The position of lysosomes within the cell determines their luminal pH
Open accessAbstract
We examined the luminal pH of individual lysosomes using quantitative ratiometric fluorescence microscopy and report an unappreciated heterogeneity: peripheral lysosomes are less acidic than juxtanuclear ones despite their comparable buffering capacity. An increased passive (leak) permeability to protons, together with reduced vacuolar H(+)-adenosine triphosphatase (V-ATPase) activity, accounts for the reduced acidifying ability of peripheral lysosomes. The altered composition of peripheral lysosomes is due, at least in part, to more limited access to material exported by the biosynthetic pathway. The balance between Rab7 and Arl8b determines the subcellular localization of lysosomes; more peripheral lysosomes have reduced Rab7 density. This in turn results in decreased recruitment of Rab-interacting lysosomal protein (RILP), an effector that regulates the recruitment and stability of the V1G1 component of the lysosomal V-ATPase. Deliberate margination of lysosomes is associated with reduced acidification and impaired proteolytic activity. The heterogeneity in lysosomal pH may be an indication of a broader functional versatility.
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The CCCP effect on lysosomal pH is concentration- and time-dependent.
“The CCCP effect on lysosomal pH seems to be concentration- and time-dependent.”
From Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases (2019) · cites this paper as [84]
In HeLa cells, the position of lysosomes within the cell determines their luminal pH; peripheral lysosomes are less acidic than perinuclear lysosomes because they have less RAB7, leading to decreased recruitment of RILP and v-ATPase subunits.
“Studies in HeLa cells show that the position of lysosomes within the cell determines their luminal pH; peripheral lysosomes are less acidic than those in the perinuclear region. This is because peripheral lysosomes have less RAB7, which leads to decreased recruitment of the RAB7 effector RILP (RAB-interacting lysosomal protein). RILP, in turn, is responsible for recruiting specific subunits of the”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Johnson et al., 2016
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- Authors
- Johnson, D. E., Ostrowski, P., Jaumouillé, V., & Grinstein, S.
- Affiliations
- Hospital for Sick Children (CA)
- Corresponding author
- Grinstein, Sergio
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2016-03-14
- Volume
- 212
- Issue
- 6
- Pages
- 677-692
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC4792074
- OpenAlex
- W2322556561
- Cited by
- 590
- References
- 73
- Citations by year
- 2026: 49 · 2025: 60 · 2024: 57 · 2023: 64 · 2022: 71 · 2021: 61 · 2020: 66 · 2019: 52 · 2018: 49 · 2017: 38 · 2016: 23
- FWCI
- 37.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Hospital for Sick Children
- Canadian Institutes of Health Research (FDN-143202)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- lysosomal pH, lysosomal acidification, V-ATPase, Rab7, Arl8b, RILP, lysosomal proteolysis
- MeSH terms
- rab7 GTP-Binding Proteins, HeLa Cells, Humans, Hydrogen-Ion Concentration, Lysosomes, Vacuoles, rab GTP-Binding Proteins, ADP-Ribosylation Factors, Vacuolar Proton-Translocating ATPases, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, Biosynthetic Pathways
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