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Autophagy. 2019 Aug;15(8):1467-1469. doi: 10.1080/15548627.2019.1609863. Epub 2019 Apr 28.

Loss of proteins associated with amyotrophic lateral sclerosis affects lysosomal acidification via different routes.

Şentürk M1,2,3, Mao D2,4,5, Bellen HJ2,3,5,6,7.

Author information

1
a Huffington Center on Aging , Baylor College of Medicine , Houston , TX , USA.
2
b Program in Developmental Biology , Baylor College of Medicine (BCM) , Houston , TX , USA.
3
c Howard Hughes Medical Institute , BCM , Houston , TX , USA.
4
d Department of Pediatrics , BCM , Houston , TX , USA.
5
e Department of Molecular and Human Genetics , BCM , Houston , TX , USA.
6
f Department of Neuroscience , BCM , Houston , TX , USA.
7
g Jan and Dan Duncan Neurological Research Institute , Texas Children's Hospital , Houston , TX , USA.

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.

KEYWORDS:

ALS; Drosophila; ER stress; MTOR; lysosomal acidification; v-ATPase

PMID:
31032688
PMCID:
PMC6613899
[Available on 2020-04-28]
DOI:
10.1080/15548627.2019.1609863

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