Isolation of DICE1: A gene frequently affected by LOH and downregulated in lung carcinomas

Wieland, Ilse; Arden, Karen C.; Michels, Dirk; Klein-Hitpaß, Ludger; Böhm, Malte; Viars, Carrie S.; Weidle, Ulrich H.

doi:10.1038/sj.onc.1202806

Cited by 58 publications

(49 citation statements)

References 31 publications

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“…There is indirect evidence that the latter interpretation may be the correct one. Wieland and co-workers (Wieland et al, 1999) have reported recently a gene, which is deleted in human lung cancer (as well as in other human tumors). They called the deleted gene, DICE-1 (deleted in lung cancer), and established it as a solid tumor suppressor gene.…”

Section: Regulation Of Cell Size By the Igf-irmentioning

confidence: 99%

The contradictions of the insulin-like growth factor 1 receptor

2000

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Section: Regulation Of Cell Size By the Igf-irmentioning

confidence: 99%

The contradictions of the insulin-like growth factor 1 receptor

2000

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“…This motif is also present in ␤-integrins and has been alternatively named as IntB motif (Takada et al, 1997). There are also vWFA motifs present in anthrax toxin receptor protein (Wigelsworth et al, 2004) and DICE1, a protein encoded by a gene located in a human tumor suppressor locus (Wieland et al, 1999).To our knowledge, Dictyostelium VwkA is the first example of a vWFA-like domain present in the same polypeptide as a protein kinase catalytic domain. Notably, the Neurospora crassa genome contains a hypothetical protein with very similar domain organization, including a vWFA-like domain and an ␣-kinase catalytic domain (GenBank accession no.…”

mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of a Novel α-Kinase with a von Willebrand Factor A-like Motif Localized to the Contractile Vacuole and Golgi Complex inDictyostelium discoideum

Betapudi

Mason

Licate

et al. 2005

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We have identified a new protein kinase in Dictyostelium discoideum that carries the same conserved class of "␣-kinase" catalytic domain as reported previously in myosin heavy chain kinases (MHCKs) in this amoeba but that has a completely novel domain organization. The protein contains an N-terminal von Willebrand factor A (vWFA)-like motif and is therefore named VwkA. Manipulation of VwkA expression level via high copy number plasmids (VwkA ؉؉ cells) or gene disruption (vwkA null cells) results in an array of cellular defects, including impaired growth and multinucleation in suspension culture, impaired development, and alterations in myosin II abundance and assembly. Despite sequence similarity to MHCKs, the purified protein failed to phosphorylate myosin II in vitro. Autophosphorylation activity, however, was enhanced by calcium/calmodulin, and the enzyme can be precipitated from cellular lysates with calmodulin-agarose, suggesting that VwkA may directly bind calmodulin. VwkA is cytosolic in distribution but enriched on the membranes of the contractile vacuole and Golgi-like structures in the cell. We propose that VwkA likely acts indirectly to influence myosin II abundance and assembly behavior and possibly has broader roles than previously characterized ␣ kinases in this organism, which all seem to be MHCKs. INTRODUCTIONNearly all aspects of cell life are regulated by protein phosphorylation involving a large number of biochemical reactions and distinct signaling pathways. Existence of ϳ500 genes encoding various protein kinases in the human genome further underscores their importance in cell life (Manning et al., 2002). Most of these conventional protein kinases belong to serine/threonine/tyrosine, a kinase superfamily whose members carry a conserved catalytic domain with recognizable sequence similarity in spite of having different targets in the cell (Hardie, 1994;Hanks and Hunter, 1995). In recent years, however, biochemical and molecular approaches have led to the identification of more divergent classes of eukaryotic protein kinases carrying a catalytic domain sequence with no sequence similarity with conventional protein kinase catalytic domains (Manning et al., 2002). One major class of unconventional protein kinases was first identified via representatives of myosin heavy chain kinases (MHCKs) in Dictyostelium discoideum (Futey et al., 1995;Côté et al., 1997) and via identification of mammalian eEF-2 kinase (eEF-2K) as an unconventional protein kinase (Ryazanov et al., 1997). This novel, conserved group of unconventional eukaryotic protein kinases has been termed the ␣-kinase family (Ryazanov et al., 1999;Drennan and Ryazanov, 2004).Molecular cloning and biochemical characterization studies demonstrated that at least three Dictyostelium ␣-kinases genes encode enzymes that can specifically phosphorylate myosin II heavy chain (MHC) in vitro and in vivo, and were thus named as MHC kinase A (MHCK A), MHC kinase B (MHCK B) and MHC kinase C (MHCK C) (Futey et al., 1995;Clancy et al., 1997;Luo et al., 200...

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“…23 Amplification of EFNB1 cDNA was performed by RT-PCR using primers 5 0 -GGCAGAG GAAGGCGAGGCGA-3 0 and 5 0 -GCAAGGGGAGGGGGT GTG-3 0 for amplification of a 1.2 kb product encompassing the entire coding region. Primer pair 5 0 -CAAGTTCCT GAGTGGGAAGG-3 0 and 5 0 -GTGTGGCCATCTTGACAG TG-3 0 was used to amplify a 455-bp product from exons 2 -4, and primer pair 5 0 -ATCATGAAGGTTGGGCAAGA-3 0 and 5 0 -TGGGGGCAGTAGTTGTTCTC-3 0 was used to amplify a 467-bp product from exons 4 and 5.…”

Section: Rt-pcrmentioning

confidence: 99%

Dissecting the molecular mechanisms in craniofrontonasal syndrome: differential mRNA expression of mutant EFNB1 and the cellular mosaic

et al. 2007

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Craniofrontonasal syndrome (CFNS) is an X-linked malformation syndrome with variable phenotype that is caused by mutations in the ephrin-B1 gene (EFNB1). Over 50% of EFNB1 mutations result in premature termination codons that may elicit mRNA degradation by the nonsense-mediated decay pathway. To assess the effects of various mutations at the transcript level, expression of EFNB1 mRNA was studied by RT-PCR in fibroblast cultures established from CFNS female patients. Compared to the wild-type and two missense mutation alleles, severe depletion of transcripts was observed for mutant alleles harbouring either splice site mutation c.407-2A4T at the exon 2/3 boundary or frameshift mutation c.377_384delTCAAGAAG in exon 2. In contrast, escape from mRNA decay was observed for mutation c.614_615delCT, which generates a premature termination codon close to the 3 0 -end of the penultimate exon 4 disobeying the '50 -55 bp' rule. These results suggest differential degradation of mutant EFNB1 transcripts by the nonsense-mediated mRNA decay pathway. Although the clinical phenotypes of the patients were not highly suggestive of a phenotype -genotype correlation, the two female patients were diagnosed with diaphragmatic hernia harbouring putative ephrin-B1 truncating mutations. Previously, disease manifestation in heterozygous females had been attributed mainly to cellular interference of divergent cell populations expressing wild-type or mutant EFNB1, depending on the pattern of X-inactivation. Upon clonal expansion of patient cells with either the wild-type or mutant EFNB1 on the active X-chromosome, we were able to separate mutant and wild-type EFNB1-expressing cells in vitro, further supporting the concept of cellular interference in CFNS.

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Isolation of DICE1: A gene frequently affected by LOH and downregulated in lung carcinomas

Cited by 58 publications

References 31 publications

The contradictions of the insulin-like growth factor 1 receptor

The contradictions of the insulin-like growth factor 1 receptor

Identification and Characterization of a Novel α-Kinase with a von Willebrand Factor A-like Motif Localized to the Contractile Vacuole and Golgi Complex inDictyostelium discoideum

Dissecting the molecular mechanisms in craniofrontonasal syndrome: differential mRNA expression of mutant EFNB1 and the cellular mosaic

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