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• W2000678720 endingPage "86" @default.
• W2000678720 startingPage "69" @default.
• W2000678720 abstract "Lysosomes, the terminal organelles on the endocytic pathway, digest macromolecules and make their components available to the cell as nutrients. Hydrolytic enzymes specific to a wide range of targets reside within the lysosome; these enzymes are activated by the highly acidic pH (between 4.5 and 5.0) in the organelles' interior. Lysosomes generate and maintain their pH gradients by using the activity of a proton-pumping V-type ATPase, which uses metabolic energy in the form of ATP to pump protons into the lysosome lumen. Because this activity separates electric charge and generates a transmembrane voltage, another ion must move to dissipate this voltage for net pumping to occur. This so-called counterion may be either a cation (moving out of the lysosome) or an anion (moving into the lysosome). Recent data support the involvement of ClC-7, a Cl − /H + antiporter, in this process, although many open questions remain as to this transporter's involvement. Although functional results also point to a cation transporter, its molecular identity remains uncertain. Both the V-ATPase and the counterion transporter are likely to be important players in the mechanisms determining the steady-state pH of the lysosome interior. Exciting new results suggest that lysosomal pH may be dynamically regulated in some cell types." @default.
• W2000678720 created "2016-06-24" @default.
• W2000678720 creator A5076523049 @default.
• W2000678720 date "2012-03-17" @default.
• W2000678720 modified "2023-10-17" @default.
• W2000678720 title "Lysosomal Acidification Mechanisms" @default.
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• W2000678720 doi "https://doi.org/10.1146/annurev-physiol-012110-142317" @default.

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