Cell

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  • 659 Drp1-Zip1 Interaction Regulates Mitochondrial Quality Surveillance System
    DOI: 10.1016/j.molcel.2018.11.009, Cho et al. report that Drp1 that is the executioner for mitochondrial fission can reduce the mitochondrial membrane potential (MMP) during the mitochondrial division, and this new action helps identify bad sectors in the interconnected mitochondria. [Hyo Min Cho, Jae Ryun Ryu, You]
  • 658 Bidirectional Control of Autophagy by BECN1 BARA Domain Dynamics
    DOI: 10.1016/j.molcel.2018.10.035, A structural, biochemical, and biophysical study of PI 3-kinase regulation by Rubicon, HIV-1 Nef, and an autophagy-activating peptide shows how BECN1 BARA domain is switched on and off in both physiology and infection, and how it can be targeted for therapeutic ind... [Chunmei Chang, Lindsey N. Youn]
  • 657 Role of Mitochondria in Ferroptosis
    DOI: 10.1016/j.molcel.2018.10.042, Gao et al. show that mitochondria play a crucial and proactive role in cysteine-deprivation-induced ferroptosis but not in GPX4 inhibition-induced ferroptosis. Mechanistically, the mitochondrial TCA cycle and electron transport chain promote cysteine-deprivation... [Minghui Gao, Junmei Yi, Jiajun]
  • 656 The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Spec...
    DOI: 10.1016/j.molcel.2018.11.012, FUS is an RNA binding protein associated with several neurodegenerative diseases, for which mode of nucleic acid binding has been elusive. Loughlin et al. solved the solution structure of FUS bound to RNA, revealing a sequence-specific recognition for a GGU moti... [Fionna E. Loughlin, Peter J. L]
  • 655 ORP2 Delivers Cholesterol to the Plasma Membrane in Exchange for Phosphatidylinositol 4, 5-Bisphosphate (PI(4,5)P2)
    DOI: 10.1016/j.molcel.2018.11.014, Cholesterol and PI(4,5)P2 are two key lipid components of the plasma membrane. Wang et al. identify ORP2 as a unique transporter of both cholesterol and PI(4,5)P2. ORP2 regulates the levels of both cholesterol and PI(4,5)P2 on the plasma membrane, and ORP2 forms... [Huan Wang, Qianli Ma, Yanfei Q]
  • 654 Genome-wide CRISPR Analysis Identifies Substrate-Specific Conjugation Modules in ER-Associated Degradation
    DOI: 10.1016/j.molcel.2018.11.015, ER-associated degradation (ERAD) is a protein quality control system that targets misfolded proteins in the early secretory pathway to the cytosol for degradation. Leto et al. use a functional genomic approach to identify distinct cellular machinery that destroy... [Dara E. Leto, David W. Morgens]
  • 653 A Compact, High-Accuracy Cas9 with a Dinucleotide PAM for In Vivo Genome Editing
    DOI: 10.1016/j.molcel.2018.12.003, Optimal viral delivery of Cas9 genome editors requires orthologs that are more compact than the commonly used SpyCas9, but existing platforms exhibit targeting restrictions, accuracy limitations, or both. Edraki et al. describe Nme2Cas9, which can edit a high de... [Alireza Edraki, Aamir Mir, Rae]
  • 652 RSC-Associated Subnucleosomes Define MNase-Sensitive Promoters in Yeast
    DOI: 10.1016/j.molcel.2018.10.046, Brahma and Henikoff resolve the composition of MNase-sensitive particles at yeast promoters by showing that these are RSC- and GRF-associated, partially unwrapped nucleosomal intermediates. For this, Brahma and Henikoff combined a targeted chromatin cleavage and re... [Sandipan Brahma, Steven Heniko]
  • 651 The F-Box Domain-Dependent Activity of EMI1 Regulates PARPi Sensitivity in Triple-Negative Breast Cancers
    DOI: 10.1016/j.molcel.2018.11.003, Marzio et al. report that cellular levels of RAD51 are kept in check by EMI1-mediated degradation. Upon DNA damage, CHK1 phosphorylation of RAD51 on Thr309 counteracts this event, allowing RAD51 accumulation and HRR. Downregulation of EMI1 in BRCA1-deficient bre... [Antonio Marzio, Joseph Puccini]
  • 650 Molecular Basis for the Single-Nucleotide Precision of Primary microRNA Processing
    DOI: 10.1016/j.molcel.2018.11.005, Target specificity of microRNA is determined by DROSHA cleavage sites. Kwon et al. show how DROSHA precisely selects the cleavage sites using the interaction between its double-stranded RNA-binding domain (dsRBD) and the mGHG motif of the primary microRNA. [S. Chul Kwon, S. Chan Baek, Ye]