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Article: Linking Heterochromatin Protein 1 (HP1) to cancer progression.

Dialynas, George K / Vitalini, Michael W / Wallrath, Lori L

2008 Volume 647, Issue 1-2, Page(s) 13–20

Abstract: All cells of a given organism contain nearly identical genetic information, yet tissues display unique gene expression profiles. This specificity is in part due to transcriptional control by epigenetic mechanisms that involve post-translational ... ...

Abstract	All cells of a given organism contain nearly identical genetic information, yet tissues display unique gene expression profiles. This specificity is in part due to transcriptional control by epigenetic mechanisms that involve post-translational modifications of histones. These modifications affect the folding of the chromatin fiber and serve as binding sites for non-histone chromosomal proteins. Here we discuss functions of the Heterochromatin Protein 1 (HP1) family of proteins that recognize H3K9me, an epigenetic mark generated by the histone methyltransferases SU(VAR)3-9 and orthologues. Loss of HP1 proteins causes chromosome segregation defects and lethality in some organisms; a reduction in levels of HP1 family members is associated with cancer progression in humans. These consequences are likely due to the role of HP1 in centromere stability, telomere capping and the regulation of euchromatic and heterochromatic gene expression.
MeSH term(s)	Animals ; Centromere/metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/physiology ; Disease Progression ; Gene Expression Regulation ; Heterochromatin ; Humans ; Models, Genetic ; Neoplasms/genetics ; Neoplasms/metabolism ; Telomere/metabolism ; Viruses/metabolism
Chemical Substances	Chromatin ; Chromosomal Proteins, Non-Histone ; Heterochromatin ; heterochromatin-specific nonhistone chromosomal protein HP-1 (107283-02-3)
Language	English
Publishing date	2008-12-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	206607-5
ISSN	1873-135X ; 0027-5107 ; 1383-5718 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
ISSN (online)	1873-135X
ISSN	0027-5107 ; 1383-5718 ; 0165-1110 ; 0165-1161 ; 0165-7992 ; 0921-8777 ; 0165-1218 ; 1383-5726 ; 0167-8817 ; 0921-8734 ; 1383-5742
DOI	10.1016/j.mrfmmm.2008.09.007
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Article ; Online: The role of Drosophila Lamin C in muscle function and gene expression.

Dialynas, George / Speese, Sean / Budnik, Vivian / Geyer, Pamela K / Wallrath, Lori L

Development (Cambridge, England)

2010 Volume 137, Issue 18, Page(s) 3067–3077

Abstract: The inner side of the nuclear envelope (NE) is lined with lamins, a meshwork of intermediate filaments that provides structural support for the nucleus and plays roles in many nuclear processes. Lamins, classified as A- or B-types on the basis of ... ...

Abstract	The inner side of the nuclear envelope (NE) is lined with lamins, a meshwork of intermediate filaments that provides structural support for the nucleus and plays roles in many nuclear processes. Lamins, classified as A- or B-types on the basis of biochemical properties, have a conserved globular head, central rod and C-terminal domain that includes an Ig-fold structural motif. In humans, mutations in A-type lamins give rise to diseases that exhibit tissue-specific defects, such as Emery-Dreifuss muscular dystrophy. Drosophila is being used as a model to determine tissue-specific functions of A-type lamins in development, with implications for understanding human disease mechanisms. The GAL4-UAS system was used to express wild-type and mutant forms of Lamin C (the presumed Drosophila A-type lamin), in an otherwise wild-type background. Larval muscle-specific expression of wild type Drosophila Lamin C caused no overt phenotype. By contrast, larval muscle-specific expression of a truncated form of Lamin C lacking the N-terminal head (Lamin C DeltaN) caused muscle defects and semi-lethality, with adult 'escapers' possessing malformed legs. The leg defects were due to a lack of larval muscle function and alterations in hormone-regulated gene expression. The consequences of Lamin C association at a gene were tested directly by targeting a Lamin C DNA-binding domain fusion protein upstream of a reporter gene. Association of Lamin C correlated with localization of the reporter gene at the nuclear periphery and gene repression. These data demonstrate connections among the Drosophila A-type lamin, hormone-induced gene expression and muscle function.
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; Drosophila melanogaster/anatomy & histology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/physiology ; Ecdysone/metabolism ; Gene Expression Regulation, Developmental ; Lamin Type A/genetics ; Lamin Type A/metabolism ; Muscles/physiopathology ; Signal Transduction
Chemical Substances	Lamin Type A ; lamin C ; Ecdysone (3604-87-3)
Language	English
Publishing date	2010-08-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.048231
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Article ; Online: Myopathic lamin mutations cause reductive stress and activate the nrf2/keap-1 pathway.

Dialynas, George / Shrestha, Om K / Ponce, Jessica M / Zwerger, Monika / Thiemann, Dylan A / Young, Grant H / Moore, Steven A / Yu, Liping / Lammerding, Jan / Wallrath, Lori L

PLoS genetics

2015 Volume 11, Issue 5, Page(s) e1005231

Abstract: Mutations in the human LMNA gene cause muscular dystrophy by mechanisms that are incompletely understood. The LMNA gene encodes A-type lamins, intermediate filaments that form a network underlying the inner nuclear membrane, providing structural support ... ...

Abstract	Mutations in the human LMNA gene cause muscular dystrophy by mechanisms that are incompletely understood. The LMNA gene encodes A-type lamins, intermediate filaments that form a network underlying the inner nuclear membrane, providing structural support for the nucleus and organizing the genome. To better understand the pathogenesis caused by mutant lamins, we performed a structural and functional analysis on LMNA missense mutations identified in muscular dystrophy patients. These mutations perturb the tertiary structure of the conserved A-type lamin Ig-fold domain. To identify the effects of these structural perturbations on lamin function, we modeled these mutations in Drosophila Lamin C and expressed the mutant lamins in muscle. We found that the structural perturbations had minimal dominant effects on nuclear stiffness, suggesting that the muscle pathology was not accompanied by major structural disruption of the peripheral nuclear lamina. However, subtle alterations in the lamina network and subnuclear reorganization of lamins remain possible. Affected muscles had cytoplasmic aggregation of lamins and additional nuclear envelope proteins. Transcription profiling revealed upregulation of many Nrf2 target genes. Nrf2 is normally sequestered in the cytoplasm by Keap-1. Under oxidative stress Nrf2 dissociates from Keap-1, translocates into the nucleus, and activates gene expression. Unexpectedly, biochemical analyses revealed high levels of reducing agents, indicative of reductive stress. The accumulation of cytoplasmic lamin aggregates correlated with elevated levels of the autophagy adaptor p62/SQSTM1, which also binds Keap-1, abrogating Nrf2 cytoplasmic sequestration, allowing Nrf2 nuclear translocation and target gene activation. Elevated p62/SQSTM1 and nuclear enrichment of Nrf2 were identified in muscle biopsies from the corresponding muscular dystrophy patients, validating the disease relevance of our Drosophila model. Thus, novel connections were made between mutant lamins and the Nrf2 signaling pathway, suggesting new avenues of therapeutic intervention that include regulation of protein folding and metabolism, as well as maintenance of redox homoeostasis.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Nucleus ; Drosophila/genetics ; Drosophila/metabolism ; Gene Expression Profiling ; Gene Expression Regulation ; Homeostasis ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Kelch-Like ECH-Associated Protein 1 ; Lamin Type A/genetics ; Lamin Type A/metabolism ; Muscle, Skeletal/metabolism ; Muscular Dystrophies/genetics ; Mutation ; NF-E2-Related Factor 2/genetics ; NF-E2-Related Factor 2/metabolism ; Nuclear Lamina/genetics ; Nuclear Lamina/metabolism ; Oxidative Stress ; Protein Conformation ; Protein Folding ; Sequestosome-1 Protein ; Signal Transduction
Chemical Substances	Adaptor Proteins, Signal Transducing ; Intracellular Signaling Peptides and Proteins ; KEAP1 protein, human ; Kelch-Like ECH-Associated Protein 1 ; LMNA protein, human ; Lamin Type A ; NF-E2-Related Factor 2 ; NFE2L2 protein, human ; SQSTM1 protein, human ; Sequestosome-1 Protein ; lamin C
Language	English
Publishing date	2015-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1005231
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Article: Plasticity of HP1 proteins in mammalian cells.

Dialynas, George K / Terjung, Stefan / Brown, Jeremy P / Aucott, Rebecca L / Baron-Luhr, Bettina / Singh, Prim B / Georgatos, Spyros D

Journal of cell science

2007 Volume 120, Issue Pt 19, Page(s) 3415–3424

Abstract: We have compared the distribution of endogenous heterochromatin protein 1 (HP1) proteins (alpha, beta and gamma) in different epithelial lines, pluripotent stem cells and embryonic fibroblasts. In parallel, we have interrogated assembly and dynamics of ... ...

Abstract	We have compared the distribution of endogenous heterochromatin protein 1 (HP1) proteins (alpha, beta and gamma) in different epithelial lines, pluripotent stem cells and embryonic fibroblasts. In parallel, we have interrogated assembly and dynamics of newly expressed HP1-GFP proteins in cells lacking both HP1alpha and HP1beta alleles, blocked at the G1-S boundary, or cultured in the presence of HDAC and HAT inhibitors. The results reveal a range of cell type and differentiation state-specific patterns that do not correlate with 'fast' or 'slow' subunit exchange in heterochromatin. Furthermore, our observations show that targeting of HP1gamma to heterochromatic sites depends on HP1alpha and H1beta and that, on an architectural level, HP1alpha is the most polymorphic variant of the HP1 family. These data provide evidence for HP1 plasticity under shifting microenvironmental conditions and offer a new conceptual framework for understanding chromatin dynamics at the molecular level.
MeSH term(s)	Animals ; Cell Line ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Epithelial Cells/cytology ; Epithelial Cells/physiology ; Fibroblasts/cytology ; Fibroblasts/physiology ; Heterochromatin/metabolism ; Humans ; Mice ; Pluripotent Stem Cells/cytology ; Pluripotent Stem Cells/physiology ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Chromosomal Proteins, Non-Histone ; Heterochromatin ; Protein Isoforms ; Recombinant Fusion Proteins ; heterochromatin-specific nonhistone chromosomal protein HP-1 (107283-02-3)
Language	English
Publishing date	2007-10-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.012914
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Article: Methylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatin.

Dialynas, George K / Makatsori, Dimitra / Kourmouli, Niki / Theodoropoulos, Panayiotis A / McLean, Kevin / Terjung, Stefan / Singh, Prim B / Georgatos, Spyros D

The Journal of biological chemistry

2006 Volume 281, Issue 20, Page(s) 14350–14360

Abstract: We have examined HP1beta-chromatin interactions in different molecular contexts in vitro and in vivo. Employing purified components we show that HP1beta exhibits selective, stoichiometric, and salt-resistant binding to recombinant histone H3, associating ...

Abstract	We have examined HP1beta-chromatin interactions in different molecular contexts in vitro and in vivo. Employing purified components we show that HP1beta exhibits selective, stoichiometric, and salt-resistant binding to recombinant histone H3, associating primarily with the helical "histone fold" domain. Furthermore, using "bulk" nucleosomes released by MNase digestion, S-phase extracts, and fragments of peripheral heterochromatin, we demonstrate that HP1beta associates more tightly with destabilized or disrupted nucleosomes (H3/H4 subcomplexes) than with intact particles. Western blotting and mass spectrometry data indicate that HP1beta-selected H3/H4 particles and subparticles possess a complex pattern of posttranslational modifications but are not particularly enriched in me3K9-H3. Consistent with these results, mapping of HP1beta and me3K9-H3 sites in vivo reveals overlapping, yet spatially distinct patterns, while transient transfection assays with synchronized cells show that stable incorporation of HP1beta-gfp into heterochromatin requires passage through the S-phase. The data amassed challenge the dogma that me3K9H3 is necessary and sufficient for HP1 binding and unveil a new mode of HP1-chromatin interactions.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Cycle ; Cell Nucleus/metabolism ; Chromosomal Proteins, Non-Histone/chemistry ; Dogs ; HeLa Cells ; Heterochromatin/chemistry ; Histones/chemistry ; Humans ; Methylation ; Molecular Sequence Data ; Protein Binding ; Rats
Chemical Substances	Chromosomal Proteins, Non-Histone ; Heterochromatin ; Histones ; heterochromatin-specific nonhistone chromosomal protein HP-1 (107283-02-3)
Language	English
Publishing date	2006-03-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M600558200
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Article: Plasticity of HP1 proteins in mammalian cells

Dialynas, George K / Terjung, Stefan / Brown, Jeremy P / Aucott, Rebecca L / Baron-Luhr, Bettina / Singh, Prim B / Georgatos, Spyros D

Journal of cell science. 2007 Oct. 1, v. 120, no. 19

2007

Abstract: We have compared the distribution of endogenous heterochromatin protein 1 (HP1) proteins (α, β and γ) in different epithelial lines, pluripotent stem cells and embryonic fibroblasts. In parallel, we have interrogated assembly and dynamics of newly ... ...

Abstract	We have compared the distribution of endogenous heterochromatin protein 1 (HP1) proteins (α, β and γ) in different epithelial lines, pluripotent stem cells and embryonic fibroblasts. In parallel, we have interrogated assembly and dynamics of newly expressed HP1-GFP proteins in cells lacking both HP1α and HP1β alleles, blocked at the G1-S boundary, or cultured in the presence of HDAC and HAT inhibitors. The results reveal a range of cell type and differentiation state-specific patterns that do not correlate with `fast' or `slow' subunit exchange in heterochromatin. Furthermore, our observations show that targeting of HP1γ to heterochromatic sites depends on HP1α and H1β and that, on an architectural level, HP1α is the most polymorphic variant of the HP1 family. These data provide evidence for HP1 plasticity under shifting microenvironmental conditions and offer a new conceptual framework for understanding chromatin dynamics at the molecular level.
Language	English
Dates of publication	2007-1001
Size	p. 3415-3424.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
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Article ; Online: A comparative study of Drosophila and human A-type lamins.

Schulze, Sandra R / Curio-Penny, Beatrice / Speese, Sean / Dialynas, George / Cryderman, Diane E / McDonough, Caitrin W / Nalbant, Demet / Petersen, Melissa / Budnik, Vivian / Geyer, Pamela K / Wallrath, Lori L

PloS one

2009 Volume 4, Issue 10, Page(s) e7564

Abstract: Nuclear intermediate filament proteins, called lamins, form a meshwork that lines the inner surface of the nuclear envelope. Lamins contain three domains: an N-terminal head, a central rod and a C-terminal tail domain possessing an Ig-fold structural ... ...

Abstract	Nuclear intermediate filament proteins, called lamins, form a meshwork that lines the inner surface of the nuclear envelope. Lamins contain three domains: an N-terminal head, a central rod and a C-terminal tail domain possessing an Ig-fold structural motif. Lamins are classified as either A- or B-type based on structure and expression pattern. The Drosophila genome possesses two genes encoding lamins, Lamin C and lamin Dm(0), which have been designated A- and B-type, respectively, based on their expression profile and structural features. In humans, mutations in the gene encoding A-type lamins are associated with a spectrum of predominantly tissue-specific diseases known as laminopathies. Linking the disease phenotypes to cellular functions of lamins has been a major challenge. Drosophila is being used as a model system to identify the roles of lamins in development. Towards this end, we performed a comparative study of Drosophila and human A-type lamins. Analysis of transgenic flies showed that human lamins localize predictably within the Drosophila nucleus. Consistent with this finding, yeast two-hybrid data demonstrated conservation of partner-protein interactions. Drosophila lacking A-type lamin show nuclear envelope defects similar to those observed with human laminopathies. Expression of mutant forms of the A-type Drosophila lamin modeled after human disease-causing amino acid substitutions revealed an essential role for the N-terminal head and the Ig-fold in larval muscle tissue. This tissue-restricted sensitivity suggests a conserved role for lamins in muscle biology. In conclusion, we show that (1) localization of A-type lamins and protein-partner interactions are conserved between Drosophila and humans, (2) loss of the Drosophila A-type lamin causes nuclear defects and (3) muscle tissue is sensitive to the expression of mutant forms of A-type lamin modeled after those causing disease in humans. These studies provide new insights on the role of lamins in nuclear biology and support Drosophila as a model for studies of human laminopathies involving muscle dysfunction.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Cell Nucleus/metabolism ; Drosophila melanogaster ; Gene Expression Regulation ; Humans ; Lamin Type A/biosynthesis ; Lamin Type A/chemistry ; Lamin Type A/genetics ; Lamin Type A/metabolism ; Muscles/pathology ; Mutation ; Nuclear Envelope/metabolism ; Tissue Distribution ; Two-Hybrid System Techniques
Chemical Substances	Lamin Type A ; lamin C
Language	English
Publishing date	2009-10-26
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0007564
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Article ; Online: A comparative study of Drosophila and human A-type lamins.

Sandra R Schulze / Beatrice Curio-Penny / Sean Speese / George Dialynas / Diane E Cryderman / Caitrin W McDonough / Demet Nalbant / Melissa Petersen / Vivian Budnik / Pamela K Geyer / Lori L Wallrath

PLoS ONE, Vol 4, Iss 10, p e

2009 Volume 7564

Abstract	Nuclear intermediate filament proteins, called lamins, form a meshwork that lines the inner surface of the nuclear envelope. Lamins contain three domains: an N-terminal head, a central rod and a C-terminal tail domain possessing an Ig-fold structural motif. Lamins are classified as either A- or B-type based on structure and expression pattern. The Drosophila genome possesses two genes encoding lamins, Lamin C and lamin Dm(0), which have been designated A- and B-type, respectively, based on their expression profile and structural features. In humans, mutations in the gene encoding A-type lamins are associated with a spectrum of predominantly tissue-specific diseases known as laminopathies. Linking the disease phenotypes to cellular functions of lamins has been a major challenge. Drosophila is being used as a model system to identify the roles of lamins in development. Towards this end, we performed a comparative study of Drosophila and human A-type lamins. Analysis of transgenic flies showed that human lamins localize predictably within the Drosophila nucleus. Consistent with this finding, yeast two-hybrid data demonstrated conservation of partner-protein interactions. Drosophila lacking A-type lamin show nuclear envelope defects similar to those observed with human laminopathies. Expression of mutant forms of the A-type Drosophila lamin modeled after human disease-causing amino acid substitutions revealed an essential role for the N-terminal head and the Ig-fold in larval muscle tissue. This tissue-restricted sensitivity suggests a conserved role for lamins in muscle biology. In conclusion, we show that (1) localization of A-type lamins and protein-partner interactions are conserved between Drosophila and humans, (2) loss of the Drosophila A-type lamin causes nuclear defects and (3) muscle tissue is sensitive to the expression of mutant forms of A-type lamin modeled after those causing disease in humans. These studies provide new insights on the role of lamins in nuclear biology and support Drosophila as a model ...
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2009-10-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Audio / Video: A Comparative Study of Drosophila and Human A-Type Lamins

PloS one. 2009 Oct., v. 4, no. 10

2009

Abstract	Nuclear intermediate filament proteins, called lamins, form a meshwork that lines the inner surface of the nuclear envelope. Lamins contain three domains: an N-terminal head, a central rod and a C-terminal tail domain possessing an Ig-fold structural motif. Lamins are classified as either A- or B-type based on structure and expression pattern. The Drosophila genome possesses two genes encoding lamins, Lamin C and lamin Dm(0), which have been designated A- and B-type, respectively, based on their expression profile and structural features. In humans, mutations in the gene encoding A-type lamins are associated with a spectrum of predominantly tissue-specific diseases known as laminopathies. Linking the disease phenotypes to cellular functions of lamins has been a major challenge. Drosophila is being used as a model system to identify the roles of lamins in development. Towards this end, we performed a comparative study of Drosophila and human A-type lamins. Analysis of transgenic flies showed that human lamins localize predictably within the Drosophila nucleus. Consistent with this finding, yeast two-hybrid data demonstrated conservation of partner-protein interactions. Drosophila lacking A-type lamin show nuclear envelope defects similar to those observed with human laminopathies. Expression of mutant forms of the A-type Drosophila lamin modeled after human disease-causing amino acid substitutions revealed an essential role for the N-terminal head and the Ig-fold in larval muscle tissue. This tissue-restricted sensitivity suggests a conserved role for lamins in muscle biology. In conclusion, we show that (1) localization of A-type lamins and protein-partner interactions are conserved between Drosophila and humans, (2) loss of the Drosophila A-type lamin causes nuclear defects and (3) muscle tissue is sensitive to the expression of mutant forms of A-type lamin modeled after those causing disease in humans. These studies provide new insights on the role of lamins in nuclear biology and support Drosophila as a model for studies of human laminopathies involving muscle dysfunction.
Keywords	Drosophila melanogaster ; insect proteins ; nuclear membrane ; genes ; mutation ; mutants ; phenotype ; cytochemistry ; cell nucleus ; larval development ; muscles ; species differences ; humans
Language	English
Dates of publication	2009-10
Document type	Article ; Audio / Video
ZDB-ID	2267670-3
ISSN	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0007564
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Article ; Online: VectorBase: a data resource for invertebrate vector genomics.

Lawson, Daniel / Arensburger, Peter / Atkinson, Peter / Besansky, Nora J / Bruggner, Robert V / Butler, Ryan / Campbell, Kathryn S / Christophides, George K / Christley, Scott / Dialynas, Emmanuel / Hammond, Martin / Hill, Catherine A / Konopinski, Nathan / Lobo, Neil F / MacCallum, Robert M / Madey, Greg / Megy, Karine / Meyer, Jason / Redmond, Seth /

Severson, David W / Stinson, Eric O / Topalis, Pantelis / Birney, Ewan / Gelbart, William M / Kafatos, Fotis C / Louis, Christos / Collins, Frank H

Nucleic acids research

2008 Volume 37, Issue Database issue, Page(s) D583–7

Abstract: VectorBase (http://www.vectorbase.org) is an NIAID-funded Bioinformatic Resource Center focused on invertebrate vectors of human pathogens. VectorBase annotates and curates vector genomes providing a web accessible integrated resource for the research ... ...

Abstract	VectorBase (http://www.vectorbase.org) is an NIAID-funded Bioinformatic Resource Center focused on invertebrate vectors of human pathogens. VectorBase annotates and curates vector genomes providing a web accessible integrated resource for the research community. Currently, VectorBase contains genome information for three mosquito species: Aedes aegypti, Anopheles gambiae and Culex quinquefasciatus, a body louse Pediculus humanus and a tick species Ixodes scapularis. Since our last report VectorBase has initiated a community annotation system, a microarray and gene expression repository and controlled vocabularies for anatomy and insecticide resistance. We have continued to develop both the software infrastructure and tools for interrogating the stored data.
MeSH term(s)	Aedes/genetics ; Animals ; Anopheles/genetics ; Arthropod Vectors/genetics ; Culex/genetics ; Culicidae/genetics ; Culicidae/metabolism ; Databases, Genetic ; Gene Expression Profiling ; Genome, Insect ; Genomics ; Ixodes/genetics ; Pediculus/genetics ; Vocabulary, Controlled
Language	English
Publishing date	2008-11-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkn857
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