Journal: Biochemical Society transactions

Loading...

Abbreviation

Biochem Soc Trans

Publisher

Portland Press

Journal Volumes

ISSN

0300-5127
1470-8752

Description

Search Results

Publications 1 - 10 of 21
  • Hiebert, Paul; Werner, Sabine (2023)
    Biochemical Society transactions
    The transcription factor NRF2 is well known as a master regulator of the cellular stress response. As such, activation of NRF2 has gained widespread attention for its potential to prevent tissue injury, but also as a possible therapeutic approach to promote repair processes. While NRF2 activation affects most or even all cell types, its effect on epithelial cells during repair processes has been particularly well studied. In response to tissue injury, these cells proliferate, migrate and/or spread to effectively repair the damage. In this review, we discuss how NRF2 governs repair of epithelial tissues, and we highlight the increasing number of NRF2 targets with diverse roles in regulating epithelial repair.
  • Akt/mTOR signalling in myelination
    Item type: Journal Article
    Norrmén, Camilla; Suter, Ueli (2013)
    Biochemical Society transactions
  • Deupi, Xavier; Standfuss, Jörg; Schertler, Gebhard (2012)
    Biochemical Society transactions
  • Niu, Xize; deMello, Andrew J. (2012)
    Biochemical Society transactions
  • Evolving protocells to prototissues
    Item type: Journal Article
    Mantri, S.; Sapra, K. T. (2013)
    Biochemical Society transactions
  • Richmond, Timothy J. (2012)
    Biochemical Society transactions
  • Mavridou, Despoina A. L.; Braun, Martin; Thoeny-Meyer, Linda; et al. (2008)
    Biochemical Society transactions
  • Neumann, D.; Schlattner, U.; Wallimann, T. (2003)
    Biochemical Society transactions
  • Loi, Marisa; Fregno, Ilaria; Guerra, Concetta; et al. (2018)
    Biochemical Society transactions
    The endoplasmic reticulum (ER) is the site of protein, lipid, phospholipid, steroid and oligosaccharide synthesis and modification, calcium ion storage, and detoxification of endogenous and exogenous products. Its volume (and activity) must be maintained under normal growth conditions, must be expanded in a controlled manner on activation of ER stress programs and must be reduced to pre-stress size during the recovery phase that follows ER stress termination. ER-phagy is the constitutive or regulated fragmentation and delivery of ER fragments to lysosomal compartments for clearance. It gives essential contribution to the maintenance of cellular homeostasis, proteostasis, lipidostasis and oligosaccharidostasis (i.e. the capacity to produce the proteome, lipidome and oligosaccharidome in appropriate quality and quantity). ER turnover is activated on ER stress, nutrient deprivation, accumulation of misfolded polypeptides, pathogen attack and by activators of macroautophagy. The selectivity of these poorly characterized catabolic pathways is ensured by proteins displayed at the limiting membrane of the ER subdomain to be removed from cells. These proteins are defined as ER-phagy receptors and engage the cytosolic macroautophagy machinery via specific modules that associate with ubiquitin-like, cytosolic proteins of the Atg8/LC3/GABARAP family. In this review, we give an overview on selective ER turnover and on the yeast and mammalian ER-phagy receptors identified so far.
  • Martoglio, B. (2003)
    Biochemical Society transactions
Publications 1 - 10 of 21