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- Scientific ReportDnaQ exonuclease‐like domain of Cas2 promotes spacer integration in a type I‐E CRISPR‐Cas system
- Gediminas Drabavicius1,
- Tomas Sinkunas1,
- Arunas Silanskas1,
- Giedrius Gasiunas1,2,
- Česlovas Venclovas1 and
- Virginijus Siksnys (siksnys{at}ibt.lt)*,1
- 1Institute of Biotechnology, Vilnius University, Vilnius, Lithuania
- 2Present Address: CasZyme, Vilnius, Lithuania
- ↵*Corresponding author. Tel: +370 5 2234354; E‐mail: siksnys{at}ibt.lt
The CRISPR4‐Cas system of the Streptococcus thermophilus spacer integration complex contains the Cas2‐DnaQ fusion protein. This study shows that the DnaQ domain is required for the processing of the protospacers prior to integration into the CRISPR array.
Synopsis
The CRISPR4‐Cas system of the Streptococcus thermophilus spacer integration complex contains the Cas2‐DnaQ fusion protein. This study shows that the DnaQ domain is required for the processing of the protospacers prior to integration into the CRISPR array.
The DnaQ domain fused to Cas2 in the S. thermophilus CRISPR4‐Cas system is a 3′–5′ exonuclease.
The DnaQ domain in the Cas1:Cas2‐DnaQ complex trims 3′ ends of protospacers to generate overhangs optimal for integration.
Cas1:Cas2‐DnaQ integrates trimmed protospacers into the CRISPR array.
EMBO Reports (2018) e45543
- Received November 24, 2017.
- Revision received May 4, 2018.
- Accepted May 8, 2018.
- © 2018 The Authors
- ArticleMap7/7D1 and Dvl form a feedback loop that facilitates microtubule remodeling and Wnt5a signaling
- Koji Kikuchi (kojik{at}kumamoto-u.ac.jp)*,1,
- Akira Nakamura2,3,
- Masaki Arata4,
- Dongbo Shi5,
- Mami Nakagawa5,
- Tsubasa Tanaka2,3,
- Tadashi Uemura4,
- Toshihiko Fujimori5,
- Akira Kikuchi6,
- Akiyoshi Uezu1,
- Yasuhisa Sakamoto1 and
- Hiroyuki Nakanishi (hnakanis{at}gpo.kumamoto-u.ac.jp)*,1
- 1Department of Molecular Pharmacology, Graduate School of Medical Sciences, Kumamoto University, Chuo‐ku Kumamoto, Japan
- 2Department of Germline Development, Institute of Molecular Embryology and Genetics, Kumamoto University, Chuo‐ku Kumamoto, Japan
- 3Graduate School of Pharmaceutical Sciences, Kumamoto University, Chuo‐ku Kumamoto, Japan
- 4Graduate School of Biostudies, Kyoto University, Sakyo‐ku Kyoto, Japan
- 5Division of Embryology, National Institute for Basic Biology, Okazaki Aichi, Japan
- 6Department of Molecular Biology and Biochemistry, Graduate School of Medicine, Osaka University, Suita Osaka, Japan
- ↵*
Corresponding author (Lead contact): +Tel: +81 96 373 5076; E‐mail: kojik{at}kumamoto-u.ac.jp
Corresponding author. +Tel: +81 96 373 5074; E‐mail: hnakanis{at}gpo.kumamoto-u.ac.jp
Microtubule‐associated proteins Map7/7D1/Ensconsin and Dishevelled form an evolutionarily conserved axis in β‐catenin‐independent Wnt signaling and/or PCP formation.
Synopsis
Microtubule‐associated proteins Map7/7D1/Ens and Dishevelled form an evolutionarily conserved axis in β‐catenin‐independent Wnt signaling and/or PCP formation.
Map7/7D1 cooperate with a Kinesin‐1 Kif5b to coordinate Dishevelled dynamics and microtubule remodeling in the Wnt5a signaling pathway.
Map7/7D1 and their fly homolog Ens show planar‐polarized distribution in both mouse and fly epithelia.
Ens is required for polarized localization of Dishevelled during PCP formation in pupal wing epithelia.
Map7/7D1/Ens play an evolutionarily conserved role in Dishevelled localization.
EMBO Reports (2018) e45471
- Received November 9, 2017.
- Revision received April 28, 2018.
- Accepted May 8, 2018.
- © 2018 The Authors
- ArticleInfection with the dengue RNA virus activates TLR9 signaling in human dendritic cells
- Jenn‐Haung Lai (laiandho{at}gmail.com)*,1,2,
- Mei‐Yi Wang1,
- Chuan‐Yueh Huang3,
- Chien‐Hsiang Wu1,
- Li‐Feng Hung3,
- Chia‐Ying Yang1,
- Po‐Yuan Ke4,
- Shue‐Fen Luo1,
- Shih‐Jen Liu5 and
- Ling‐Jun Ho (lingjunho{at}nhri.org.tw)*,3
- 1Division of Allergy, Immunology, and Rheumatology, Department of Internal Medicine, Chang Gung Memorial Hospital, Chang Gung University, Tao‐Yuan, Taiwan
- 2Graduate Institute of Clinical Research, National Defense Medical Center, Taipei, Taiwan
- 3Institute of Cellular and System Medicine, National Health Research Institute, Zhunan, Miaoli, Taiwan
- 4Department of Biochemistry & Molecular Biology, College of Medicine, Chang Gung University, Tao‐Yuan, Taiwan
- 5National Institute of Infectious Diseases and Vaccinology, National Health Research Institutes, Zhunan, Miaoli, Taiwan
- ↵*
Corresponding author. Tel: +886 2 8791 8382; Fax: +886 2 8791 8382; E‐mail: laiandho{at}gmail.com
Corresponding author. Tel: +886 2 8791 8382; Fax: +886 2 8791 8382; E‐mail: lingjunho{at}nhri.org.tw
Infection of human dendritic cells with a dengue RNA virus activates TLR9—known to recognize bacterial or viral DNA but not viral RNA—through inducing mitochondrial DNA release into the cytosol.
Synopsis
Infection of human dendritic cells with a dengue RNA virus activates TLR9—known to recognize bacterial or viral DNA but not viral RNA—through inducing mitochondrial DNA release into the cytosol.
Infection of human DCs with DENV induces ROS generation, inflammasome activation, oxidization of mtDNA and opening of the mitochondrial permeability transition pores resulting in the release of both non‐oxidized and oxidized mtDNA into the cytosol.
Cytosolic mtDNA increases TLR9 expression, binds to TLR9 and induces immune activation such as anti‐viral interferon production.
The significance of TLR9 in DENV infection is confirmed by examining bone marrow‐derived dendritic cells prepared from Tlr9‐knockout mice.
EMBO Reports (2018) e46182
- Received March 25, 2018.
- Revision received May 14, 2018.
- Accepted May 18, 2018.
- © 2018 The Authors
- Scientific ReportYAP and TAZ are essential for basal and squamous cell carcinoma initiation
- Maud Debaugnies1,†,
- Adriana Sánchez‐Danés1,†,
- Sandrine Rorive2,
- Maylis Raphaël1,
- Mélanie Liagre1,
- Marie‐Astrid Parent1,
- Audrey Brisebarre1,
- Isabelle Salmon2 and
- Cédric Blanpain (cedric.blanpain{at}ulb.ac.be)*,1,3
- 1Laboratory of Stem Cells and Cancer, Université Libre de Bruxelles, Brussels, Belgium
- 2Department of Pathology, Erasme University Hospital, University Libre de Bruxelles, Brussels, Belgium
- 3WELBIO, Université Libre de Bruxelles, Brussels, Belgium
- ↵*Corresponding author. Tel: +32 2555 4175; E‐mail: cedric.blanpain{at}ulb.ac.be
↵† These authors contributed equally to this work
The Hippo pathway transcription factors YAP and TAZ are expressed and active in basal and squamous cell carcinoma in mice and humans. Conditional deletion of YAP and TAZ in mouse models prevents skin cancer initiation.
Synopsis
The Hippo pathway transcription factors YAP and TAZ are expressed and active in basal and squamous cell carcinoma in mice and humans. Conditional deletion of YAP and TAZ in mouse models prevents skin cancer initiation.
YAP and TAZ are expressed in mouse and human basal and squamous cell carcinoma.
YAP and TAZ are mainly nuclear in basal and squamous cell carcinoma.
Basal and squamous cell carcinomas express YAP gene signatures.
Conditional deletion of YAP and TAZ prevents skin cancer initiation in mice.
EMBO Reports (2018) e45809
- Received January 16, 2018.
- Revision received May 4, 2018.
- Accepted May 14, 2018.
- © 2018 The Authors
- Science & SocietyThe revival of the extended phenotypeAfter more than 30 years, Dawkins’ Extended Phenotype hypothesis is enriching evolutionary biology and inspiring potential applications
After more than 30 years, Dawkins’ Extended Phenotype hypothesis is enriching evolutionary biology and inspiring potential applications
- Philip Hunter (ph{at}philiphunter.com)1
When Richard Dawkins proposed the Extended Phenotype hypothesis, it was an interesting addition to explain beaver dams or termite nests. With new technologies and a renewed interest, it is now inspiring research to understand co‐evolution in ecosystems and applications in agriculture and conservation.
EMBO Reports (2018) e46477
- © 2018 The Author
- ArticleIdentification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites
- Thomas Di Mattia1,2,3,4,
- Léa P Wilhelm1,2,3,4,
- Souade Ikhlef5,
- Corinne Wendling1,2,3,4,
- Danièle Spehner1,2,3,4,
- Yves Nominé1,2,3,4,
- Francesca Giordano6,
- Carole Mathelin1,2,3,4,7,
- Guillaume Drin5,
- Catherine Tomasetto (catherine-laure.tomasetto{at}igbmc.fr)*,1,2,3,4 and
- Fabien Alpy (fabien.alpy{at}igbmc.fr)*,1,2,3,4
- 1Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France
- 2Institut National de la Santé et de la Recherche Médicale (INSERM), U1258, Illkirch, France
- 3Centre National de la Recherche Scientifique (CNRS), UMR7104, Illkirch, France
- 4Université de Strasbourg, Illkirch, France
- 5CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d'Azur, Valbonne, France
- 6Institut de Biologie Intégrative de la Cellule, CEA, CNRS, Paris‐Sud University Paris‐Saclay University, Gif‐sur‐Yvette Cedex 91198, France
- 7Senology Unit, Strasbourg University Hospital (CHRU), Hôpital de Hautepierre, Strasbourg, France
- ↵*
Corresponding author. Tel: +33 3 88 65 34 24; Fax: +33 3 88 65 32 01; E‐mail: catherine-laure.tomasetto{at}igbmc.fr
Corresponding author. Tel: +33 3 88 65 35 19; Fax: +33 3 88 65 32 01; E‐mail: fabien.alpy{at}igbmc.fr
The endoplasmic reticulum (ER) makes physical contacts with most cellular organelles. This study identifies MOSPD2 as a new ER‐anchored receptor, which binds FFAT‐motif containing proteins in other organelles such as Golgi, endosomes and mitochondria.
Synopsis
The endoplasmic reticulum (ER) makes physical contacts with most cellular organelles. MOSPD2 (motile sperm domain‐containing protein 2) is a new ER‐anchored receptor, which binds FFAT (two phenylalanines in an acidic track)‐motif containing proteins. Analogous to vesicle‐associated membrane protein‐associated protein (VAP)‐A and VAP‐B, MOSPD2 mediates the formation of contact sites between the ER and a variety of organelles (including endosomes, mitochondria or Golgi).
Motile sperm domain‐containing protein 2 (MOSPD2) is a novel ER‐anchored VAP homolog.
The FFAT motif is recognized by the Major Sperm Protein (MSP) domain of MOSPD2.
MOSPD2 interacts with a variety of organelle (endosomes, mitochondria or Golgi)‐bound proteins and thereby builds membrane contact sites.
EMBO Reports (2018) e45453
- Received November 8, 2017.
- Revision received April 27, 2018.
- Accepted May 7, 2018.
- © 2018 The Authors. Published under the terms of the CC BY NC ND 4.0 license
This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs 4.0 License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
- Science & SocietyRisk in synthetic biology—Views from the labEarly career scientists’ concerns about synthetic biology open up new perspectives on risk and responsibility in research
Early career scientists’ concerns about synthetic biology open up new perspectives on risk and responsibility in research
Gauging young scientists’ concerns about and views of research in synthetic biology opens up new perspectives on career paths, economic expectations and mental health issues in cutting‐edge research.
EMBO Reports (2018) e45958
- © 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.
