P2X4 and lysosome fusion

Murrell-Lagnado, Ruth D and Frick, Manfred (2019) P2X4 and lysosome fusion. Current Opinion in Pharmacology, 47. pp. 126-132. ISSN 1471-4892

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Abstract

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.

Item Type: Article
Keywords: P2X4 purinergic receptors lysosomes fusion calcium signalling
Schools and Departments: School of Life Sciences > Neuroscience
Subjects: Q Science
Q Science > QP Physiology
Q Science > QP Physiology > QP0351 Neurophysiology and neuropsychology
R Medicine
R Medicine > RM Therapeutics. Pharmacology
Depositing User: Ruth Murrell-Lagnado
Date Deposited: 03 Apr 2019 13:42
Last Modified: 03 Jun 2019 16:01
URI: http://sro.sussex.ac.uk/id/eprint/82970
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