Purinergic Signalling

, Volume 7, Issue 1, pp 7–19

C terminus of the P2X7 receptor: treasure hunting

  • Helio Miranda Costa-Junior
  • Flávia Sarmento Vieira
  • Robson Coutinho-Silva
Review

DOI: 10.1007/s11302-011-9215-1

Cite this article as:
Costa-Junior, H.M., Sarmento Vieira, F. & Coutinho-Silva, R. Purinergic Signalling (2011) 7: 7. doi:10.1007/s11302-011-9215-1

Abstract

P2X receptor (P2XR) is a family of the ATP-gated ion channel family and can permeabilize the plasma membrane to small cations such as potassium, sodium, and calcium, resulting in cellular depolarization. There are seven P2XR that have been described and cloned, with 45% identity in amino acid sequence. Each P2X receptors has two transmembrane domains that are separated by an extracellular loop and an intracellular N and C terminus. Unlike the other P2X receptors, the P2X7R has a larger C terminus with an extra 200 amino acid residues compared with the other receptors. The C terminus of the P2X7R has been implicated in regulating receptor function including signaling pathway activation, cellular localization, protein–protein interactions, and post-translational modification (PTM). In the present review, we discuss the role of the P2X7R C terminus in regards to receptor function, describe the specific domains and motifs found therein and compare the C terminus sequence with others proteins to discover predicted domains or sites of PTM.

Keywords

P2X7 C terminus Intracellular signaling Motif Protein–protein interaction 

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Helio Miranda Costa-Junior
    • 1
    • 2
    • 3
  • Flávia Sarmento Vieira
    • 3
  • Robson Coutinho-Silva
    • 3
  1. 1.Instituto de Biofísica Carlos Chagas Filho-UFRJ, Av. Carlos Chagas Filho n 373, Bloco G do CCSCidade UniversitáriaRio de JaneiroBrazil
  2. 2.CryoBio - Centro de Criogenia e Terapia CelularRio de JaneiroBrazil
  3. 3.Laboratório de ImunofisiologiaUniversidade Federal do Rio de Janeiro, Instituto de Biofísica Carlos Chagas Filho, CCSRio de JaneiroBrazil

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