The EMBO Journal Table of Contents for 1 December 2014; Vol. 33, No. 23

1 December 2014 | Volume 33, Number 23 Submit Table of Contents Have you seen? Articles Retractions Volume 33, Number 23 Have you seen? Small, smaller… dendritic spine Super‐resolution microscopy describes actin dynamics and the spatial distribution of its regulators in dendritic spines, and reveals an organization different from traditional mechanisms of cortical actin control. Pietro Pilo Boyl and Walter Witke Published online 16.10.2014 MALT1 protease: equilibrating immunity versus tolerance The unexpected finding that the NF‐κB‐regulating MALT1 protease can act either immunogenic or tolerogenic in vivo bears important implications for the clinical development of MALT1 inhibitors. Arianna Bertossi and Daniel Krappmann Published online 31.10.2014 How stem cells get “turned on” Activation of muscle stem cells requires defined energy levels. Recent results determine autophagic flux as crucial contributor to the metabolic state of muscle stem cells. Amy J Wagers Published online 24.10.2014 Articles Nanoscale segregation of actin nucleation and elongation factors determines dendritic spine protrusion Super‐resolution microscopy reveals how nanoscale organization of F‐actin regulators correlates with changes in neuronal dendritic spine morphology. Branched F‐actin nucleation occurs at the vicinity of the postsynapse density, while elongation occurs at the tip of finger‐like protrusions. Anaël Chazeau, Amine Mehidi, Deepak Nair, Jérémie J Gautier, Cécile Leduc, Ingrid Chamma, Frieda Kage, Adel Kechkar, Olivier Thoumine, Klemens Rottner, Daniel Choquet, Alexis Gautreau, Jean‐Baptiste Sibarita, and Grégory Giannone Published online 07.10.2014 Malt1 protease inactivation efficiently dampens immune responses but causes spontaneous autoimmunity The protease activity of MALT1 is essential for the adaptive immune response, the generation of Treg cells, and the prevention of autoimmune gastritis. Maike Jaworski, Ben J Marsland, Jasmine Gehrig, Werner Held, Stéphanie Favre, Sanjiv A Luther, Mai Perroud, Déla Golshayan, Olivier Gaide, and Margot Thome Published online 15.10.2014 Induction of autophagy supports the bioenergetic demands of quiescent muscle stem cell activation Tang and Rando report induction of autophagy by the nutrient sensor SIRT1 as crucial energy provider for efficient proliferation/differentiation in quiescent muscle satellite cells in vivo. Ann H Tang and Thomas A Rando Published online 14.10.2014 Parkin‐independent mitophagy requires Drp1 and maintains the integrity of mammalian heart and brain In vivo analysis reveals a synergistic role of mitochondrial fission protein Drp1 and Parkinson's disease‐associated ligase parkin in the regulation of ubiquitination and degradation of mitochondria in the heart and brain. Yusuke Kageyama, Masahiko Hoshijima, Kinya Seo, Djahida Bedja, Polina Sysa‐Shah, Shaida A Andrabi, Weiran Chen, Ahmet Höke, Valina L Dawson, Ted M Dawson, Kathleen Gabrielson, David A Kass, Miho Iijima, and Hiromi Sesaki Published online 27.10.2014 IκΒα inhibits apoptosis at the outer mitochondrial membrane independently of NF‐κB retention IkBα interacts with VDAC and hexokinase II at mitochondria to prevent cytochrome c release and apoptosis of tumor cells, independently of its function as an NF‐κB inhibitor. Evangelos Pazarentzos, Anne‐Laure Mahul‐Mellier, Christoph Datler, Wanwisa Chaisaklert, Ming‐Shih Hwang, Jan Kroon, Ding Qize, Foy Osborne, Abdullah Al‐Rubaish, Amein Al‐Ali, Nicholas D Mazarakis, Eric O Aboagye, and Stefan Grimm Published online 31.10.2014 The exosome‐binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase Mtr4 is an RNA helicase involved in targeting nuclear RNAs for degradation. A new crystal structure reveals the basis for Mtr4 recruitment on the nuclear exosome through a direct interaction with Rrp6 and Rrp47. Benjamin Schuch, Monika Feigenbutz, Debora L Makino, Sebastian Falk, Claire Basquin, Phil Mitchell, and Elena Conti Published online 15.10.2014 Structure of the Rad50 DNA double‐strand break repair protein in complex with DNA The first structural insight into DNA binding by an SMC protein reveals the importance of Rad50–DNA interaction for some but not other functions of the MRN complex. Anna Rojowska, Katja Lammens, Florian U Seifert, Carolin Direnberger, Heidi Feldmann, and Karl‐Peter Hopfner Published online 27.10.2014 APC/CCdh1 controls CtIP stability during the cell cycle and in response to DNA damage Regulation of CtIP, a DNA‐end resection factor involved in repair pathway choice, represents a new means of genome stability control by the cell cycle ubiquitin ligase APC/C. Lorenzo Lafranchi, Harmen R de Boer, Elisabeth GE de Vries, Shao‐En Ong, Alessandro A Sartori, and Marcel ATM van Vugt Published online 27.10.2014 Retractions Retraction: ‘A subfamily of RNA‐binding DEAD‐box proteins acts as an estrogen receptor α coactivator through the N‐terminal activation domain (AF‐1) with an RNA coactivator, SRA’ Michiko Watanabe, Junn Yanagisawa, Hirochika Kitagawa, Ken‐ichi Takeyama, Satoko Ogawa, Yukitomo Arao, Miyuki Suzawa, Yoko Kobayashi, Tetsu Yano, Hiroyuki Yoshikawa, Yoshikazu Masuhiro, and Shigeaki Kato Published online 30.11.2014 Retraction: ‘Transrepression by a liganded nuclear receptor via a bHLH activator through co‐regulator switching’ Akiko Murayama, Mi‐sun Kim, Junn Yanagisawa, Ken‐ichi Takeyama, and Shigeaki Kato Published online 30.11.2014 Retraction: ‘Ligand‐induced transrepression by VDR through association of WSTF with acetylated histones’ Ryoji Fujiki, Mi‐sun Kim, Yasumasa Sasaki, Kimihiro Yoshimura, Hirochika Kitagawa, and Shigeaki Kato Published online 30.11.2014 Retraction: ‘A cell cycle‐dependent co‐repressor mediates photoreceptor cell‐specific nuclear receptor function’ Shinichiro Takezawa, Atsushi Yokoyama, Maiko Okada, Ryoji Fujiki, Aya Iriyama, Yasuo Yanagi, Hiroaki Ito, Ichiro Takada, Masahiko Kishimoto, Atsushi Miyajima, Ken‐ichi Takeyama, Kazuhiko Umesono, Hirochika Kitagawa, and Shigeaki Kato Published online 30.11.2014   Unsubscribe from or edit your subscription for this service. 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