Blar i forfatter "Overå, Katrine Stange"

Viser treff 1-3 av 3

    • Generation of the short TRIM32 isoform is regulated by Lys 247 acetylation and a PEST sequence 

      Garcia-Garcia, Juncal; Overå, Katrine Stange; Khan, Waqas; Sjøttem, Eva (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-05-17)
      TRIM32 is an E3 ligase implicated in diverse biological pathways and pathologies such as muscular dystrophy and cancer. TRIM32 are expressed both as full-length proteins, and as a truncated protein. The mechanisms for regulating these isoforms are poorly understood. Here we identify a PEST sequence in TRIM32 located in the unstructured region between the RING-BBox-CoiledCoil domains and the NHL ...

    • 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. ...