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Michael J. Grey, Eva Cloots, Mariska S. Simpson, Nicole LeDuc, Yevgeniy V. Serebrenik, Heidi De Luca, Delphine De Sutter, Phi Luong, Jay R. Thiagarajah, Adrienne W. Paton, James C. Paton, Markus A. Seeliger, Sven Eyckerman, Sophie Janssens, Wayne I. Lencer
Grey et al. discover a mechanism by which the epithelial-specific ER stress sensor IRE1β acts as a negative regulator of IRE1α. IRE1β interacts directly with IRE1α to suppress XBP-1 splicing and modify the unfolded protein response to endoplasmic reticulum stress in intestinal epithelial cells.
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Wiebke Schormann, Santosh Hariharan, David W. Andrews
Schormann et al. provide a reference library of confocal micrographs of key organelles in live epithelial cells as landmarks and a derived feature set that can be used to assign protein localization throughout the secretory pathway and to key organelles via a quantitative unbiased image-based classifier.
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Alexander Schulz, Yuichi Sekine, Motunrayo J. Oyeyemi, Alexander J. Abrams, Manasa Basavaraju, Sung Min Han, Marco Groth, Helen Morrison, Stephen M. Strittmatter, Marc Hammarlund
GDPGP1 and its C. elegans homologue mcp-1 are identified as novel stress-responsive genes in neuronal cells. Stress-induced down-regulation of GDPGP1/mcp-1 reduces cellular glycogen levels and contributes to hypoxia sensitivity and neurodegeneration across species.
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Kangmin He, Eli Song, Srigokul Upadhyayula, Song Dang, Raphael Gaudin, Wesley Skillern, Kevin Bu, Benjamin R. Capraro, Iris Rapoport, Ilja Kusters, Minghe Ma, Tom Kirchhausen
Coat disassembly, driven by the Hsc70 “uncoating ATPase” and mediated by auxilin, occurs within seconds after vesicle release. Using single-molecule imaging, He et al. find that auxilins are absent from assembling pits. Therefore, Hsc70 is not responsible for the clathrin exchange during pit formation.
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Alexandra Colin, Gaëlle Letort, Nitzan Razin, Maria Almonacid, Wylie Ahmed, Timo Betz, Marie-Emilie Terret, Nir S. Gov, Raphaël Voituriez, Zoher Gueroui, Marie-Hélène Verlhac
Nucleus centering in mouse oocytes depends on a gradient of actin-positive vesicle persistence. Modeling coupled to 3D simulations and experimental testing of predictions coming from the simulations demonstrate that this gradient nonspecifically centers large objects during prophase I and meiosis I in oocytes.
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Sandra Sofía Edwards-Jorquera, Floris Bosveld, Yohanns A. Bellaïche, Ana-María Lennon-Duménil, Ana-María Lennon-Duménil, Álvaro Glavic, Álvaro Glavic
The authors show the dual regulation of phagosomal degradation and migration of Drosophila macrophages by Trpml, a lysosomal calcium channel. Trpml promotes cell migration by activating actomyosin contractility but supports phagosomal degradation through a myosin-independent mechanism.
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Arnaud Rondelet, Yu-Chih Lin, Divya Singh, Arthur T. Porfetye, Harish C. Thakur, Andreas Hecker, Pia Brinkert, Nadine Schmidt, Shweta Bendre, Franziska Müller, Lisa Mazul, Per O. Widlund, Tanja Bange, Michael Hiller, Ingrid R. Vetter, Alexander W. Bird
Clathrin stabilizes microtubules and promotes chromosome alignment during mitosis. Rondelet et al. show that the clathrin–adaptor interaction mechanism is repurposed to recruit GTSE1 to the spindle, which inhibits the microtubule depolymerase MCAK and promotes chromosome alignment by stabilizing nonkinetochore microtubules.

Related Articles from Rockefeller University Press

Current Issue
Volume 219,
Issue 1,
January 6, 2020
Reviews & Opinions
Review
Daniel Blumenthal, Janis K. Burkhardt
T cell activation requires force production at the immunological synapse. Blumenthal and Burkhardt describe how distinct actin structures contribute to this process, addressing canonical immunological models from a mechanobiology perspective.
Spotlight
Neel S. Singhal, Evan M. Lee, Dengke K. Ma
Singhal et al. highlight new findings from Schulz et al. regarding the survival-promoting effects of GDPGP1 in neural cells.
Spotlight
Linda Ma, Daniel A. Starr
Ma and Starr highlight new work from Rahman et al. that reveals new insight into the mechanisms controlling embryonic pronuclei fusion.

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