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Both Normal and Transforming PCPH Proteins Have Guanosine

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Both Normal and Transforming PCPH Proteins Have Guanosine [CANCER RESEARCH 60, 1720–1728, March 15, 2000] Both Normal and Transforming PCPH Proteins Have Guanosine Diphosphatase Activity But Only the Oncoprotein Cooperates with Ras in Activating Extracellular Signal-regulated Kinase ERK11 Juan A. Recio, J. Guillermo Pa´ez, Baishali Maskeri, Mark Loveland, Juan A. Velasco, and Vicente Notario2 Laboratory of Experimental Carcinogenesis, Department of Radiation Medicine, Georgetown University Medical Center, Washington, DC 20007 ABSTRACT ORF3 of PCPH and the translation of the mutated protein to terminate 33 residues downstream in the new ORF. Consequently, the mt-PCPH Previous reports from our laboratory described the activation of the oncoprotein is a truncated form (246 versus 469 amino acids) of its PCPH gene into the PCPH oncogene (mt-PCPH, reported previously as Cph) by a single point mutational deletion. As a consequence, the mt- normal counterpart and contains an additional, rather hydrophobic PCPH oncoprotein is a truncated form of the normal PCPH protein. COOH-terminal tail (6). Although both proteins have ribonucleotide diphosphate-binding activity, Biochemical analyses of the in vitro translated products of mt- only mt-PCPH acted synergistically with a human H-Ras oncoprotein to PCPH and PCPH and functional analyses of cells transformed by transform murine NIH3T3 fibroblasts. We report here the expression of mt-PCPH oncogene or transfected with expression constructs of the PCPH and mt-PCPH proteins in Escherichia coli and the finding that PCPH allowed us to demonstrate (6) that: (a) the products encoded by the purified bacterial recombinant proteins have intrinsic guanosine both PCPH and mt-PCPH genes are ribonucleotide-binding proteins; diphosphatase (GDPase) activity. However, expression of the Syrian ham- ster PCPH and mt-PCPH proteins in haploid yeast strains engineered to (b) although they share partial homology with GTP/GDP exchange be GDPase deficient by targeted disruption of the single GDA1 allele did factors, they do not catalyze nucleotide exchange on the H-Ras protein not complement their glycosylation-disabled phenotype, suggesting the or any other small G proteins tested; (c) steady-state levels of PCPH existence of significant functional differences between the mammalian and and particularly mt-PCPH mRNA are up-regulated in serum-deprived yeast enzymes. Results from transient cotransfections into NIH3T3, cells; and (d) the mt-PCPH oncoprotein, and to a lesser extent the COS-7, or 293T cells indicated that, in mammalian cells, both PCPH and PCPH protein, provide the cells with enhanced stress-survival func- mt-PCPH cause an overall down-regulation of the stimulatory effect of tions against a variety of stress factors. Although these results suggest epidermal growth factor or the activated ras or raf oncogenes on the Ras/mitogen-activated protein kinase/extracellular signal-regulated ki- that PCPH participates in cellular mechanisms of response to stress, nase (ERK) signaling pathway. However, despite this overall negative its biochemical activity remains unknown. regulatory role on Ras signaling, mt-PCPH, but not PCPH, cooperated Most recently, we completed the cDNA cloning, sequencing, and with the Ras oncoprotein to produce a prolonged stimulation of the chromosomal mapping of the mouse (4) and human (5) PCPH proto- phosphorylation of ERK1 but had no effect on the phosphorylation levels oncogenes and determined that PCPH expression is frequently altered of ERK2. These results represent a clear difference between the mecha- in human neoplasms (5). Indeed, PCPH was not expressed in 16 of 16 nisms of action of PCPH and mt-PCPH and suggest that the ability to primary human renal carcinomas, although it was highly expressed in cause a sustained activation of ERK1 may be an important determinant of the transforming activity of mt-PCPH. matched normal kidney, and PCPH mRNA was also undetectable in the majority (67.4%) of the human tumor cell lines tested. In addition, recent data (7) showed that some human tumor cell lines expressed INTRODUCTION both the normal Mr 47,000 PCPH protein and a smaller immunore- ϳ active polypeptide with the size (Mr 30,000) of the mt-PCPH The PCPH oncogene (initially reported as Cph and termed mt- protein. These data suggested that PCPH loss and perhaps truncation PCPH here) was originally isolated in our laboratory from chemically may be involved in the development of some human tumors. There- initiated, neoplastic Syrian hamster embryo fibroblasts on the basis of fore, it becomes essential to identify the biochemical activity of the its ability to transform NIH3T3 cells upon serial cycles of transfection normal and transforming PCPH proteins. (1, 2). We further demonstrated that mt-PCPH synergizes with the We report here the expression of the PCPH and mt-PCPH proteins human H-ras oncogene in transforming NIH3T3 cells (2), and that the in Escherichia coli and the finding that the recombinant proteins have PCPH proto-oncogene (termed PCPH here) is highly conserved in eukaryotic cells, from yeast to humans, and it is expressed in most GDPase activity. However, expression of the Syrian hamster PCPH normal adult tissues in Syrian hamsters, mice, and humans (3–5), and mt-PCPH proteins in yeast strains engineered to be GDPase suggesting that the normal PCPH protein may have an important deficient by targeted disruption of the single GDA1 allele did not cellular function. Recently, we isolated full-length cDNA clones of complement their glycosylation-disabled phenotype, suggesting the the Syrian hamster mt-PCPH and PCPH, determined their nucleotide existence of significant functional differences between the mamma- sequence, and demonstrated that mt-PCPH was activated by a point lian and yeast enzymes. Results indicate that, in mammalian cells, mutational deletion (6) within the coding region of the proto- both PCPH and mt-PCPH cause an overall down-regulation of the oncogene. This single bp change causes both a shift in the normal Ras/MEK signaling pathway. Despite this, mt-PCPH, but not PCPH, activated ERK1 but not ERK2 when cotransfected with an activated Received 9/22/99; accepted 1/18/00. human H-ras oncogene. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. 1 Supported by USPHS Grant CA64472 from the National Cancer Institute and by 3 The abbreviations used are: ORF, open reading frame; ERK, extracellular signal- USPHS Grant P30-CA51008. regulated kinase; MEK, mitogen-activated protein kinase/ERK; EGF, epidermal growth 2 To whom requests for reprints should be addressed, at Department of Radiation factor; GDPase, guanosine diphosphatase; IPTG, isopropyl-␤-D-thiogalactopyranoside; Medicine, Georgetown University Medical Center, Research Building, Room E215, 3970 MBP, myelin basic protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; HA, Reservoir Road, NW, Washington, DC 20007. Phone: (202) 687-2102; Fax: (202) 687- hemagglutinin; AP-1, activating protein-1; SRE, serum response element; PKC, protein 2221; E-mail: [email protected]. kinase C. 1720 Downloaded from cancerres.aacrjournals.org on October 1, 2021. © 2000 American Association for Cancer Research. PCPH ONCOPROTEIN AND ERK1 ACTIVATION MATERIALS AND METHODS the color of the lysate on the absorbance measurements. Reactions were performed in the presence of L-[35S]methionine (Amersham, Arlington Plasmids and General Methods. The cytomegalovirus-based vector Heights, IL), as described previously (14). Radiolabeled translation products pcDNA3 (Invitrogen, Carlsbad, CA) containing the cDNA inserts (6) of PCPH were resolved by SDS-PAGE (12.5%), and dried gels were exposed to X-ray (pcDNA3-PCPH) and mt-PCPH (pcDNA3-mt-PCPH) was used for the ex- films. pression of the PCPH and mt-PCPH proteins in mammalian cells, using Construction of Bacterial Expression Vectors. The inducible pET- insertless pcDNA-3 as control. Expression of oncogenic Ras and Raf was 30a(ϩ) bacterial expression vector (Novagen, Madison, WI) was used to Val12 accomplished using constitutive vectors with Ha-ras (pRasV12) and v-raf subclone the inserts from the Syrian hamster PCPH and mt-PCPH cDNA (pvRaf) under the transcriptional control of the Rous sarcoma virus promoter clones (6). The PCPH and mt-PCPH inserts were excised from the original (8). Luciferase reporter vectors pAP1-Luc and pSRE-Luc were obtained from cDNA cloning vector by cleavage with BspHI and XhoI, and pET-30a(ϩ) was Stratagene Cloning Systems (La Jolla, CA). Protein determinations were done linearized by cleavage with NcoI and XhoI. The unique BspHI in the PCPH using the BCA Protein Assay System (Pierce, Rockford, IL). Luciferase and mt-PCPH sequences is located at the ATG codon in position 13. Because determinations were carried out 48 h after cotransfections with pAP1-Luc and BspHI and NcoI generate compatible 5Ј overhangs, ligation of the PCPH pSRE-Luc using the Promega (Madison, WI) assay system, with the help of a inserts with the linearized pET-30a(ϩ) vector allowed directional cloning and Lumat LB9501 luminometer (Berthold Analytical Instruments, EG&G Wallac, regenerated the original ATG codon 13, keeping the PCPH or mt-PCPH Gaithersburg, MD). sequences in-frame with the 5Ј sequences of the pET-30a(ϩ) vector (Fig. 3A). Mammalian Cells, Culture, and Transfection Conditions. Normal Thus, both PCPH and mt-PCPH expression constructs lacked the first 12
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