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  • 1
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    Fat mass and obesity related (FTO) shuttles between the nucleus and cytoplasm (2014)
    Portland Press
    Details
    Publication Date: 2014-09-23
    Description: SNPs on a chromosome 16 locus encompassing FTO , as well as IRX3, 5 , 6, FTM and FTL are robustly associated with human obesity. FTO catalyzes the Fe(II)- and 2OG-dependent demethylation of RNA and is an amino acid (AA) sensor that couples AA levels to mTORC1 signaling, thereby playing a key role in regulating growth and translation. However, the cellular compartment in which FTO primarily resides to perform its biochemical role is unclear. Here, we undertake live cell imaging of GFP-FTO, and demonstrate that FTO resides in both the nucleus and cytoplasm. We show using ‘fluorescence loss in photo bleaching’ (FLIP) that a mobile FTO fraction shuttles between both compartments. We performed a proteomic study and identified Exportin 2 (XPO2), one of a family of proteins that mediates the shuttling of proteins between the nucleus and the cytoplasm, as a binding partner of FTO. Finally, using deletion studies, we show that the N-terminus of FTO is required for its ability to shuttle between the nucleus and cytoplasm. In conclusion, FTO is present in both the nucleus and cytoplasm, with a mobile fraction that shuttles between both cellular compartments, possibly by interaction with XPO2.
    Print ISSN: 0144-8463
    Electronic ISSN: 1573-4935
    Topics: Biology , Chemistry and Pharmacology
    Published by Portland Press
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  • 2
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    Dendritic cell stimulation by mycobacterial Hsp70 is mediated through CCR5 (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-21
    Description: An effective host immune response to mycobacterial infection must control pathogen dissemination without inducing immunopathology. Constitutive overexpression of mycobacterial heat shock protein (myHsp70) is associated with impaired bacterial persistence, but the immune-mediated mechanisms are unknown. We found that myHsp70, in addition to enhancing antigen delivery to human dendritic cells, signaled through the CCR5 chemokine receptor, promoting dendritic cell aggregation, immune synapse formation between dendritic cells and T cells, and the generation of effector immune responses. Thus, CCR5 acts as a pattern-recognition receptor for myHsp70, which may have implications for both the pathophysiology of tuberculosis and the use of myHsps in tumor-directed immunotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Floto, R Andres -- MacAry, Paul A -- Boname, Jessica M -- Mien, Tan Suet -- Kampmann, Beate -- Hair, James R -- Huey, Oh Seen -- Houben, Edith N G -- Pieters, Jean -- Day, Cheryl -- Oehlmann, Wulf -- Singh, Mahavir -- Smith, Kenneth G C -- Lehner, Paul J -- 077273/Wellcome Trust/United Kingdom -- G0600823/Medical Research Council/United Kingdom -- G108/485/Medical Research Council/United Kingdom -- G9800943/Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):454-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Cambridge Institute for Medical Research, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053144" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/immunology/*physiology ; Calcium Signaling ; Cell Adhesion Molecules/metabolism ; Cell Aggregation ; Cell Line, Tumor ; Cell Membrane/ultrastructure ; Cell Movement ; Dendritic Cells/*immunology/*physiology/ultrastructure ; HSP70 Heat-Shock Proteins/immunology/*physiology ; Humans ; Interleukin-6/metabolism ; Mycobacterium bovis/immunology/physiology ; *Mycobacterium tuberculosis ; Pseudopodia/ultrastructure ; Receptors, CCR5/genetics/*physiology ; T-Lymphocytes/immunology/physiology ; T-Lymphocytes, Cytotoxic/immunology
    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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  • 3
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    Latency-associated degradation of the MRP1 drug transporter during latent human cytomegalovirus infection (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-04-13
    Description: The reactivation of latent human cytomegalovirus (HCMV) infection after transplantation is associated with high morbidity and mortality. In vivo, myeloid cells and their progenitors are an important site of HCMV latency, whose establishment and/or maintenance require expression of the viral transcript UL138. Using stable isotope labeling by amino acids in cell culture-based mass spectrometry, we found a dramatic UL138-mediated loss of cell surface multidrug resistance-associated protein-1 (MRP1) and the reduction of substrate export by this transporter. Latency-associated loss of MRP1 and accumulation of the cytotoxic drug vincristine, an MRP1 substrate, depleted virus from naturally latent CD14(+) and CD34(+) progenitors, all of which are in vivo sites of latency. The UL138-mediated loss of MRP1 provides a marker for detecting latent HCMV infection and a therapeutic target for eliminating latently infected cells before transplantation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3683642/" 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/PMC3683642/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weekes, Michael P -- Tan, Shireen Y L -- Poole, Emma -- Talbot, Suzanne -- Antrobus, Robin -- Smith, Duncan L -- Montag, Christina -- Gygi, Steven P -- Sinclair, John H -- Lehner, Paul J -- 084957/Wellcome Trust/United Kingdom -- 084957/Z/08/Z/Wellcome Trust/United Kingdom -- 093966/Wellcome Trust/United Kingdom -- 093966/Z/10/Z/Wellcome Trust/United Kingdom -- 100140/Wellcome Trust/United Kingdom -- G0701279/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2013 Apr 12;340(6129):199-202. doi: 10.1126/science.1235047.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23580527" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD34/analysis ; Cell Line, Tumor ; Cytomegalovirus/genetics/*physiology ; Cytomegalovirus Infections/*metabolism/*virology ; Dendritic Cells/physiology ; Down-Regulation ; Humans ; Lysosomes/metabolism ; Monocyte-Macrophage Precursor Cells/metabolism/virology ; Monocytes/metabolism/virology ; Multidrug Resistance-Associated Proteins/genetics/*metabolism ; Vincristine/metabolism/pharmacology ; Viral Proteins/*metabolism ; *Virus Latency
    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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  • 4
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    A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-29
    Description: Newly assembled major histocompatibility complex (MHC) class I molecules, together with the endoplasmic reticulum chaperone calreticulin, interact with the transporter associated with antigen processing (TAP) through a molecule called tapasin. The molecular cloning of tapasin revealed it to be a transmembrane glycoprotein encoded by an MHC-linked gene. It is a member of the immunoglobulin superfamily with a probable cytoplasmic endoplasmic reticulum retention signal. Up to four MHC class I-tapasin complexes were found to bind to each TAP molecule. Expression of tapasin in a negative mutant human cell line (220) restored class I-TAP association and normal class I cell surface expression. Tapasin expression also corrected the defective recognition of virus-infected 220 cells by class I-restricted cytotoxic T cells, establishing a critical functional role for tapasin in MHC class I-restricted antigen processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ortmann, B -- Copeman, J -- Lehner, P J -- Sadasivan, B -- Herberg, J A -- Grandea, A G -- Riddell, S R -- Tampe, R -- Spies, T -- Trowsdale, J -- Cresswell, P -- AI30581/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1997 Aug 29;277(5330):1306-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Section of Immunobiology, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9271576" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*metabolism ; Amino Acid Sequence ; Antigen Presentation ; Antiporters/chemistry/genetics/*metabolism ; Calcium-Binding Proteins/metabolism ; Calreticulin ; Cell Line ; Cell Line, Transformed ; Chromosome Mapping ; Chromosomes, Human, Pair 6 ; Cloning, Molecular ; Dimerization ; Endoplasmic Reticulum/metabolism ; Genetic Linkage ; HLA Antigens/*metabolism ; Histocompatibility Antigens Class I/*metabolism ; Humans ; Immunoglobulin G/chemistry ; Immunoglobulins/chemistry/genetics/*metabolism ; Major Histocompatibility Complex/genetics ; Membrane Transport Proteins ; Molecular Sequence Data ; Ribonucleoproteins/metabolism ; Sequence Homology, Amino Acid ; T-Lymphocytes, Cytotoxic ; Tumor Cells, Cultured
    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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  • 5
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    GENE SILENCING. Epigenetic silencing by the HUSH complex mediates position-effect variegation in human cells (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-05-30
    Description: Forward genetic screens in Drosophila melanogaster for modifiers of position-effect variegation have revealed the basis of much of our understanding of heterochromatin. We took an analogous approach to identify genes required for epigenetic repression in human cells. A nonlethal forward genetic screen in near-haploid KBM7 cells identified the HUSH (human silencing hub) complex, comprising three poorly characterized proteins, TASOR, MPP8, and periphilin; this complex is absent from Drosophila but is conserved from fish to humans. Loss of HUSH components resulted in decreased H3K9me3 both at endogenous genomic loci and at retroviruses integrated into heterochromatin. Our results suggest that the HUSH complex is recruited to genomic loci rich in H3K9me3, where subsequent recruitment of the methyltransferase SETDB1 is required for further H3K9me3 deposition to maintain transcriptional silencing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4487827/" 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/PMC4487827/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tchasovnikarova, Iva A -- Timms, Richard T -- Matheson, Nicholas J -- Wals, Kim -- Antrobus, Robin -- Gottgens, Berthold -- Dougan, Gordon -- Dawson, Mark A -- Lehner, Paul J -- 100140/Wellcome Trust/United Kingdom -- 101835/Wellcome Trust/United Kingdom -- 101835/Z/13/Z/Wellcome Trust/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2015 Jun 26;348(6242):1481-5. doi: 10.1126/science.aaa7227. Epub 2015 May 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Cambridge Institute for Medical Research, Addenbrooke's Hospital, Cambridge CB2 0XY, UK. ; Department of Haematology, Cambridge Institute for Medical Research, Addenbrooke's Hospital, Cambridge CB2 0XY, UK. ; Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Cambridge CB10 1SA, UK. ; Peter MacCallum Cancer Centre, East Melbourne, Victoria 3002, Australia. ; Department of Medicine, Cambridge Institute for Medical Research, Addenbrooke's Hospital, Cambridge CB2 0XY, UK. pjl30@cam.ac.uk.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26022416" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Neoplasm/genetics/*metabolism ; *Chromosomal Position Effects ; Conserved Sequence ; Drosophila melanogaster/genetics/metabolism ; Evolution, Molecular ; *Gene Silencing ; Genes, Reporter ; Genetic Loci ; Green Fluorescent Proteins/genetics ; HeLa Cells ; Heterochromatin/metabolism ; Histones/*metabolism ; Humans ; Immunoprecipitation ; Multiprotein Complexes/genetics/*metabolism ; Nuclear Proteins/genetics/*metabolism ; Phosphoproteins/genetics/*metabolism ; Protein Methyltransferases/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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  • 6
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    HRD1 ubiquitinates MHC class I luminal residues [Cell Biology] (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-08-28
    Description: Misfolded MHC class I heavy chains (MHC I HCs) are targeted for endoplasmic reticulum (ER)-associated degradation (ERAD) by the ubiquitin E3 ligase HRD1, and E2 ubiquitin conjugating enzyme UBE2J1, and represent one of the few known endogenous ERAD substrates. The mechanism by which misfolded proteins are dislocated across the ER...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 7
    Electronic Resource
    Electronic Resource
    Regulation of MHC class I heterodimer stability and interaction with TAP by tapasin (1997)
    Springer
    Immunogenetics 46 (1997), S. 477-483 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Major histocompatibility complex (MHC) class I molecules are heterodimers of a class I heavy chain and β2-microglobulin that bind peptides supplied by the MHC region-encoded transporters associated with antigen processing (TAP). Peptide binding by class I heterodimers is necessary for their maturation into stable complexes and is dependent on their physical association with TAP. In human mutant 721.220 cells, however, a novel genetic defect causes the failure of class I heterodimers to associate with TAP. This deficiency correlates with lack of expression of a glycoprotein, tapasin (TAP-associated glycoprotein), which has been found in association with class I heterodimers and TAP. Employing a transcomplementation analysis, we obtained evidence co-localizing the genetic defect of mutant 220 cells and the structural or a regulatory gene controlling the expression of tapasin on the short arm of chromosome 6, which includes the MHC. Expression of tapasin and the normal interaction of class I heterodimers with TAP are concomitantly restored, indicating the probable function of tapasin as a physical link between these complexes. In further support of this model, the absence of tapasin in mutant 220 cells correlates with reduced class I heterodimer stability, suggesting that tapasin may stabilize class I heterodimers and thereby enhance their association with TAP. These results further implicate tapasin in a mechanism that promotes peptide binding by class I heterodimers through their interaction with TAP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510050308
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    Paper (German National Licenses)
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  • 8
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    Latency, chromatin remodeling, and reactivation of human cytomegalovirus in the dendritic cells of healthy carriers (2005)
    National Academy of Sciences
    Details
    Publication Date: 2005-02-28
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    The dominantly expressed class I molecule of the chicken MHC is explained by coevolution with the polymorphic peptide transporter (TAP) genes (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-05-02
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Down-regulation of NKG2D and NKp80 ligands by Kaposi's sarcoma-associated herpesvirus K5 protects against NK cell cytotoxicity (2008)
    National Academy of Sciences
    Details
    Publication Date: 2008-01-29
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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