odd Oz: A novel Drosophila pair rule gene

Levine, Anna; Bashan-Ahrend, Ayelet; Budai-Hadrian, Ofra; Gartenberg, Devorah; Menasherow, Sophia; Wides, Ron

doi:10.1016/0092-8674(94)90220-8

Cited by 142 publications

(176 citation statements)

References 35 publications

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“…The name is derived from the odd oz phenotype (hence the name odz) observed in odz mutants, in which the odd-numbered body segments are deleted, and from the simultaneous independent cloning of this gene as a potential invertebrate ortholog of glycoprotein tenascin-C (hence the other name tenascin-like molecule major, or ten-m). 18,19 The encoded protein in Drosophila bears little resemblance to Tenascin but continues to harbor the original name. Rather, it is believed to be a transmembrane protein with a C-terminal ODZ3 (indicated by a red arrow).…”

Section: Discussionmentioning

confidence: 99%

Homozygous null mutation in ODZ3 causes microphthalmia in humans

Aldahmesh

Mohammed

Al-Hazzaa

et al. 2012

Genetics in Medicine

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Purpose: Microphthalmia is a condition in which eyes are small in size, often associated with coloboma, as a result of aberrant eye development. Isolated microphthalmia is a model disease for studying early development of the human eye, and mutations in several key genes related to eye development have been linked to this phenotype. methods: In our search for novel genes that cause autosomal recessive microphthalmia when mutated, we enrolled a family that consists of third-cousin parents and two children with isolated colobomatous microphthalmia.Results: Exome and autozygome analysis identified a null mutation in ODZ3, one of four vertebrate orthologs of odz in Drosophila. conclusion: Our data highlight a role for ODZ3 in the early development of the human eye. 2012:14(11):900-904 Genet Med

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Section: Discussionmentioning

confidence: 99%

Homozygous null mutation in ODZ3 causes microphthalmia in humans

Aldahmesh

Mohammed

Al-Hazzaa

et al. 2012

Genetics in Medicine

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“…The Ten-m/Odz protein was first found in Drosophila where it was proposed to be either a secreted tenascin-like molecule (1) or type I transmembrane receptor (2). We have subsequently identified and characterized the mouse Ten-m and found that it characterizes a new family of genes composed of 4 members (Ten-m1-4).…”

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confidence: 99%

All Four Members of the Ten-m/Odz Family of Transmembrane Proteins Form Dimers

Feng

Zhou

Oohashi

et al. 2002

Journal of Biological Chemistry

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Ten-m/Odz/teneurins are a new family of four distinct type II transmembrane molecules. Their extracellular domains are composed of an array of eight consecutive EGF modules followed by a large globular domain. Two of the eight modules contain only 5 instead of the typical 6 cysteine residues and have the capability to dimerize in a covalent, disulfide-linked fashion. The structural properties of the extracellular domains of all four mouse Ten-m proteins have been analyzed using secreted, recombinant molecules produced by mammalian HEK-293 cells. Electron microscopic analysis supported by analytical ultracentrifugation data revealed that the recombinant extracellular domains of all Ten-m proteins formed homodimers. SDS-PAGE analysis under nonreducing conditions as well as negative staining after partial denaturation of the molecules indicated that the globular COOH-terminal domains of Ten-m1 and -m4 contained subdomains with a pronounced stability against denaturing agents, especially when compared with the homologous domains of Ten-m2 and -m3. Cotransfection experiments of mammalian cells with two different extracellular domains revealed that Ten-m molecules have also the ability to form heterodimers, a property that, combined with alternative splicing events, allows the formation of a multitude of molecules with different characteristics from a limited set of genes.The Ten-m/Odz protein was first found in Drosophila where it was proposed to be either a secreted tenascin-like molecule (1) or type I transmembrane receptor (2). We have subsequently identified and characterized the mouse Ten-m and found that it characterizes a new family of genes composed of 4 members (Ten-m1-4). The biochemical analysis of recombinant fragments of mouse Ten-m1 and alkaline phosphatase fusion proteins revealed that Ten-m1 is expressed as a type II transmembrane molecule. Furthermore, we could demonstrate that two of the eight tandemly arranged EGF 1 modules present in the extracellular domain of mouse Ten-m1 containing 5 instead of 6 cysteine residues facilitate the dimerization of two molecules in a covalent, disulfide-linked fashion. Members of the Ten-m family have in the meantime also been described in rat (3), chicken (4 -7), human (8, 9), zebrafish (10), and Caenorhabditis elegans (11).The expression pattern of Ten-m/Odz in flies and mammals suggests important roles during as well as after development. In Drosophila embryogenesis, Ten-m/Odz is expressed in seven stripes during the blastoderm stage (12) and later also in the central nervous system (1), heart (2), and eye (13). Expression studies of Ten-m1-4 in adult mouse tissues showed a widespread expression with the highest levels in the brain (14, 15). In chicken, both teneurin-1 (corresponding to Ten-m1) and teneurin-2 (corresponding to Ten-m2) are expressed in neurons of the developing visual system (4). Furthermore, teneurin-2 mRNA and protein are also found in the developing limbs, somites, and craniofacial mesenchyme (7). During the segmentation period of zebrafish, T...

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“…We have recently cloned DOC4, a gene that is induced during cellular stress (Wang et al, 1998). DOC4 encodes a large secreted protein that is related to Drosophila Tenm, a protein that plays a critical role in early¯y development (Baumgartner et al, 1994;Levine et al, 1994). Comparison of the predicted peptide sequence of DOC4 to other known proteins revealed complete sequence identity between its Nterminus and the novel portion of g-heregulin.…”

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confidence: 99%

γ-heregulin is the product of a chromosomal translocation fusing the DOC4 and HGL/NRG1 genes in the MDA-MB-175 breast cancer cell line

et al. 1999

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g-heregulin is a recently described novel isoform of the heregulin/neuregulin class of EGF-like ligands that bind to and activate receptors of the ErbB family. Deregulated signaling through the heregulin-ErbB pathway is thought to be implicated in the development of a subset of human breast cancers. g-heregulin has been found to be expressed in the culture supernatant of MDA-MB-175, a breast carcinoma cell line. g-heregulin is characterized by the presence of a large N-terminal peptide extension that is not found in other heregulin isoforms. Here we report that this unique N-terminal extension of g-heregulin is identical to the N-terminus of DOC4, a product of a recently identi®ed CHOPdependent stress-induced gene. Human DOC4 and the heregulin-encoding genes map to di erent chromosomes and the MDA-MB-175 cell line contains a chromosomal translocation that leads to the fusion of DOC4 and HGL, on chromosomes 11 and 8, respectively. Thus, gheregulin is a product of a mutant fusion gene and not a bona ®de normal isoform. We speculate that the mutation may be selected for by virtue of its ability to activate ErbB signaling through the production of an autocrine ligand.

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odd Oz: A novel Drosophila pair rule gene

Cited by 142 publications

References 35 publications

Homozygous null mutation in ODZ3 causes microphthalmia in humans

Homozygous null mutation in ODZ3 causes microphthalmia in humans

All Four Members of the Ten-m/Odz Family of Transmembrane Proteins Form Dimers

γ-heregulin is the product of a chromosomal translocation fusing the DOC4 and HGL/NRG1 genes in the MDA-MB-175 breast cancer cell line

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