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- ArticleKAP1 regulates endogenous retroviruses in adult human cells and contributes to innate immune control
- Christopher HC Tie1,
- Liane Fernandes1,
- Lucia Conde2,
- Luisa Robbez‐Masson1,
- Rebecca P Sumner1,
- Tom Peacock1,
- Maria Teresa Rodriguez‐Plata1,
- Greta Mickute1,
- Robert Gifford3,
- Greg J Towers1,
- Javier Herrero2 and
- Helen M Rowe (h.rowe{at}ucl.ac.uk)*,1
- 1Division of Infection and Immunity, University College London, London, UK
- 2Bill Lyons Informatics Centre, UCL Cancer Institute, London, UK
- 3MRC‐University of Glasgow Centre for Virus Research, Glasgow, UK
- ↵*Corresponding author. Tel: +44 207 6796926; E‐mail: h.rowe{at}ucl.ac.uk
KAP1 represses ERVs during development by interacting with their repetitive sequences through KRAB‐zinc finger proteins. KAP1 regulation of ERVs persists in adult human cells, which promotes genome stability and reduces autoimmune responses.
Synopsis
KAP1 represses ERVs during development by interacting with their repetitive sequences through KRAB‐zinc finger proteins. KAP1 regulation of ERVs persists in adult human cells, which promotes genome stability and reduces autoimmune responses.
KAP1 regulation of ERVs persists in differentiated human cells including adult PBMCs.
KAP1 regulates zinc finger genes, HERV‐T, HERV‐K14C and HERV‐S, present in diverse mammals.
KAP1 inactivation leads to the induction of innate immune genes through MAVS‐dependent signalling.
EMBO Reports (2018) e45000
- Received August 11, 2017.
- Revision received June 21, 2018.
- Accepted July 9, 2018.
- © 2018 The Authors. Published under the terms of the CC BY 4.0 license
This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Science & SocietyA planet too rich in fibreMicrofibre pollution may have major consequences on the environment and human health
Microfibre pollution may have major consequences on the environment and human health
- Melissa Suran (mnsuran{at}u.northwestern.edu)1
Plastic microfibers from synthetic clothing have become pervasive in the environment, and appear even in drinking water and food products with unknown consequences for human and environmental health.
EMBO Reports (2018) e46701
- © 2018 The Author
- ArticlePlanar cell polarity gene Fuz triggers apoptosis in neurodegenerative disease models
- Zhefan Stephen Chen1,2,
- Li Li1,2,
- Shaohong Peng1,2,
- Francis M Chen3,
- Qian Zhang1,2,
- Ying An1,2,
- Xiao Lin2,
- Wen Li2,
- Alex Chun Koon1,2,
- Ting‐Fung Chan2,3,4,5,
- Kwok‐Fai Lau2,3,4,
- Jacky Chi Ki Ngo2,3,
- Wing Tak Wong3,
- Kin Ming Kwan3,6,7 and
- Ho Yin Edwin Chan (hyechan{at}cuhk.edu.hk)*,1,2,3,4,5
- 1Laboratory of Drosophila Research, School of Life Sciences Faculty of Science The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China
- 2Biochemistry Program, School of Life Sciences Faculty of Science The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China
- 3Cell and Molecular Biology Program, School of Life Sciences Faculty of Science The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China
- 4Molecular Biotechnology Program, School of Life Sciences, Faculty of Science, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China
- 5Gerald Choa Neuroscience Centre, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China
- 6Partner State Key Laboratory of Agrobiotechnology (CUHK), The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China
- 7Centre for Cell and Developmental Biology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, China
- ↵*Corresponding author. Tel: +852 3943 4021; Fax: +852 2603 7732; E‐mail: hyechan{at}cuhk.edu.hk
The planar cell polarity protein Fuz has a pro‐apoptotic function in neurons and contributes to polyQ‐induced neurodegeneration in Drosophila. In multiple neurodegenerative disease models Fuz expression is upegulated due a hypomethylation of its promoter.
Synopsis
The planar cell polarity protein Fuz has a pro‐apoptotic function in neurons and contributes to polyQ‐induced neurodegeneration in Drosophila. In multiple neurodegenerative disease models Fuz expression is upegulated due a hypomethylation of its promoter.
Fuz stimulates a Dvl/Rac1 GTPase/MEKK1/JNK/caspase signaling pathway to trigger apoptosis.
YY1 inhibits Fuz transcription by promoting DNA hypermethylation.
Fuz promoter hypomethylation and transcriptional upregulation are observed in polyQ, amyloid beta peptide, Tau and α‐synuclein models of neurodegeneration.
EMBO Reports (2018) e45409
- Received October 31, 2017.
- Revision received June 15, 2018.
- Accepted June 22, 2018.
- © 2018 The Authors
- ArticleSPATC1L maintains the integrity of the sperm head‐tail junction
- Jihye Kim1,
- Jun Tae Kwon1,
- Juri Jeong1,
- Jaehwan Kim1,
- Seong Hyeon Hong1,
- Jinyoung Kim1,
- Zee Yong Park1,
- Kyung Hwun Chung1,
- Edward M Eddy2 and
- Chunghee Cho (choch{at}gist.ac.kr)*,1
- 1School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Korea
- 2Reproductive and Developmental Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA
- ↵*Corresponding author. Tel: +82 62 715 2490; E‐mail: choch{at}gist.ac.kr
The male‐germ‐cell‐specific protein SPATC1L localizes to the neck region of the sperm and associates with PKA that phosphorylates CABPZB. SPATC1L maintains the stability of the sperm head‐tail junction.
Synopsis
The male‐germ‐cell‐specific protein SPATC1L localizes to the neck region of the sperm and associates with PKA that phosphorylates CABPZB. SPATC1L maintains the stability of the sperm head‐tail junction.
SPATC1L localizes to the connecting piece of testicular sperm and interacts with the regulatory subunit of PKA, increasing PKA activity.
SPATC1L potentially promotes PKA‐mediated CAPZB phosphorylation and regulates F‐actin dynamics during spermiogenesis.
Loss of SPATC1L in mice results in separation of sperm heads from tails leading to male sterility.
EMBO Reports (2018) e45991
- Received February 21, 2018.
- Revision received June 25, 2018.
- Accepted July 3, 2018.
- © 2018 Gwangju Institue of Science and Technology
- ArticleStructural basis for specific inhibition of the highly sensitive ShHTL7 receptor
- Umar Shahul Hameed1,†,
- Imran Haider2,†,
- Muhammad Jamil2,
- Boubacar A Kountche2,
- Xianrong Guo3,
- Randa A Zarban2,
- Dongjin Kim2,
- Salim Al‐Babili (salim.babili{at}kaust.edu.sa)*,2 and
- Stefan T Arold (stefan.arold{at}kaust.edu.sa)*,1
- 1Division of Biological and Environmental Sciences and Engineering, Computational Bioscience Research Center, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia
- 2Division of Biological and Environmental Sciences and Engineering, The Bioactives Lab, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia
- 3Core Labs, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia
- ↵*
Corresponding author. Tel: +966 1280 82565; E‐mail: salim.babili{at}kaust.edu.sa
Corresponding author. Tel: +966 1280 82557; E‐mail: stefan.arold{at}kaust.edu.sa
↵† These authors contributed equally to this work
Germination of the parasitic plant Striga depends on ShHTL receptors that sense host‐released strigolactones. This study shows that Triton X‐100 inhibits Striga hermonthica seed germination without affecting host plants by specifically plugging the catalytic site of ShHTL7, thus interfering with downstream signaling.
Synopsis
The parasitic plant Striga controls its germination through the ShHTL family of proteins that sense the presence of host‐produced strigolactones. This study shows that Triton X‐100 inhibits Striga hermonthica seed germination without affecting host plants by specifically plugging the catalytic site of ShHTL7, the most potent ShHTL member, precluding its structural rearrangements required for downstream signaling.
Triton X‐100 and related molecules are promising lead compounds for inhibiting S. hermonthica seed germination without affecting the host plant.
The X‐ray structure of ShHTL7 explains how Triton X‐100 precludes structural changes required for downstream signaling.
ShHTL7‐specific inhibition by Triton X‐100 demonstrates the dominant role of this particular ShHTL receptor for Striga germination.
EMBO Reports (2018) e45619
- Received December 9, 2017.
- Revision received June 19, 2018.
- Accepted June 20, 2018.
- © 2018 The Authors. Published under the terms of the CC BY 4.0 license
This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- ArticleChemical and genetic control of IFNγ‐induced MHCII expression
- Ruud H Wijdeven1,
- Marvin M van Luijn2,
- Annet F Wierenga‐Wolf2,
- Jimmy J Akkermans1,
- Peter J van den Elsen3,
- Rogier Q Hintzen2,4 and
- Jacques Neefjes (j.j.c.neefjes{at}lumc.nl)*,1
- 1Department of Cell and Chemical Biology, LUMC, Leiden, The Netherlands
- 2Department of Immunology, MS Center ErasMS, Erasmus MC, University Medical Center, Rotterdam, The Netherlands
- 3Department of Immunohematology and Blood Transfusion, LUMC, Leiden, The Netherlands
- 4Department of Neurology, MS Center ErasMS, Erasmus MC, University Medical Center, Rotterdam, The Netherlands
- ↵*Corresponding author. Tel: +31715263800; E‐mail: j.j.c.neefjes{at}lumc.nl
IFNγ‐induced expression of MHC class II molecules in non‐immune tissue is critical for inflammation and autoimmune diseases. This study identifies novel genetic and chemical factors that control MHCII expression, and potentially autoimmune diseases.
Synopsis
IFNγ‐induced expression of MHC class II molecules in non‐immune tissue is critical for inflammation and autoimmune diseases. This study identifies novel genetic and chemical factors that control MHCII expression, and potentially autoimmune diseases.
Oxidative stressors affect IFNγ‐induced MHC class II expression in non‐haematopoietic tissues.
A Keap1‐Cul3‐MYST1‐BPTF axis and HDAC1/2 control IFNγ‐induced MHC class II expression.
These pathways are targeted by arsenite but also by autoimmune suppressing drugs such as DMF.
EMBO Reports (2018) e45553
- Received November 27, 2017.
- Revision received June 5, 2018.
- Accepted June 24, 2018.
- © 2018 The Authors
- Scientific ReportSirt1 protects from K‐Ras‐driven lung carcinogenesis
- Luis Filipe Costa‐Machado1,
- Roberto Martín‐Hernández2,
- Miguel Ángel Sanchez‐Luengo3,
- Katharina Hess4,
- Claudia Vales‐Villamarin1,
- Marta Barradas1,
- Cian Lynch4,5,
- Daniel de la Nava1,
- Alberto Diaz‐Ruiz6,7,
- Rafael de Cabo6,7,
- Marta Cañamero8,9,
- Lola Martinez3,
- Marta Sanchez‐Carbayo10,
- Daniel Herranz (dh710{at}cinj.rutgers.edu)*,4,11,
- Manuel Serrano (manuel.serrano{at}irbbarcelona.org)*,4,5,12 and
- Pablo J Fernandez‐Marcos (pablojose.fernandez{at}imdea.org)*,1,4
- 1Bioactive Products and Metabolic Syndrome Group – BIOPROMET, Madrid Institute for Advanced Studies ‐ IMDEA Food, CEI UAM+CSIC, Madrid, Spain
- 2GENYAL Nutrigenomic Platform, Madrid Institute for Advanced Studies ‐ IMDEA Food, CEI UAM+CSIC, Madrid, Spain
- 3Flow Cytometry Unit, Spanish National Cancer Research Center (CNIO), Madrid, Spain
- 4Tumor Suppression Group, Spanish National Cancer Research Center (CNIO), Madrid, Spain
- 5Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology (BIST), Barcelona, Spain
- 6Translational Gerontology Branch, National Institute on Aging, National Institutes of Health, Baltimore, MD, USA
- 7Nutritional Interventions Group, Precision Nutrition and Aging, Madrid Institute for Advanced Studies ‐ IMDEA Food, CEI UAM+CSIC, Madrid, Spain
- 8Histopathology Unit, Spanish National Cancer Research Center (CNIO), Madrid, Spain
- 9Pathology and Tissue Analysis, Pharma Research and Early Development Roche Innovation Centre, Munich, Germany
- 10Translational Oncology Lab, Lucio Lascaray Research Center, University of the Basque Country, Vitoria‐Gasteiz, Spain
- 11Rutgers Cancer Institute of New Jersey and Department of Pharmacology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, New Brunswick, NJ, USA
- 12Catalan Institution for Research and Advanced Studies (ICREA), Barcelona, Spain
- ↵*
Corresponding author. Tel: +17322354064; E‐mail: dh710{at}cinj.rutgers.edu
Corresponding author. Tel: +34934020287; E‐mail: manuel.serrano{at}irbbarcelona.org
Corresponding author. Tel: +34917278100; E‐mail: pablojose.fernandez{at}imdea.org
The NAD+‐dependent deacetylase SIRT1 can be oncogenic or tumor suppressive depending on the tissue. This study demonstrates a tumor suppressive role for SIRT1 in K‐RAS‐driven lung adenocarcinomas in mice and humans.
Synopsis
The NAD+‐dependent deacetylase SIRT1 can be oncogenic or tumor suppressive depending on the tissue. This study demonstrates a tumor suppressive role for SIRT1 in K‐RAS‐driven lung adenocarcinomas in mice and humans.
Sirt1 protects against oncogenic K‐Ras‐driven lung adenocarcinoma in mice and humans.
Sirt1 overexpression in mouse pneumocytes alters pathways involved in tumor development.
Oncogenic K‐Ras activation reduces Sirt1 protein stability through the MAPK pathway.
EMBO Reports (2018) e43879
- Received December 30, 2016.
- Revision received June 18, 2018.
- Accepted June 22, 2018.
- © 2018 The Authors
