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P2X4 and lysosome fusion

journal contribution
posted on 2023-06-09, 17:28 authored by Ruth Murrell-LagnadoRuth Murrell-Lagnado, Manfred Frick
Similar to other members of the P2X receptor family, the P2X4 receptor at the plasma membrane forms a highly Ca2+ permeable, non-selective cation channel that is activated by extracellular ATP. Yet, P2X4 differs from the other subtypes, as it is predominantly localized on late endosomal, lysosomal and/or lysosome-related organelles. It is targeted there by virtue of tyrosine-based and di-leucine like trafficking motifs contained within its C-terminal and N-terminal regions respectively. The physiological role of the stable intracellular expression of P2X4 in acidic compartments has been a long-standing puzzle. Recent evidence, however, points to a dual role in the regulation of ion fluxes across lysosomal membranes to control lysosome membrane fusion and in the re-sensitization of receptors exposed to extracellular ATP.

History

Publication status

  • Published

Journal

Current Opinion in Pharmacology

ISSN

1471-4892

Publisher

Elsevier

Volume

47

Page range

126-132

Department affiliated with

  • Neuroscience Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2019-04-03

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