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  • 1.
    Grebe, Markus
    Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Out of the shade and into the light2011In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 13, no 4, p. 347-349Article in journal (Refereed)
    Abstract [en]

    Plants reach for the sun by avoiding the shade and by directly growing towards the light. Two studies now suggest that the polar relocation of PIN3, a transporter directing the flow of the plant hormone auxin, drives both growth processes. PIN3 repolarization occurs downstream of shade perception through phytochrome photoreceptors, whereas blue light perceived by phototropin initiates polar recycling of PIN3 and growth towards the light.

  • 2.
    Ikeda, Yoshihisa
    et al.
    Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Men, Shuzhen
    Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Fischer, Urs
    Stepanova, Anna N
    Alonso, José M
    Ljung, Karin
    Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Grebe, Markus
    Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
    Local auxin biosynthesis modulates gradient-directed planar polarity in Arabidopsis2009In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 11, no 6, p. 731-738Article in journal (Refereed)
    Abstract [en]

    The coordination of cell polarity within the plane of a single tissue layer (planar polarity) is a crucial task during development of multicellular organisms. Mechanisms underlying establishment of planar polarity, however, differ substantially between plants and animals. In Arabidopsis thaliana, planar polarity of root-hair positioning along epidermal cells is coordinated towards maximum concentration of an auxin gradient in the root tip. This gradient has been hypothesized to be sink-driven and computational modelling suggests that auxin efflux carrier activity may be sufficient to generate the gradient in the absence of auxin biosynthesis in the root. Here, we demonstrate that the Raf-like kinase CONSTITUTIVE TRIPLE RESPONSE1 (CTR1; Refs 8, 9) acts as a concentration-dependent repressor of a biosynthesis-dependent auxin gradient that modulates planar polarity in the root tip. We analysed auxin biosynthesis and concentration gradients in a variety of root-hair-position mutants affected in CTR1 activity, auxin biosynthesis and transport. Our results reveal that planar polarity relies on influx- and efflux-carrier-mediated auxin redistribution from a local biosynthesis maximum. Thus, a local source of auxin biosynthesis contributes to gradient homeostasis during long-range coordination of cellular morphogenesis.

  • 3. Lystad, Aif Hakon
    et al.
    Carlsson, Sven R
    Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
    de la Ballina, Laura R.
    Kauffman, Karlina J.
    Nag, Shanta
    Yoshimori, Tamotsu
    Melia, Thomas J.
    Simonsen, Anne
    Distinct functions of ATG16L1 isoforms in membrane binding and LC3B lipidation in autophagy-related processes2019In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 21, no 3, p. 372-383Article in journal (Refereed)
    Abstract [en]

    Covalent modification of LC3 and GABARAP proteins to phosphatidylethanolamine in the double-membrane phagophore is a key event in the early phase of macroautophagy, but can also occur on single-membrane structures. In both cases this involves transfer of LC3/GABARAP from ATG3 to phosphatidylethanolamine at the target membrane. Here we have purified the full-length human ATG12-5-ATG16L1 complex and show its essential role in LC3B/GABARAP lipidation in vitro. We have identified two functionally distinct membrane-binding regions in ATG16L1. An N-terminal membrane-binding amphipathic helix is required for LC3B lipidation under all conditions tested. By contrast, the C-terminal membrane-binding region is dispensable for canonical autophagy but essential for VPS34-independent LC3B lipidation at perturbed endosomes. We further show that the ATG16L1 C-terminus can compensate for WIPI2 depletion to sustain lipidation during starvation. This C-terminal membrane-binding region is present only in the beta-isoform of ATG16L1, showing that ATG16L1 isoforms mechanistically distinguish between different LC3B lipidation mechanisms under different cellular conditions.

  • 4.
    Rietdorf, Jens
    et al.
    European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
    Ploubidou, Aspasia
    European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
    Reckmann, Inge
    European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany .
    Holmström, Anna
    European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
    Frischknecht, Friedrich
    European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
    Zettl, Markus
    European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
    Zimmermann, Timo
    European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
    Way, Michael
    Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.
    Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus2001In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 3, no 11, p. 992-1000Article in journal (Refereed)
    Abstract [en]

    Vaccinia virus, a close relative of the causative agent of smallpox, exploits actin polymerization to enhance its cell-to-cell spread. We show that actin-based motility of vaccinia is initiated only at the plasma membrane and remains associated with it. There must therefore be another form of cytoplasmic viral transport, from the cell centre, where the virus replicates, to the periphery. Video analysis reveals that GFP-labelled intracellular enveloped virus particles (IEVs) move from their perinuclear site of assembly to the plasma membrane on microtubules. We show that the viral membrane protein A36R, which is essential for actin-based motility of vaccinia, is also involved in microtubule-mediated movement of IEVs. We further show that conventional kinesin is recruited to IEVs via the light chain TPR repeats and is required for microtubule-based motility of the virus. Vaccinia thus sequentially exploits the microtubule and actin cytoskeletons to enhance its cell-to-cell spread.

  • 5.
    Sorrentino, Alessandro
    et al.
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    Thakur, Noopur
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    Grimsby, Susanne
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    Marcusson, Anders
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    von Bulow, Verena
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    Schuster, Norbert
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    Zhang, Shouting
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    Heldin, Carl-Henrik
    1.Ludwig Institute for Cancer Research, Rudbeck Laboratory, Uppsala University, Sweden.
    Landström, Maréne
    Umeå University, Faculty of Medicine, Department of Medical Biosciences, Pathology.
    The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner2008In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 10, no 10, p. 1199-1207Article in journal (Refereed)
    Abstract [en]

    Transforming growth factor-beta (TGF-beta) is a multifunctional cytokine that regulates embryonic development and tissue homeostasis; however, aberrations of its activity occur in cancer. TGF-beta signals through its Type II and Type I receptors (TbetaRII and TbetaRI) causing phosphorylation of Smad proteins. TGF-beta-associated kinase 1 (TAK1), a member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family, was originally identified as an effector of TGF-beta-induced p38 activation. However, the molecular mechanisms for its activation are unknown. Here we report that the ubiquitin ligase (E3) TRAF6 interacts with a consensus motif present in TbetaRI. The TbetaRI-TRAF6 interaction is required for TGF-beta-induced autoubiquitylation of TRAF6 and subsequent activation of the TAK1-p38/JNK pathway, which leads to apoptosis. TbetaRI kinase activity is required for activation of the canonical Smad pathway, whereas E3 activity of TRAF6 regulates the activation of TAK1 in a receptor kinase-independent manner. Intriguingly, TGF-beta-induced TRAF6-mediated Lys 63-linked polyubiquitylation of TAK1 Lys 34 correlates with TAK1 activation. Our data show that TGF-beta specifically activates TAK1 through interaction of TbetaRI with TRAF6, whereas activation of Smad2 is not dependent on TRAF6.

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