retroviridae/metabolismo , Infecções por Retroviridae/veterinária , Infecções por Retroviridae/virologia , Proteínas dos Retroviridae/genética , Sarcoma/virologia , Neoplasias Cutâneas/virologia , Infecções Tumorais por Vírus/metabolismo , Infecções Tumorais por Vírus/veterinária , Infecções Tumorais por Vírus/virologia
14.
Nephron Exp Nephrol ; 93(1): e9-17, 2003 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-12411744

RESUMO

Autosomal dominant polycystic kidney disease (ADPKD) is a very common inherited disease caused by mutations in PKD1 or PKD2 genes characterized by progressive enlargement of fluid-filled cysts and loss of renal function [1]. Previous studies proposed a role for human polycystin-1 in renal morphogenesis acting as a matrix receptor in focal adhesions and for polycystin-2 as a putative calcium channel [2, 3]. The genome of Caenorhabditis elegans contains 2 new members of the polycystin family: lov-1, the homolog for PKD1; and pkd-2, the homolog for PKD2 [4; this paper]. Mutation analysis in C. elegans showed similarly compromised male mating behaviors in all single and double lov-1 and pkd-2 mutants, indicating their participation in a single genetic pathway. Expression analysis localized LOV-1 and PKD-2 to the ends of sensory neurons in male tails and to the tips of CEM neurons in the head, consistent with functions as chemo- or mechanosensors. Human and C. elegans PKD1 and PKD2 homologs, transfected into mammalian renal epithelial cells, co-localized with paxillin in focal adhesions suggesting function in a single biological pathway. Based on the role of polycystins in C. elegans sensory neuron function and the conservation of PKD pathways we suggest that polycystins act as sensors of the extracellular environment, initiating, via focal adhesion assembly, intracellular transduction events in neuronal or morphogenetic processes.


Assuntos
Proteínas de Membrana/genética , Rim Policístico Autossômico Dominante/metabolismo , Sequência de Aminoácidos , Animais , Caenorhabditis elegans/genética , Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/fisiologia , Proteínas de Caenorhabditis elegans/biossíntese , Proteínas de Caenorhabditis elegans/química , Proteínas de Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/fisiologia , Linhagem Celular , Genes de Helmintos/genética , Genoma , Humanos , Rim , Células LLC-PK1/química , Masculino , Proteínas de Membrana/biossíntese , Proteínas de Membrana/química , Proteínas de Membrana/fisiologia , Dados de Sequência Molecular , Neurônios Aferentes/metabolismo , Biossíntese de Proteínas , Estrutura Terciária de Proteína/genética , Estrutura Terciária de Proteína/fisiologia , Proteínas/química , Proteínas/genética , Proteínas/fisiologia , Homologia de Sequência do Ácido Nucleico , Comportamento Sexual Animal/fisiologia , Transdução de Sinais/genética , Transdução de Sinais/fisiologia , Suínos , Canais de Cátion TRPP
15.
Trends Cell Biol ; 12(10): 479-84, 2002 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-12441252

RESUMO

The formation and regulation of tubule shape and size is fundamental to the development and function of many tissues and organs in metazoan organisms. The excretory canals of the nematode Caenorhabditis elegans are a fascinating example of cell morphogenesis, as the tiny worm manages to create a complicated set of tubular epithelia within a single cell. In addition to the inherent attraction of studying this cytoengineering feat, the excretory cell provides a simple genetically tractable model for studying tubule formation and regulation of tubule diameter. Mutations in the exc genes alter the diameter of the lumenal surface of these tubules. Cloning of these genes reveals a set of proteins that both control tubule diameter and regulate the comparative growth of the apical and basal tubular surfaces.


Assuntos
Caenorhabditis elegans/crescimento & desenvolvimento , Células Epiteliais/citologia , Animais , Caenorhabditis elegans/citologia , Células Epiteliais/fisiologia , Larva/citologia , Larva/crescimento & desenvolvimento
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