Reassignment of the <i>EPB4·1</i> gene to 1p36 and assessment of its involvement in neuroblastomas

Huang, Shun; Lichtenauer, Urs; Pack, Svetlana D.; Wang, C.; Kim, A. C.; Lutchman, Mohini; Koch, Christian A.; Torres-Cruz, Joshua; Huang, Shu-Ching; Benz, Edward J.; Christiansen, Holger; Dockhorn‐Dworniczak, Barbara; Poremba, C.; Vortmeyer, Alexander O.; Chishti, Athar H.; Zhuang, Zhengping

doi:10.1046/j.1365-2362.2001.00892.x

Cited by 19 publications

(11 citation statements)

References 13 publications

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“…To further demonstrate the specificity of dematin-GLUT1 interaction, we transfected an Xpress-tagged protein 4.1R construct and GLUT1 in HEK293T cells. We have previously shown that this 4.1R construct expresses both 80-and 135-kDa isoforms of protein 4.1R (23). Co-immunoprecipitation of protein 4.1 using an Xpress monoclonal, under the same conditions as used for the dematin-GLUT1 interaction, did not immunoprecipitate GLUT1 (Fig.…”

Section: Resultsmentioning

confidence: 76%

Dematin and Adducin Provide a Novel Link between the Spectrin Cytoskeleton and Human Erythrocyte Membrane by Directly Interacting with Glucose Transporter-1

Khan

Hanada

Mohseni

et al. 2008

Journal of Biological Chemistry

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Dematin and adducin are actin-binding proteins located at the spectrin-actin junctions, also called the junctional complex, in the erythrocyte membrane. Here we propose a new model whereby dematin and adducin link the junctional complex to human erythrocyte plasma membrane. Using a combination of surface labeling, immunoprecipitation, and vesicle proteomics approaches, we have identified glucose transporter-1 as the receptor for dematin and adducin in the human erythrocyte membrane. This finding is the first description of a transmembrane protein that binds to dematin and adducin, thus providing a rationale for the attachment of the junctional complex to the lipid bilayer. Because homologues of dematin, adducin, and glucose transporter-1 exist in many non-erythroid cells, we propose that a conserved mechanism may exist that couples sugar and other related transporters to the actin cytoskeleton.

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Section: Resultsmentioning

confidence: 76%

Dematin and Adducin Provide a Novel Link between the Spectrin Cytoskeleton and Human Erythrocyte Membrane by Directly Interacting with Glucose Transporter-1

Khan

Hanada

Mohseni

et al. 2008

Journal of Biological Chemistry

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“…However, these studies have not identified a consistent region of deletion. Furthermore, these and other studies have proposed over 20 genes within these regions as candidate neuroblastoma tumor suppressors, none of which have yet been proven to play a significant causative role in neuroblastoma tumor development (Ejeskar et al, 2000;Judson et al, 2000;De Toledo et al, 2001;Huang et al, 2001;Abel et al, 2002;Cerignoli et al, 2002;Krona et al, 2003;Thompson et al, 2003;Mathysen et al, 2004). Our current work was designed to determine the location and extent of 1p deletion in a very large primary tumor cohort by extensive genotyping, sequencing, gene identification, and transcript characterization.…”

Section: Discussionmentioning

confidence: 98%

Definition and characterization of a region of 1p36.3 consistently deleted in neuroblastoma

et al. 2004

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Substantial genomic and functional evidence from primary tumors and cell lines indicates that a consistent region of distal chromosome 1p is deleted in a sizable proportion of human neuroblastomas, suggesting that this region contains one or more tumor suppressor genes. To determine systematically and precisely the location and extent of 1p deletion in neuroblastomas, we performed allelic loss studies of 737 primary neuroblastomas and genotype analysis of 46 neuroblastoma cell lines. Together, the results defined a single region within 1p36.3 that was consistently deleted in 25% of tumors and 87% of cell lines. Two neuroblastoma patients had constitutional deletions of distal 1p36 that overlapped the tumor-defined region. The tumor-and constitutionally-derived deletions together defined a smallest region of consistent deletion (SRD) between D1S2795 and D1S253. The 1p36.3 SRD was deleted in all but one of the 184 tumors with 1p deletion. Physical mapping and DNA sequencing determined that the SRD minimally spans an estimated 729 kb. Genomic content and sequence analysis of the SRD identified 15 characterized, nine uncharacterized, and six predicted genes in the region. The RNA expression profiles of 21 of the genes were investigated in a variety of normal tissues. The SHREW1 and KCNAB2 genes both had tissue-restricted expression patterns, including expression in the nervous system. In addition, a novel gene (CHD5) with strong homology to proteins involved in chromatin remodeling was expressed mainly in neural tissues. Together, these results suggest that one or more genes involved in neuroblastoma tumorigenesis or tumor progression are likely contained within this region.

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“…In this regard, Protein 4.1R and Protein 4.1B have been reported to function as negative growth regulators in the pathogenesis of a diverse number of human cancers (Tran et al, 1999;Huang et al, 2001;Charboneau et al, 2002), including meningiomas (Gutmann et al, 1997Perry et al, 2000;Robb et al, 2003). The present study was undertaken to define the critical domain of Protein 4.1B necessary for meningioma growth suppression as a first step towards elucidating the molecular mechanism underlying Protein 4.1B function.…”

Section: Discussionmentioning

confidence: 99%

Membrane localization of the U2 domain of Protein 4.1B is necessary and sufficient for meningioma growth suppression

et al. 2005

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Meningiomas are common central nervous system tumors; however, the molecular mechanisms underlying their pathogenesis are largely undefined. Previous work has implicated Protein 4.1B as an important tumor suppressor involved in the development of these neoplasms. In this report, we demonstrate that the U2 domain is necessary and sufficient for the ability of Protein 4.1B to function as a meningioma growth suppressor. Using a series of truncation and deletion constructs of DAL-1 (a fragment of Protein 4.1B that retains all the growth suppressive properties), we narrowed the domain required for 4.1B growth suppression to a fragment containing a portion of the FERM domain and the U2 domain using clonogenic assays on meningioma cells. Deletion of the U2 domain in the context of the full-length DAL-1 molecule eliminated growth suppressor function, as measured by thymidine incorporation and caspase-3 activation. Moreover, targeting the U2 domain to the plasma membrane using a membrane localization signal (MLS) reduced cell proliferation, similar to wild-type DAL-1. Collectively, the data suggest that the U2 domain, when properly targeted to the plasma membrane, contains all the residues necessary for mediating Protein 4.1B growth suppression.

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Reassignment of the EPB4·1 gene to 1p36 and assessment of its involvement in neuroblastomas

Cited by 19 publications

References 13 publications

Dematin and Adducin Provide a Novel Link between the Spectrin Cytoskeleton and Human Erythrocyte Membrane by Directly Interacting with Glucose Transporter-1

Dematin and Adducin Provide a Novel Link between the Spectrin Cytoskeleton and Human Erythrocyte Membrane by Directly Interacting with Glucose Transporter-1

Definition and characterization of a region of 1p36.3 consistently deleted in neuroblastoma

Membrane localization of the U2 domain of Protein 4.1B is necessary and sufficient for meningioma growth suppression

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