• AlphaFold-multimer predicts ATG8 protein binding motifs crucial for autophagy research 

      Olsvik, Hallvard Lauritz; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-02-08)
      Proteins are structural and executing macromolecules essential for life in all biological systems. Insight into proteins structures is required for detailed mechanistic understanding of how they work and solve different tasks. The ability to predict three-dimensional (3D) protein structures from primary sequence information has therefore been an open research question for more than 50 years. The ...
    • ATG8 Family Proteins Act as Scaffolds for Assembly of the ULK Complex SEQUENCE REQUIREMENTS FOR LC3-INTERACTING REGION (LIR) MOTIFS 

      Alemu, Endalkachew Ashenafi; Lamark, Trond; Torgersen, Knut Martin; Birgisdottir, Åsa birna; Larsen, Kenneth Bowitz; Jain, Ashish; Olsvik, Hallvard Lauritz; Øvervatn, Aud Karin; Kirkin, Vladimir; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2012-10-05)
      Autophagy is a lysosome-dependent degradation system conserved among eukaryotes. The mammalian Atg1 homologues, Unc-51 like kinase (ULK) 1 and 2, are multifunctional proteins with roles in autophagy, neurite outgrowth, and vesicle transport. The mammalian ULK complex involved in autophagy consists of ULK1, ULK2, ATG13, FIP200, and ATG101. We have used pulldown and peptide array overlay assays to ...
    • FYCO1 contains a C-terminally extended, LC3A/B-preferring LC3-interacting region (LIR) motif required for efficient maturation of autophagosomes during basal autophagy 

      Olsvik, Hallvard Lauritz; Lamark, Trond; Takagi, Kenji; Larsen, Kenneth Bowitz; Evjen, gry; Øvervatn, Aud Karin; Mizushima, Tsunehiro; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2015-10-14)
      FYCO1 (FYVE and coiled-coil protein 1) is a transport adaptor that binds to phosphatidylinositol 3-phosphate, to Rab7, and to LC3 (microtubule-associated protein 1 light chain 3) to mediate transport of late endosomes and autophagosomes along microtubules in the plus end direction. We have previously shown that FYCO1 binds to LC3B via a 19-amino acid sequence containing a putative core LC3-interacting ...
    • The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy following TBK1 phosphorylation of its LIR 

      Rasmussen, Nikoline Lander; Zhou, Jianwen; Olsvik, Hallvard Lauritz; Kaeser-Pebernard, Stéphanie; Lamark, Trond; Dengjel, Joern; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-03-09)
      The inflammatory repressor TNIP1/ABIN-1 is important for keeping in check inflammatory and cell-death pathways to avoid potentially dangerous sustained activation of these pathways. We have now found that TNIP1 is rapidly degraded by selective macroautophagy/autophagy early (0–4 h) after activation of TLR3 by poly(I:C)-treatment to allow expression of pro-inflammatory genes and proteins. A few hours ...
    • Phosphorylation of the LIR Domain of SCOC Modulates ATG8 Binding Affinity and Specificity 

      Wirth, Martina; Mouilleron, Stephane; Zhang, Wenxin; Abudu, Yakubu Princely; Jain, Ashish; Olsvik, Hallvard Lauritz; Bruun, Jack-Ansgar; Razi, Minoo; Jefferies, Harold B.J.; Lee, Rebecca; Joshi, Dhira; O'Reilly, Nicola; Johansen, Terje; Tooze, Sharon A (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-04-24)
      <p>Autophagy is a highly conserved degradative pathway, essential for cellular homeostasis and implicated in diseases including cancer and neurodegeneration. Autophagy-related 8 (ATG8) proteins play a central role in autophagosome formation and selective delivery of cytoplasmic cargo to lysosomes by recruiting autophagy adaptors and receptors. The LC3-interacting region (LIR) docking site (LDS) of ...
    • Starvation induces rapid degradation of selective autophagy receptors by endosomal microautophagy 

      Mejlvang, Jakob; Olsvik, Hallvard Lauritz; Svenning, Steingrim; Bruun, Jack-Ansgar; Abudu, Yakubu Princely; Larsen, Kenneth Bowitz; Brech, Andreas; Hansen, Tom Egil; Brenne, Hanne Britt; Hansen, Terkel; Stenmark, Harald Alfred; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2018-07-17)
      It is not clear to what extent starvation-induced autophagy affects the proteome on a global scale and whether it is selective. In this study, we report based on quantitative proteomics that cells during the first 4 h of acute starvation elicit lysosomal degradation of up to 2–3% of the proteome. The most significant changes are caused by an immediate autophagic response elicited by shortage of amino ...
    • TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1 

      Zhou, Jianwen; Rasmussen, Nikoline Lander; Olsvik, Hallvard Lauritz; Akimov, Vyacheslav; Hu, Zehan; Evjen, Gry; Kaeser-Pebernard, Stéphanie; Sankar, Devanarayanan Siva; Roubaty, Carole; Verlhac, Pauline; van de Beck, Nicole; Reggiori, Fulvio; Abudu, Yakubu Princely; Blagoev, Blagoy; Lamark, Trond; Johansen, Terje; Dengjel, Jörn (Journal article; Tidsskriftartikkel, 2022-12-27)
      Limitation of excessive inflammation due to selective degradation of pro-inflammatory proteins is one of the cytoprotective functions attributed to autophagy. In the current study, we highlight that selective autophagy also plays a vital role in promoting the establishment of a robust inflammatory response. Under inflammatory conditions, here TLR3-activation by poly(I:C) treatment, the inflammation ...
    • The ubiquitin E3 ligase TRIM27 emerges as a new player in mitophagy 

      Berge, Anne Kristin McLaren; Garcia, Juncal Garcia; Sjøttem, Eva; Olsvik, Hallvard Lauritz (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-01-05)
      Mitochondria are the center for energy production, cell fate determination and synthesis of essential biomolecules in cells. Hence, mitochondrial quality control mechanisms are essential for cellular health. Failure of these control mechanisms may lead to damaged mitochondria that represent a threat to cell survival. Mitophagy is a selective autophagy process that removes damaged mitochondria ...