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Article ; Online: Navigating the cell: UNC-53 and the navigators, a family of cytoskeletal regulators with multiple roles in cell migration, outgrowth and trafficking.

Stringham, Eve G / Schmidt, Kristopher L

2009 Volume 3, Issue 4, Page(s) 342–346

Abstract: Changes in cell shape are associated with a variety of processes including cell migration, axon outgrowth, cell division and vesicle trafficking. C. elegans UNC-53 and its vertebrate homologs, the Navigators, are required for the migration of cells and ... ...

Abstract	Changes in cell shape are associated with a variety of processes including cell migration, axon outgrowth, cell division and vesicle trafficking. C. elegans UNC-53 and its vertebrate homologs, the Navigators, are required for the migration of cells and the outgrowth of neuronal processes. The identification of novel molecular interactions and live imaging studies have revealed that UNC-53/NAVs are signal transducers associated with actin filaments, microtubules and intermediate filaments. In addition to modulating cytoskeletal dynamics at the leading edge of migrating or outgrowing cells, both UNC-53 and the navigators are expressed in adult cells, conspicuously those with specialized roles in endocytosis or secretion. Collectively, these results suggest that UNC-53/NAVs may be a central regulator of cytoskeletal dynamics, responsible for integrating signaling cues to multiple components of the cytoskeleton to coordinate rearrangement during cell outgrowth or trafficking.
MeSH term(s)	Animals ; Biological Transport/physiology ; Caenorhabditis elegans Proteins/physiology ; Cell Enlargement ; Cell Movement/physiology ; Cytoskeleton/metabolism ; Humans ; Microfilament Proteins/physiology
Chemical Substances	Caenorhabditis elegans Proteins ; Microfilament Proteins ; UNC-53 protein, C elegans
Language	English
Publishing date	2009-10-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2268518-2
ISSN	1933-6926 ; 1933-6918
ISSN (online)	1933-6926
ISSN	1933-6918
DOI	10.4161/cam.3.4.9451
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Distinct cell guidance pathways controlled by the Rac and Rho GEF domains of UNC-73/TRIO in Caenorhabditis elegans.

Marcus-Gueret, Nancy / Schmidt, Kristopher L / Stringham, Eve G

Genetics

2011 Volume 190, Issue 1, Page(s) 129–142

Abstract: The cytoskeleton regulator UNC-53/NAV2 is required for both the anterior and posterior outgrowth of several neurons as well as that of the excretory cell while the kinesin-like motor VAB-8 is essential for most posteriorly directed migrations in ... ...

Abstract	The cytoskeleton regulator UNC-53/NAV2 is required for both the anterior and posterior outgrowth of several neurons as well as that of the excretory cell while the kinesin-like motor VAB-8 is essential for most posteriorly directed migrations in Caenorhabditis elegans. Null mutations in either unc-53 or vab-8 result in reduced posterior excretory canal outgrowth, while double null mutants display an enhanced canal extension defect, suggesting the genes act in separate pathways to control this posteriorly directed outgrowth. Genetic analysis of putative interactors of UNC-53 or VAB-8, and cell-specific rescue experiments suggest that VAB-8, SAX-3/ROBO, SLT-1/Slit, and EVA-1 are functioning together in the outgrowth of the excretory canals, while UNC-53 appears to function in a parallel pathway with UNC-71/ADAM. The known VAB-8 interactor, the Rac/Rho GEF UNC-73/TRIO operates in both pathways, as isoform specific alleles exhibit enhancement of the phenotype in double-mutant combination with either unc-53 or vab-8. On the basis of these results, we propose a bipartite model for UNC-73/TRIO activity in excretory canal extension: a cell autonomous function that is mediated by the Rho-specific GEF domain of the UNC-73E isoform in conjunction with UNC-53 and UNC-71 and a cell nonautonomous function that is mediated by the Rac-specific GEF domain of the UNC-73B isoform, through partnering with VAB-8 and the receptors SAX-3 and EVA-1.
MeSH term(s)	Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/growth & development ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Movement/genetics ; Gonads/metabolism ; Guanine Nucleotide Exchange Factors/chemistry ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Models, Biological ; Myoblasts/metabolism ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Protein Structure, Tertiary ; Receptors, Immunologic/metabolism ; Signal Transduction ; Roundabout Proteins
Chemical Substances	Caenorhabditis elegans Proteins ; Guanine Nucleotide Exchange Factors ; Microfilament Proteins ; Nerve Tissue Proteins ; Receptors, Immunologic ; UNC-53 protein, C elegans ; UNC-73 protein, C elegans ; vab-8 protein, C elegans
Language	English
Publishing date	2011-10-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2167-2
ISSN	1943-2631 ; 0016-6731
ISSN (online)	1943-2631
ISSN	0016-6731
DOI	10.1534/genetics.111.134429
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Article ; Online: Live cell imaging of the cytoskeleton.

Stringham, Eve G / Marcus-Gueret, Nancy / Ramsay, Laura / Schmidt, Kristopher L

Methods in enzymology

2012 Volume 505, Page(s) 203–217

Abstract: The cytoskeleton is the network of cytoplasmic protein filaments, composed of microtubules (MTs), actin filaments, and intermediate filaments, that provides an internal scaffold to give the cell shape. The organization of the cytoskeleton is not static ... ...

Abstract	The cytoskeleton is the network of cytoplasmic protein filaments, composed of microtubules (MTs), actin filaments, and intermediate filaments, that provides an internal scaffold to give the cell shape. The organization of the cytoskeleton is not static but rather rearranges to enable a variety of fundamental cellular processes including chromosome segregation, cytokinesis, cell migration, cell polarity, cell adhesion, neuron outgrowth, chemotaxis, muscle contraction, cytoplasmic streaming, locomotion by flagella, subcellular organelle distribution, and intracellular trafficking. Given this multifunctional role, it is not surprising that cytoskeletal defects have been associated with a large variety of human diseases including neurodegenerative disorders, cancer, muscular dystrophies, and cardiac disorders. Therefore, understanding the molecular basis of cytoskeleton dynamics and its impact on cell biology is of vital importance. In this chapter, we provide an overview of some of the methods used to image cytoskeleton dynamics in live cells, placing an emphasis on recent advances in the visualization of the MT and the actin cytoskeleton in multicellular organisms.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans ; Cell Tracking/methods ; Cytoskeleton/metabolism ; Green Fluorescent Proteins ; HEK293 Cells ; Humans ; Microscopy, Fluorescence ; Microtubule-Associated Proteins/genetics ; Microtubules/metabolism ; Peptides
Chemical Substances	EB1 microtubule binding proteins ; Microtubule-Associated Proteins ; Peptides ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2012
Publishing country	United States
Document type	Journal Article
ISSN	1557-7988 ; 0076-6879
ISSN (online)	1557-7988
ISSN	0076-6879
DOI	10.1016/B978-0-12-388448-0.00019-X
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Article: The cell migration molecule UNC-53/NAV2 is linked to the ARP2/3 complex by ABI-1.

Schmidt, Kristopher L / Marcus-Gueret, Nancy / Adeleye, Adetayo / Webber, Jordan / Baillie, David / Stringham, Eve G

Development (Cambridge, England)

2009 Volume 136, Issue 4, Page(s) 563–574

Abstract: The shape changes that are required to position a cell to migrate or grow out in a particular direction involve a coordinated reorganization of the actin cytoskeleton. Although it is known that the ARP2/3 complex nucleates actin filament assembly, ... ...

Abstract	The shape changes that are required to position a cell to migrate or grow out in a particular direction involve a coordinated reorganization of the actin cytoskeleton. Although it is known that the ARP2/3 complex nucleates actin filament assembly, exactly how the information from guidance cues is integrated to elicit ARP2/3-mediated remodeling during outgrowth remains vague. Previous studies have shown that C. elegans UNC-53 and its vertebrate homolog NAV (Neuronal Navigators) are required for the migration of cells and neuronal processes. We have identified ABI-1 as a novel molecular partner of UNC-53/NAV2 and have found that a restricted calponin homology (CH) domain of UNC-53 is sufficient to bind ABI-1. ABI-1 and UNC-53 have an overlapping expression pattern, and display similar cell migration phenotypes in the excretory cell, and in mechanosensory and motoneurons. Migration defects were also observed after RNAi of proteins known to function with abi-1 in actin dynamics, including nck-1, wve-1 and arx-2. We propose that UNC-53/NAV2, through its CH domain, acts as a scaffold that links ABI-1 to the ARP2/3 complex to regulate actin cytoskeleton remodeling.
MeSH term(s)	Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Amino Acid Sequence ; Animals ; Axons/metabolism ; Body Patterning ; Caenorhabditis elegans/cytology ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Movement ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Green Fluorescent Proteins/metabolism ; Microfilament Proteins/chemistry ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Motor Neurons/cytology ; Motor Neurons/metabolism ; Mutation/genetics ; Phenotype ; Protein Binding ; Protein Isoforms/metabolism ; Protein Structure, Tertiary ; RNA Interference
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; Caenorhabditis elegans Proteins ; Cytoskeletal Proteins ; Microfilament Proteins ; Protein Isoforms ; UNC-53 protein, C elegans ; abi-1 protein, C elegans ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2009-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.016816
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Article ; Online: Abelson interactor-1 (ABI-1) interacts with MRL adaptor protein MIG-10 and is required in guided cell migrations and process outgrowth in C. elegans.

McShea, Molly A / Schmidt, Kristopher L / Dubuke, Michelle L / Baldiga, Christina E / Sullender, Meagan E / Reis, Andrea L / Zhang, Subaiou / O'Toole, Sean M / Jeffers, Mary C / Warden, Rachel M / Kenney, Allison H / Gosselin, Jennifer / Kuhlwein, Mark / Hashmi, Sana K / Stringham, Eve G / Ryder, Elizabeth F

Developmental biology

2012 Volume 373, Issue 1, Page(s) 1–13

Abstract: Directed cell migration and process outgrowth are vital to proper development of many metazoan tissues. These processes are dependent on reorganization of the actin cytoskeleton in response to external guidance cues. During development of the nervous ... ...

Abstract	Directed cell migration and process outgrowth are vital to proper development of many metazoan tissues. These processes are dependent on reorganization of the actin cytoskeleton in response to external guidance cues. During development of the nervous system, the MIG-10/RIAM/Lamellipodin (MRL) signaling proteins are thought to transmit positional information from surface guidance cues to the actin polymerization machinery, and thus to promote polarized outgrowth of axons. In C. elegans, mutations in the MRL family member gene mig-10 result in animals that have defects in axon guidance, neuronal migration, and the outgrowth of the processes or 'canals' of the excretory cell, which is required for osmoregulation in the worm. In addition, mig-10 mutant animals have recently been shown to have defects in clustering of vesicles at the synapse. To determine additional molecular partners of MIG-10, we conducted a yeast two-hybrid screen using isoform MIG-10A as bait and isolated Abelson-interactor protein-1 (ABI-1). ABI-1, a downstream target of Abl non-receptor tyrosine kinase, is a member of the WAVE regulatory complex (WRC) involved in the initiation of actin polymerization. Further analysis using a co-immunoprecipitation system confirmed the interaction of MIG-10 and ABI-1 and showed that it requires the SH3 domain of ABI-1. Single mutants for mig-10 and abi-1 displayed similar phenotypes of incomplete migration of the ALM neurons and truncated outgrowth of the excretory cell canals, suggesting that the ABI-1/MIG-10 interaction is relevant in vivo. Cell autonomous expression of MIG-10 isoforms rescued both the neuronal migration and the canal outgrowth defects, showing that MIG-10 functions autonomously in the ALM neurons and the excretory cell. These results suggest that MIG-10 and ABI-1 interact physically to promote cell migration and process outgrowth in vivo. In the excretory canal, ABI-1 is thought to act downstream of UNC-53/NAV2, linking this large scaffolding protein to actin polymerization during excretory canal outgrowth. abi-1(RNAi) enhanced the excretory canal truncation observed in mig-10 mutants, while double mutant analysis between unc-53 and mig-10 showed no increased truncation of the posterior canal beyond that observed in mig-10 mutants. Morphological analysis of mig-10 and unc-53 mutants showed that these genes regulate canal diameter as well as its length, suggesting that defective lumen formation may be linked to the ability of the excretory canal to grow out longitudinally. Taken together, our results suggest that MIG-10, UNC-53, and ABI-1 act sequentially to mediate excretory cell process outgrowth.
MeSH term(s)	Analysis of Variance ; Animals ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Movement/physiology ; Cell Surface Extensions/physiology ; Cytoskeletal Proteins/metabolism ; Immunoprecipitation ; Microfilament Proteins/metabolism ; Mutation/genetics ; Nervous System/embryology ; RNA Interference ; Two-Hybrid System Techniques
Chemical Substances	Caenorhabditis elegans Proteins ; Cytoskeletal Proteins ; Microfilament Proteins ; Mig-10 protein, C elegans ; UNC-53 protein, C elegans ; abi-1 protein, C elegans
Language	English
Publishing date	2012-09-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2012.09.017
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Journal: Transgenic hsp16-lacZ Strains of the Soil Nematode Caenorhabditis elegans as Biological Monitors of Environmental Stress

Stringham, Eve G. / Candido, E. P. M.

Environmental Toxicology and Chemistry

1994 Volume 13, Page(s) 1211–1220

Abstract: Es wurden stabile transgene Linien der Nematode Caenorhabiditis elegans abgeleitet, die Fusionen der hsp16-Gene (codieren fuer eine Familie stressinduzierbarer 16 kDa-Proteine) mit lacZ-Reportergenen von Escherichia coli enthalten. Diese Staemme ... ...

Abstract	Es wurden stabile transgene Linien der Nematode Caenorhabiditis elegans abgeleitet, die Fusionen der hsp16-Gene (codieren fuer eine Familie stressinduzierbarer 16 kDa-Proteine) mit lacZ-Reportergenen von Escherichia coli enthalten. Diese Staemme exprimieren als Reaktion auf Hitzeschock oder eine Reihe chemischer Stressfaktoren erhoehte beta-Galactosidase-Spiegel im Zellkern. Als Stressausloeser wurden die Ionen Cd(2+), Cu(2+), Hg(2+), Pb(2+), Zn(2+), Arsenat sowie das Herbizid Paraquad in die Untersuchungen einbezogen. Einige der Reagenzien bewirken hierbei spezifische Gewebeveraenderungen (Pb(2+) und Cd(2+) im Schlund, Hg(2+) im Intestinaltrakt);dies legt nahe, dass das getestete Biomonitoring-System auch zur selektiven Detektion von Kontaminanten in Gemischen geeignet sein koennte. Eine effektive, kostenguenstige Assay-Methode zur Quantifizierung der beta-Galactosidaseproduktion wurde entwickelt. Die beschriebene Induktion erfolgte generell bereits unterhalb der LC50 der Testsubstanz.
Keywords	Biomonitoring ; Testsubstanz ; Chemikalien ; Gentechnik ; Gen ; Gewebe ; Schadstoffwirkung ; Protein ; Arsenat ; Stress ; Ionen ; Stoffgemisch ; LC 50 ; Herbizid ; Nematoden ; Zellkern ; Gentechnisch veraenderte Organismen ; Bodenorganismen ; Cadmium ; Kupfer ; Quecksilber ; Blei ; Zink ; Arsen ; Schadstoffexposition ; Biotest ; Expositionsdauer ; Genexpression ; Enzym ; Enzymaktivitaet
Language	English
Document type	Journal
Database	OPAC and Environmental database (ULIDAT) of The Federal Environment Agency (UBA)

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Article: X-linked recessive atrophic macular degeneration from RPGR mutation.

Ayyagari, Radha / Demirci, F Yesim / Liu, Jiafan / Bingham, Eve L / Stringham, Heather / Kakuk, Laura E / Boehnke, Michael / Gorin, Michael B / Richards, Julia E / Sieving, Paul A

Genomics

2002 Volume 80, Issue 2, Page(s) 166–171

Abstract: ... including X-linked cone dystrophy (COD1). The RPGR gene nonsense mutation G-->T at open reading frame (ORF ...

Abstract	We mapped a new X-linked recessive atrophic macular degeneration locus to Xp21.1-p11.4 and show allelic involvement of the gene RPGR, which normally causes severe peripheral retinal degeneration leading to global blindness. Ten affected males whom we examined had primarily macular atrophy causing progressive loss of visual acuity with minimal peripheral visual impairment. One additional male showed extensive macular degeneration plus peripheral loss of retinal pigment epithelium and choriocapillaries. Full-field electroretinograms (ERGs) showed normal cone and rod responses in some affected males despite advanced macular degeneration, emphasizing the dissociation of atrophic macular degeneration from generalized cone degenerations, including X-linked cone dystrophy (COD1). The RPGR gene nonsense mutation G-->T at open reading frame (ORF)15+1164 cosegregated with the disease and may create a donor splice site. Identification of an RPGR mutation in atrophic maculardegeneration expands the phenotypic range associated with this gene and provides a new tool for the dissection of the relationship between clinically different retinal pathologies.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Carrier Proteins/genetics ; Chromosomes, Human, X ; Codon, Nonsense ; Eye Proteins ; Female ; Genes, Recessive ; Heterozygote ; Humans ; Macular Degeneration/genetics ; Macular Degeneration/physiopathology ; Male ; Middle Aged ; Retina/pathology ; Sequence Analysis, DNA
Chemical Substances	Carrier Proteins ; Codon, Nonsense ; Eye Proteins ; RPGR protein, human
Language	English
Publishing date	2002-02-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	356334-0
ISSN	1089-8646 ; 0888-7543
ISSN (online)	1089-8646
ISSN	0888-7543
DOI	10.1006/geno.2002.6815
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Article: Abelson interactor-1 (ABI-1) interacts with MRL adaptor protein MIG-10 and is required in guided cell migrations and process outgrowth in C. elegans

McShea, Molly A. / Schmidt, Kristopher L. / Dubuke, Michelle L. / Baldiga, Christina E. / Sullender, Meagan E. / Reis, Andrea L. / Zhang, Subaiou / O'Toole, Sean M. / Jeffers, Mary C. / Warden, Rachel M. / Kenney, Allison H. / Gosselin, Jennifer / Kuhlwein, Mark / Hashmi, Sana K. / Stringham, Eve G. / Ryder, Elizabeth F.

Developmental biology

Volume v. 373,, Issue no. 1

Abstract	Directed cell migration and process outgrowth are vital to proper development of many metazoan tissues. These processes are dependent on reorganization of the actin cytoskeleton in response to external guidance cues. During development of the nervous system, the MIG-10/RIAM/Lamellipodin (MRL) signaling proteins are thought to transmit positional information from surface guidance cues to the actin polymerization machinery, and thus to promote polarized outgrowth of axons. In C. elegans, mutations in the MRL family member gene mig-10 result in animals that have defects in axon guidance, neuronal migration, and the outgrowth of the processes or ‘canals’ of the excretory cell, which is required for osmoregulation in the worm. In addition, mig-10 mutant animals have recently been shown to have defects in clustering of vesicles at the synapse. To determine additional molecular partners of MIG-10, we conducted a yeast two-hybrid screen using isoform MIG-10A as bait and isolated Abelson-interactor protein-1 (ABI-1). ABI-1, a downstream target of Abl non-receptor tyrosine kinase, is a member of the WAVE regulatory complex (WRC) involved in the initiation of actin polymerization. Further analysis using a co-immunoprecipitation system confirmed the interaction of MIG-10 and ABI-1 and showed that it requires the SH3 domain of ABI-1. Single mutants for mig-10 and abi-1 displayed similar phenotypes of incomplete migration of the ALM neurons and truncated outgrowth of the excretory cell canals, suggesting that the ABI-1/MIG-10 interaction is relevant in vivo. Cell autonomous expression of MIG-10 isoforms rescued both the neuronal migration and the canal outgrowth defects, showing that MIG-10 functions autonomously in the ALM neurons and the excretory cell. These results suggest that MIG-10 and ABI-1 interact physically to promote cell migration and process outgrowth in vivo. In the excretory canal, ABI-1 is thought to act downstream of UNC-53/NAV2, linking this large scaffolding protein to actin polymerization during excretory canal outgrowth. abi-1(RNAi) enhanced the excretory canal truncation observed in mig-10 mutants, while double mutant analysis between unc-53 and mig-10 showed no increased truncation of the posterior canal beyond that observed in mig-10 mutants. Morphological analysis of mig-10 and unc-53 mutants showed that these genes regulate canal diameter as well as its length, suggesting that defective lumen formation may be linked to the ability of the excretory canal to grow out longitudinally. Taken together, our results suggest that MIG-10, UNC-53, and ABI-1 act sequentially to mediate excretory cell process outgrowth.
Keywords	animals ; Animalia ; actin ; axons ; genes ; osmoregulation ; mutation ; polymerization ; phenotype ; two hybrid system techniques ; RNA interference ; mutants ; neurodevelopment ; tyrosine ; cell movement ; scaffolding proteins ; microfilaments ; synapse ; tissues
Language	English
Document type	Article
ISSN	0012-1606
Database	AGRIS - International Information System for the Agricultural Sciences and Technology

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Article ; Online: Navigating the cell: UNC-53 and the navigators, a family of cytoskeletal regulators with multiple roles in cell migration, outgrowth and trafficking.

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Article ; Online: Distinct cell guidance pathways controlled by the Rac and Rho GEF domains of UNC-73/TRIO in Caenorhabditis elegans.

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Article ; Online: Live cell imaging of the cytoskeleton.

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Article: The cell migration molecule UNC-53/NAV2 is linked to the ARP2/3 complex by ABI-1.

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Article ; Online: Abelson interactor-1 (ABI-1) interacts with MRL adaptor protein MIG-10 and is required in guided cell migrations and process outgrowth in C. elegans.

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Journal: Transgenic hsp16-lacZ Strains of the Soil Nematode Caenorhabditis elegans as Biological Monitors of Environmental Stress

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Article: X-linked recessive atrophic macular degeneration from RPGR mutation.

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Article: Abelson interactor-1 (ABI-1) interacts with MRL adaptor protein MIG-10 and is required in guided cell migrations and process outgrowth in C. elegans

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