Open Close
Reference
Citation
Şentürk, M., Mao, D., Bellen, H.J. (2019). Loss of proteins associated with amyotrophic lateral sclerosis affects lysosomal acidification via different routes.  Autophagy 15(8): 1467--1469.
FlyBase ID
FBrf0242755
Publication Type
Note
Abstract

Abnormal accumulation of proteins is a hallmark of a variety of neurological diseases including amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Maintenance of protein homeostasis (proteostasis) in neurons via proteasomal and macroautophagy/autophagy-lysosomal degradation is thought to be central for proper neuronal function and survival. We recently reported evolutionarily conserved roles for two ALS-linked proteins, UBQLN2 (ubiquilin 2) and VAPB, in regulation of lysosomal degradation. Ubiquilins are required for v-ATPase-mediated lysosomal acidification, whereas VAPs are required for the PtdIns4P-mediated endo-lysosomal trafficking pathway.

PubMed ID
PubMed Central ID
PMC6613899 (PMC) (EuropePMC)
Related Publication(s)
Research paper

Ubiquilins regulate autophagic flux through mTOR signalling and lysosomal acidification.
Şentürk et al., 2019, Nat. Cell Biol. 21(3): 384--396 [FBrf0241650]

VAMP associated proteins are required for autophagic and lysosomal degradation by promoting a PtdIns4P-mediated endosomal pathway.
Mao et al., 2019, Autophagy 15(7): 1214--1233 [FBrf0242566]

Associated Information
Comments
Associated Files
Other Information
Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Autophagy
    Title
    Autophagy
    Publication Year
    2005-
    ISBN/ISSN
    1554-8627 1554-8635
    Data From Reference