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Showing 1–23 of 23 results
Advanced filters: Author: Oliver Daumke Clear advanced filters

  • The conserved eukaryotic heterotrimeric NatC complex co-translationally acetylates the N-termini of numerous target proteins. Here, the authors provide insights into the catalytic mechanism of NatC by determining the crystal structures of Saccharomyces cerevisiae NatC in the absence and presence of cofactors and peptide substrates and reveal the molecular basis of substrate binding by further biochemical analyses.

    • Stephan Grunwald
    • Linus V. M. Hopf
    • Oliver Daumke
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates the function of membrane proteins. Here, the authors map lysine acetylation predominantly in membrane-interaction regions in peripheral membrane proteins and show with three candidate proteins how lysine acetylation is a regulator of membrane protein function.

    • Alan K. Okada
    • Kazuki Teranishi
    • Ralf Langen
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Structural details of mouse EHD2 are provided along with in vitro and in vivo assays, showing how an EHD oligomer is formed and how perpendicular curvature stresses on a membrane surface can result in remodelling of membranes by EHD oligomeric rings. The functional implications of the EHD2 structure for understanding of membrane deformation are also discussed.

    • Oliver Daumke
    • Richard Lundmark
    • Harvey T. McMahon
    Research
    Nature
    Volume: 449, P: 923-927

  • The MICOS complex has an essential role in crista junction formation and mitochondrial inner membrane morphology. Here, the authors show that one of its components, Mic60, known to form contact sites between inner and outer membranes, also displays membrane-shaping activity.

    • Manuel Hessenberger
    • Ralf M. Zerbes
    • Oliver Daumke
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11

  • Dysferlin-deficient muscular dystrophy is a devastating and untreatable disease. Using Cas9, the authors restored dysferlin in muscle stem cells from patients ex vivo and show proof-of-concept for autologous cell replacement therapies in a new humanized mouse model.

    • Helena Escobar
    • Silvia Di Francescantonio
    • Simone Spuler
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-17

  • The AAA+ ATPase p97 is an essential hexameric protein with multiple protein interaction partners and cellular functions. Here, the authors use interaction mapping to examine partner proteins of this large complex, and assess the effects of these proteins on the disassembly of the p97 complex.

    • Anup Arumughan
    • Yvette Roske
    • Erich E. Wanker
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-13

  • Protein kinase A (PKA) is a key mediator of cyclic AMP signalling. Here, Eccles et al. show that ARHGAP36 antagonizes PKA by acting as a kinase inhibitor and targeting the catalytic subunit for endolysosomal degradation, thus reducing sensitivity of cells to cAMP and promoting Hedgehog signalling.

    • Rebecca L. Eccles
    • Maciej T. Czajkowski
    • Oliver Rocks
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-16

  • Lenardo and colleagues identify a new human genetic disease, GISELL, whereby ceramide lipid homeostasis is disrupted, thereby altering T cell longevity. Deficiency of GTPase of the immunity-associated protein 5 (GIMAP5) in patients leads to cellular senescence, immunodeficiency and early mortality.

    • Ann Y. Park
    • Michael Leney-Greene
    • Michael J. Lenardo
    Research
    Nature Immunology
    Volume: 25, P: 282-293

  • Here the authors characterise the impact of phosphorylation site mutations in intrinsically disordered regions (IDRs) on protein-protein interactions, highlighting the critical role of phosphorylation of IDRs in health and disease.

    • Trendelina Rrustemi
    • Katrina Meyer
    • Matthias Selbach
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-19

  • The inner mitochondrial membrane forms cristae, which are crucial for mitochondrial function. This Review explores the protein complexes that regulate cristae dynamics, including remodelling and fusion, and discusses recent structural insights that have increased our understanding of mitochondrial architecture.

    • Oliver Daumke
    • Martin van der Laan
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 26, P: 706-724

  • Cancer is often associated with mutant transcription factors (TFs) but their functional characterization is challenging. Here, the authors describe a recurrent mutation within TF IRF4 in human lymphomas and they show how it causes a complex switch in TF specificity and functionality.

    • Nikolai Schleussner
    • Pierre Cauchy
    • Stephan Mathas
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-18

  • Compound library screening combined with medicinal chemistry and structural biology approaches enables the development of potent and highly selective cell-permeable small-molecule inhibitors of phosphatidylinositol 3-kinase C2α activity and function.

    • Wen-Ting Lo
    • Hassane Belabed
    • Volker Haucke
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 19, P: 18-27

  • Crystal and electron cryo-tomography structures of Mgm1 from Chaetomium thermophilum reveal that Mgm1 forms bent tetramers, which further assemble into helical filaments on both positively and negatively curved membranes.

    • Katja Faelber
    • Lea Dietrich
    • Oliver Daumke
    Research
    Nature
    Volume: 571, P: 429-433

  • High-resolution structures of phosphatidylinositol 3-kinase (PI3K) type IIa unravel a coincident mechanism of lipid-induced enzyme activation and enable the development of inhibitors of class II PI3K function with applications in biomedicine.

    • Wen-Ting Lo
    • Yingyi Zhang
    • Volker Haucke
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 218-228

  • The crystal structure of the large GTPase dynamin tetramer is presented, suggesting a mechanism by which oligomerization of dynamin is regulated, and revealing how mutations that interfere with tetramer formation and autoinhibition are of relevance to understanding the congenital muscle disorders Charcot–Marie–Tooth neuropathy and centronuclear myopathy.

    • Thomas F. Reubold
    • Katja Faelber
    • Susanne Eschenburg
    Research
    Nature
    Volume: 525, P: 404-408

  • Dynamin is a protein that catalyses the scission of clathrin-coated pits at the plasma membrane. The mechanisms of dynamin-catalysed scission remain poorly understood. Here, the structure of the stalk region of human MxA, a dynamin-like protein, is presented. A structural model of MxA oligomerization and stimulated GTP hydrolysis is put forward that has functional implications for all members of the dynamin family.

    • Song Gao
    • Alexander von der Malsburg
    • Oliver Daumke
    Research
    Nature
    Volume: 465, P: 502-506