Browsing by Author "Lamark, Trond"

Now showing items 21-27 of 27

    • The Selective Autophagy Receptor p62 Forms a Flexible Filamentous Helical Scaffold 

      Ciuffa, Rodolfo; Lamark, Trond; Tarafder, Abul K.; Guesdon, Audrey; Rybina, Sofia; Hagen, Wim J.H.; Johansen, Terje; Sachse, Carsten (Journal article; Tidsskriftartikkel; Peer reviewed, 2015-05-05)
      The scaffold protein p62/SQSTM1 is involved in protein turnover and signaling and is commonly found in dense protein bodies in eukaryotic cells. In autophagy, p62 acts as a selective autophagy receptor that recognizes and shuttles ubiquitinated proteins to the autophagosome for degradation. The structural organization of p62 in cellular bodies and the interplay of these assemblies with ubiquitin ...

    • Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors 

      Johansen, Terje; Lamark, Trond (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-07-13)
      Selective autophagy relies on soluble or membrane-bound cargo receptors that recognize cargo and bring about autophagosome formation at the cargo. The cargo-bound receptors interact with lipidated ATG8 family proteins anchored in the membrane at the concave side of the forming autophagosome. The interaction is mediated by 15- to 20-amino-acid-long sequence motifs called LC3-interacting region (LIR) ...

    • The soluble reticulophagy receptor CALCOCO1 is also a Golgiphagy receptor. 

      Nthiga, Thaddaeus Mutugi; Shrestha, Birendra Kumar; Lamark, Trond; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-06-24)
      Cellular stress response mechanisms typically increase organellar quantity and volume. To restore cellular homeostasis and organellar integrity, the surplus organelles are cleared by macroautophagy/autophagy, an intracellular process that shuttles cytoplasmic material to the lysosomes for degradation. The degradation is mediated by autophagy receptors that selectively link the degradable cargo to ...

    • Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake 

      Jakobi, Arjen J.; Huber, Stefan T.; Mortensen, Simon A.; Schultz, Sebastian; Palara, Anthimi; Kuhm, Tanja; Shrestha, Birendra Kumar; Lamark, Trond; Hagen, Wim J.H.; Wilmanns, Matthias; Johansen, Terje; Brech, Andreas; Sachse, Carsten (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-01-23)
      p62/SQSTM1 is an autophagy receptor and signaling adaptor with an N-terminal PB1 domain that forms the scaffold of phase-separated p62 bodies in the cell. The molecular determinants that govern PB1 domain filament formation in vitro remain to be determined and the role of p62 filaments inside the cell is currently unclear. We here determine four high-resolution cryo-EM structures of different human ...

    • 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 ...

    • TRIM27 is an autophagy substrate facilitating mitochondria clustering and mitophagy via phosphorylated TBK1 

      Garcia, Juncal Garcia; Berge, Anne Kristin McLaren; Overå, Katrine Stange; Larsen, Kenneth Bowitz; Bhujabal, Zambarlal Babanrao; Brech, Andreas; Abudu, Yakubu Princely; Lamark, Trond; Johansen, Terje; Sjøttem, Eva (Journal article; Tidsskriftartikkel; Peer reviewed, 2022-09-16)
      Tripartite motif-containing protein 27 (TRIM27/also called RFP) is a multifunctional ubiquitin E3 ligase involved in numerous cellular functions, such as proliferation, apoptosis, regulation of the NF-kB pathway, endosomal recycling and the innate immune response. TRIM27 interacts directly with TANK-binding kinase 1 (TBK1) and regulates its stability. TBK1 in complex with autophagy receptors is ...

    • TRIM32, but not its muscular dystrophy-associated mutant, positively regulates and is targeted to autophagic degradation by p62/SQSTM1 

      Overå, Katrine Stange; Garcia-Garcia, Juncal; Bhujabal, Zambarlal; Jain, Ashish; Larsen, Kenneth Bowitz; Deretic, Vojo; Johansen, Terje; Lamark, Trond; Sjøttem, Eva (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-12-02)
      The tripartite motif (TRIM) proteins constitute a family of ubiquitin E3 ligases involved in a multitude of cellular processes, including protein homeostasis and autophagy. TRIM32 is characterized by six protein–protein interaction domains termed NHL, various point mutations in which are associated with limb-girdle-muscular dystrophy 2H (LGMD2H). Here, we show that TRIM32 is an autophagy substrate. ...