Chromosomal localization and promoter analysis of the adenomatous polyposis coli binding protein RP1

Wadle, Andreas; Thiel, Gerald; Mischo, Axel; Jung, Volker; Pfreundschuh, Michael; Renner, Christoph

doi:10.1038/sj.onc.1204797

Cited by 3 publications

(4 citation statements)

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“…ATF4 transactivates the transcription of specific genes through binding to the cAMP response element (CRE) TAGACGTCA (Karpinski et al, 1992). Multiple gene promoters have been identified as being transactivated by ATF4, including CHOP/GADD153 (Fawcett et al, 1999), interleukin-2 CD28 response element (CD28RE) (Butscher et al, 1998), and the adenomatous polyposis coli (APC) tumor suppressor-binding protein RP1 (Wadle et al, 2001). The transcriptional selectivity of ATF4 is modulated by the formation of heterodimers with multiple C/EBP bZIP proteins including: CHOP/ GADD153 (Gachon et al, 2001), C/EBPa (Nishizawa and Nagata, 1992), C/EBPb, CRP2 (Vallejo et al, 1993), and C/EBPg (Vinson et al, 1993) as well as AP-1 family members (fos and jun proteins) (Hai and Curran, 1991;Kato et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia

2003

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Regions of hypoxia are a hallmark of solid tumors. Tumor cells modulate the regulation of specific genes allowing adaptation and survival in the harsh hypoxic environment. We have identified SKIP3, a novel human kinase-like gene, which is overexpressed in multiple human tumors and is regulated by hypoxia. SKIP3 is an ortholog of the Drosophila tribbles, rat NIPK, dog C5FW, and human C8FW genes. Drosophila tribbles is involved in slowing cell-cycle progression during Drosophila development, but little is known regarding the function or tissue distribution of the vertebrate orthologs. We show that the normal tissue expression of SKIP3 is confined to human liver, while multiple primary human lung, colon, and breast tumors express high levels of SKIP3 transcript. Endogenous SKIP3 protein accumulates within 48 h under hypoxic growth conditions in HT-29 and PC-3 cells, with upregulation of the SKIP3 mRNA transcript by 72 h. We identified activating transcription factor 4 (ATF4) as a SKIP3-binding partner using the yeast-two-hybrid assay. Coexpression of SKIP3 and ATF4 showed that SKIP3 is associated with the proteolysis of ATF4, which can be blocked using a proteosome inhibitor. These results indicate that SKIP3 may be an important participant in tumor cell growth.

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Section: Introductionmentioning

confidence: 99%

SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia

2003

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“…cDNA inserts were retrieved from the plasmid DNA by EcoRI/Xho restriction and analyzed by agarose gel-electrophoresis as described. 26 Inserts were automatically sequenced (LICOR 4000L; MWG, Munich, Germany) and the nucleotide sequence data analyzed using public data bases (BLAST) as described. 27 Prediction of glycosylation pattern was done using NetOGlyc 2.0 Server software.…”

Section: Isolation Of Plasmid Dna From Monoclonal Yeast Culturementioning

confidence: 99%

“…25 cDNA synthesis and quantitative real-time RT-PCR reactions were carried out on a light-cycler machine (Roche, Mannheim, Germany) as described previously. 26 RT-PCR conditions were as follows unless otherwise specified: 95°C 10 min, 94°C 1 min, annealing 60°C 1 min, extension 72°C 2 min for a total of 32-5 cycles. All PCR reagents including high fidelity Taq-polymerase and PCR-buffer were obtained from Roche (Mannheim, Germany).…”

Section: Rt-pcrmentioning

confidence: 99%

Serological identification of breast cancer-related antigens from aSaccharomyces cerevisiae surface display library

et al. 2005

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A yeast cell surface display technology was used for the isolation and characterization of tumor antigens recognised by autologous or allogeneic breast cancer serum. More than 100 clones recognized by patient serum were isolated using high-through-put fluorescence activated cell sorting. Combined serological and sequence analysis confirmed that a number of proteins known to be overexpressed in breast cancer tissue could be detected. A recently identified small breast epithelial mucin almost exclusively expressed in mammary gland tissue was isolated as a mutated protein variant. Subsequent serological analysis using the yeast expression system for the wild-type and mutant form showed a strong recognition by patient sera, whereas no significant recognition was observed for the respective prokaryotically expressed proteins. The small breast epithelial mucin is present to a large extent in a membrane bound format and might be used for tumor targeting strategies. ' 2005 Wiley-Liss, Inc.Key words: tumor antigens; serological screening; yeast surface display; cDNA expression library One of the major goals in the field of cancer immunotherapy is the identification of appropriate target antigens for either vaccine or antibody based approaches. The systematic search for tumorspecific antigens and their derived peptides started with the work of Boon et al.1 using T cell epitope cloning and Rammensee et al.2 using peptide elution. The value of both methods has been demonstrated in many areas including cancer. Both methods do have their intrinsic limitations, however, by relying either on the existence of a T-cell line or clone for the epitope cloning approach or on a sufficient amount of tumor tissue to allow for the successful identification of immunogenic peptides. The advent of a serological approach such as the serological identification of antigens by recombinant expression cloning (SEREX) with high-titered immunoglobulin G antibodies obtained from the sera of cancer patients represented a hallmark in modern tumor serology as it allowed for the immediate identification of tumor related antigens.3 SEREX has led to the identification of a multitude of new cancer antigens in different tumor entities and the international SEREX database (www2.licr.org/CancerImmunomeDB/) holds more than 2,000 different gene entries of potentially cancer related antigens. The importance of this technology goes beyond the serological identification of candidate tumor antigens by creating a link between T and B cell immunology as strong antibody responses are considered to depend on the presence of T cell help.4,5 The analysis of the B cell repertoire helps to identify antigens that might become valid targets for immunotherapy with cancer vaccines aiming to induce cytotoxic T cell responses.6,7 Evidence has accumulated over the recent years, however, that the antigen repertoire detectable by the conventional SEREX approach is limited. 8 This might be attributed in part to the fact that potential antigens that are subject to posttranslational ...

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“…MAPRE proteins have been characterised recently as a new family of microtubule‐associated proteins with up to 7 homologues 1. EB1 and RP1 are the best studied members of this family that have been identified independently by 2 groups searching for new molecules involved in the process of T‐cell activation or new interaction partners of the adenomatous polyposis coli protein (APC), respectively 2, 3, 4. MAPRE family members are characterized by their capability to bind to the C‐terminus of the APC protein and tubulin 5.…”

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confidence: 99%

Characterization of Hap/BAG‐1 variants as RP1 binding proteins with antiapoptotic activity

Wadle

Mischo

Henrich

et al. 2005

Intl Journal of Cancer

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The MAPRE protein family (EB1, RP1, EB2) represents a highly conserved group of proteins that localize preferentially to the plus end of microtubules, both in the nucleus and cytoplasm. In addition, MAPRE family members are characterized by their capability to bind to the C‐terminus of the adenomatous polyposis coli (APC) protein and tubulin in order to stabilize microtubules. Apart from the interaction with APC and tubulin, no other direct binding partners are known today. Because the RP1 gene product was identified in activated T cells, we set out to search for new interacting molecules in a yeast 2‐hybrid system. We isolated a cDNA variant encoding for the antiapoptotic Hap/BAG‐1 protein truncated by 34 amino acids at the C‐terminus. In the original Hap/BAG‐1 protein, the C‐terminal domain is responsible for binding to Bcl‐2 and Hsp/Hsc70, which is believed to be the reason for its antiapoptotic activity. Although this putative Hap/BAG‐1 variant protein showed no interaction with Bcl‐2 or Hsp/Hsc70, it was perfectly able to confer resistance to apoptosis. Subcellular distribution analysis revealed that the Hap/Bag‐1 variant protein localized homogenously to the cytoplasm and shuttles into the nucleus in response to stress, a process that could be blocked by RP1 protein overexpression. © 2005 Wiley‐Liss, Inc.

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Chromosomal localization and promoter analysis of the adenomatous polyposis coli binding protein RP1

Cited by 3 publications

References 31 publications

SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia

SKIP3, a novel Drosophila tribbles ortholog, is overexpressed in human tumors and is regulated by hypoxia

Serological identification of breast cancer-related antigens from aSaccharomyces cerevisiae surface display library

Characterization of Hap/BAG‐1 variants as RP1 binding proteins with antiapoptotic activity

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