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  • 1
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    Receptor and betagamma binding sites in the alpha subunit of the retinal G protein transducin (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-17
    Description: Transmembrane receptors for hormones, neurotransmitters, light, and odorants mediate their cellular effects by activating heterotrimeric guanine nucleotide-binding proteins (G proteins). Crystal structures have revealed contact surfaces between G protein subunits, but not the surfaces or molecular mechanism through which Galphabetagamma responds to activation by transmembrane receptors. Such a surface was identified from the results of testing 100 mutant alpha subunits of the retinal G protein transducin for their ability to interact with rhodopsin. Sites at which alanine substitutions impaired this interaction mapped to two distinct Galpha surfaces: a betagamma-binding surface and a putative receptor-interacting surface. On the basis of these results a mechanism for receptor-catalyzed exchange of guanosine diphosphate for guanosine triphosphate is proposed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onrust, R -- Herzmark, P -- Chi, P -- Garcia, P D -- Lichtarge, O -- Kingsley, C -- Bourne, H R -- CA-54427/CA/NCI NIH HHS/ -- GM-27800/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):381-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143-0450, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8994033" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Compounds/pharmacology ; Animals ; Binding Sites ; COS Cells ; Fluorides/pharmacology ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Models, Molecular ; Mutation ; Phenotype ; *Protein Conformation ; Retinaldehyde/pharmacology ; Rhodopsin/*metabolism/pharmacology ; Rod Cell Outer Segment/metabolism ; Transducin/*chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    ETV1 is a lineage survival factor that cooperates with KIT in gastrointestinal stromal tumours (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-10-12
    Description: Gastrointestinal stromal tumour (GIST) is the most common human sarcoma and is primarily defined by activating mutations in the KIT or PDGFRA receptor tyrosine kinases. KIT is highly expressed in interstitial cells of Cajal (ICCs)-the presumed cell of origin for GIST-as well as in haematopoietic stem cells, melanocytes, mast cells and germ cells. Yet, families harbouring germline activating KIT mutations and mice with knock-in Kit mutations almost exclusively develop ICC hyperplasia and GIST, suggesting that the cellular context is important for KIT to mediate oncogenesis. Here we show that the ETS family member ETV1 is highly expressed in the subtypes of ICCs sensitive to oncogenic KIT mediated transformation, and is required for their development. In addition, ETV1 is universally highly expressed in GISTs and is required for growth of imatinib-sensitive and resistant GIST cell lines. Transcriptome profiling and global analyses of ETV1-binding sites suggest that ETV1 is a master regulator of an ICC-GIST-specific transcription network mainly through enhancer binding. The ETV1 transcriptional program is further regulated by activated KIT, which prolongs ETV1 protein stability and cooperates with ETV1 to promote tumorigenesis. We propose that GIST arises from ICCs with high levels of endogenous ETV1 expression that, when coupled with an activating KIT mutation, drives an oncogenic ETS transcriptional program. This differs from other ETS-dependent tumours such as prostate cancer, melanoma and Ewing sarcoma where genomic translocation or amplification drives aberrant ETS expression. It also represents a novel mechanism of oncogenic transcription factor activation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955195/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955195/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chi, Ping -- Chen, Yu -- Zhang, Lei -- Guo, Xingyi -- Wongvipat, John -- Shamu, Tambudzai -- Fletcher, Jonathan A -- Dewell, Scott -- Maki, Robert G -- Zheng, Deyou -- Antonescu, Cristina R -- Allis, C David -- Sawyers, Charles L -- 5F32CA130372/CA/NCI NIH HHS/ -- CA148260/CA/NCI NIH HHS/ -- CA47179/CA/NCI NIH HHS/ -- F32 CA130372/CA/NCI NIH HHS/ -- F32 CA130372-02/CA/NCI NIH HHS/ -- GM40922/GM/NIGMS NIH HHS/ -- K08 CA140946/CA/NCI NIH HHS/ -- K08 CA140946-02/CA/NCI NIH HHS/ -- K08CA140946/CA/NCI NIH HHS/ -- P01 CA047179/CA/NCI NIH HHS/ -- P01 CA047179-169002/CA/NCI NIH HHS/ -- P01CA47179/CA/NCI NIH HHS/ -- R21 MH087840/MH/NIMH NIH HHS/ -- R21 MH087840-01/MH/NIMH NIH HHS/ -- R21MH087840/MH/NIMH NIH HHS/ -- RC2 CA148260-02/CA/NCI NIH HHS/ -- England -- Nature. 2010 Oct 14;467(7317):849-53. doi: 10.1038/nature09409. Epub 2010 Oct 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20927104" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzamides ; Binding Sites ; Biomarkers, Tumor/genetics/metabolism ; Cell Line, Tumor ; *Cell Lineage ; Cell Survival/drug effects ; *Cell Transformation, Neoplastic ; DNA-Binding Proteins/antagonists & inhibitors/genetics/*metabolism ; Disease Progression ; Enhancer Elements, Genetic/genetics ; Gastrointestinal Stromal Tumors/*metabolism/*pathology ; Gene Expression Profiling ; Gene Expression Regulation, Neoplastic/genetics ; Humans ; Imatinib Mesylate ; Interstitial Cells of Cajal/metabolism/pathology ; Mice ; Mutant Proteins/genetics/metabolism ; Mutation ; NIH 3T3 Cells ; Oncogenes/genetics/*physiology ; Piperazines/pharmacology ; Protein Stability ; Proto-Oncogene Proteins c-kit/genetics/*metabolism ; Pyrimidines/pharmacology ; Signal Transduction ; Transcription Factors/antagonists & inhibitors/genetics/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Pif1 helicase and Poldelta promote recombination-coupled DNA synthesis via bubble migration (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-09-13
    Description: During DNA repair by homologous recombination (HR), DNA synthesis copies information from a template DNA molecule. Multiple DNA polymerases have been implicated in repair-specific DNA synthesis, but it has remained unclear whether a DNA helicase is involved in this reaction. A good candidate DNA helicase is Pif1, an evolutionarily conserved helicase in Saccharomyces cerevisiae important for break-induced replication (BIR) as well as HR-dependent telomere maintenance in the absence of telomerase found in 10-15% of all cancers. Pif1 has a role in DNA synthesis across hard-to-replicate sites and in lagging-strand synthesis with polymerase delta (Poldelta). Here we provide evidence that Pif1 stimulates DNA synthesis during BIR and crossover recombination. The initial steps of BIR occur normally in Pif1-deficient cells, but Poldelta recruitment and DNA synthesis are decreased, resulting in premature resolution of DNA intermediates into half-crossovers. Purified Pif1 protein strongly stimulates Poldelta-mediated DNA synthesis from a D-loop made by the Rad51 recombinase. Notably, Pif1 liberates the newly synthesized strand to prevent the accumulation of topological constraint and to facilitate extensive DNA synthesis via the establishment of a migrating D-loop structure. Our results uncover a novel function of Pif1 and provide insights into the mechanism of HR.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3915060/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3915060/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, Marenda A -- Kwon, YoungHo -- Xu, Yuanyuan -- Chung, Woo-Hyun -- Chi, Peter -- Niu, Hengyao -- Mayle, Ryan -- Chen, Xuefeng -- Malkova, Anna -- Sung, Patrick -- Ira, Grzegorz -- ES007061/ES/NIEHS NIH HHS/ -- ES015632/ES/NIEHS NIH HHS/ -- GM057814/GM/NIGMS NIH HHS/ -- GM080600/GM/NIGMS NIH HHS/ -- GM084242/GM/NIGMS NIH HHS/ -- R01 ES007061/ES/NIEHS NIH HHS/ -- R01 ES015632/ES/NIEHS NIH HHS/ -- R01 GM057814/GM/NIGMS NIH HHS/ -- R01 GM080600/GM/NIGMS NIH HHS/ -- R01 GM084242/GM/NIGMS NIH HHS/ -- R03 ES016434/ES/NIEHS NIH HHS/ -- T32 GM008307/GM/NIGMS NIH HHS/ -- T32GM07526-34/GM/NIGMS NIH HHS/ -- England -- Nature. 2013 Oct 17;502(7471):393-6. doi: 10.1038/nature12585. Epub 2013 Sep 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Baylor College of Medicine, Department of Molecular & Human Genetics, One Baylor Plaza, Houston, Texas 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24025768" target="_blank"〉PubMed〈/a〉
    Keywords: *Crossing Over, Genetic ; DNA Helicases/deficiency/genetics/*metabolism ; DNA Polymerase III/*metabolism ; DNA Repair ; *DNA Replication ; DNA, Fungal/*biosynthesis/chemistry/metabolism ; Nucleic Acid Conformation ; Rad51 Recombinase/metabolism ; Saccharomyces cerevisiae/*enzymology/*genetics/metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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