P2X7 Interactions and Signaling – Making Head or Tail of It
Extracellular adenine nucleotides play important roles in cell–cell communication and tissue homeostasis. High concentrations of extracellular ATP released by dying cells are sensed as a danger signal by the P2X7 receptor, a non-specific cation channel. Studies in P2X7 knockout mice and numerous dis...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2019-08-01
|
| Series: | Frontiers in Molecular Neuroscience |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fnmol.2019.00183/full |
| _version_ | 1818032564593491968 |
|---|---|
| author | Robin Kopp Anna Krautloher Antonio Ramírez-Fernández Annette Nicke |
| author_facet | Robin Kopp Anna Krautloher Antonio Ramírez-Fernández Annette Nicke |
| author_sort | Robin Kopp |
| collection | DOAJ |
| description | Extracellular adenine nucleotides play important roles in cell–cell communication and tissue homeostasis. High concentrations of extracellular ATP released by dying cells are sensed as a danger signal by the P2X7 receptor, a non-specific cation channel. Studies in P2X7 knockout mice and numerous disease models have demonstrated an important role of this receptor in inflammatory processes. P2X7 activation has been shown to induce a variety of cellular responses that are not usually associated with ion channel function, for example changes in the plasma membrane composition and morphology, ectodomain shedding, activation of lipases, kinases, and transcription factors, as well as cytokine release and apoptosis. In contrast to all other P2X family members, the P2X7 receptor contains a long intracellular C-terminus that constitutes 40% of the whole protein and is considered essential for most of these effects. So far, over 50 different proteins have been identified to physically interact with the P2X7 receptor. However, few of these interactions have been confirmed in independent studies and for the majority of these proteins, the interaction domains and the physiological consequences of the interactions are only poorly described. Also, while the structure of the P2X7 extracellular domain has recently been resolved, information about the organization and structure of its C-terminal tail remains elusive. After shortly describing the structure and assembly of the P2X7 receptor, this review gives an update of the identified or proposed interaction domains within the P2X7 C-terminus, describes signaling pathways in which this receptor has been involved, and provides an overlook of the identified interaction partners. |
| first_indexed | 2024-12-10T06:09:23Z |
| format | Article |
| id | doaj.art-d86b62d93fd84d9f94a0a62abfe0092e |
| institution | Directory Open Access Journal |
| issn | 1662-5099 |
| language | English |
| last_indexed | 2024-12-10T06:09:23Z |
| publishDate | 2019-08-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Neuroscience |
| spelling | doaj.art-d86b62d93fd84d9f94a0a62abfe0092e2022-12-22T01:59:37ZengFrontiers Media S.A.Frontiers in Molecular Neuroscience1662-50992019-08-011210.3389/fnmol.2019.00183476017P2X7 Interactions and Signaling – Making Head or Tail of ItRobin KoppAnna KrautloherAntonio Ramírez-FernándezAnnette NickeExtracellular adenine nucleotides play important roles in cell–cell communication and tissue homeostasis. High concentrations of extracellular ATP released by dying cells are sensed as a danger signal by the P2X7 receptor, a non-specific cation channel. Studies in P2X7 knockout mice and numerous disease models have demonstrated an important role of this receptor in inflammatory processes. P2X7 activation has been shown to induce a variety of cellular responses that are not usually associated with ion channel function, for example changes in the plasma membrane composition and morphology, ectodomain shedding, activation of lipases, kinases, and transcription factors, as well as cytokine release and apoptosis. In contrast to all other P2X family members, the P2X7 receptor contains a long intracellular C-terminus that constitutes 40% of the whole protein and is considered essential for most of these effects. So far, over 50 different proteins have been identified to physically interact with the P2X7 receptor. However, few of these interactions have been confirmed in independent studies and for the majority of these proteins, the interaction domains and the physiological consequences of the interactions are only poorly described. Also, while the structure of the P2X7 extracellular domain has recently been resolved, information about the organization and structure of its C-terminal tail remains elusive. After shortly describing the structure and assembly of the P2X7 receptor, this review gives an update of the identified or proposed interaction domains within the P2X7 C-terminus, describes signaling pathways in which this receptor has been involved, and provides an overlook of the identified interaction partners.https://www.frontiersin.org/article/10.3389/fnmol.2019.00183/fullC-terminusprotein-protein interaction (PPI)signaling/signaling pathwaysP2X7 (purino) receptornetwork |
| spellingShingle | Robin Kopp Anna Krautloher Antonio Ramírez-Fernández Annette Nicke P2X7 Interactions and Signaling – Making Head or Tail of It Frontiers in Molecular Neuroscience C-terminus protein-protein interaction (PPI) signaling/signaling pathways P2X7 (purino) receptor network |
| title | P2X7 Interactions and Signaling – Making Head or Tail of It |
| title_full | P2X7 Interactions and Signaling – Making Head or Tail of It |
| title_fullStr | P2X7 Interactions and Signaling – Making Head or Tail of It |
| title_full_unstemmed | P2X7 Interactions and Signaling – Making Head or Tail of It |
| title_short | P2X7 Interactions and Signaling – Making Head or Tail of It |
| title_sort | p2x7 interactions and signaling making head or tail of it |
| topic | C-terminus protein-protein interaction (PPI) signaling/signaling pathways P2X7 (purino) receptor network |
| url | https://www.frontiersin.org/article/10.3389/fnmol.2019.00183/full |
| work_keys_str_mv | AT robinkopp p2x7interactionsandsignalingmakingheadortailofit AT annakrautloher p2x7interactionsandsignalingmakingheadortailofit AT antonioramirezfernandez p2x7interactionsandsignalingmakingheadortailofit AT annettenicke p2x7interactionsandsignalingmakingheadortailofit |