1. Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors.: trafficking motif of P2X ATP-gated channels
- Author
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R. Alan North, François Rassendren, Lin-Hua Jiang, Severine Chaumont, Aubin Penna, Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Institute of Molecular Physiology, and University of Sheffield [Sheffield]
- Subjects
MESH: Sequence Homology, Amino Acid ,MESH: Neurons ,MESH: Amino Acid Sequence ,Endoplasmic Reticulum ,Biochemistry ,MESH: Protein Structure, Tertiary ,0302 clinical medicine ,Adenosine Triphosphate ,Chlorocebus aethiops ,MESH: Adenosine Triphosphate ,MESH: Animals ,Receptor ,Internalization ,media_common ,Neurons ,0303 health sciences ,Cell Polarity ,ion channels ,MESH: Protein Subunits ,Cell biology ,Transport protein ,stabilization ,Protein Transport ,MESH: Cell Polarity ,Intracellular ,Ionotropic effect ,MESH: Protein Transport ,MESH: Rats ,Protein subunit ,media_common.quotation_subject ,Recombinant Fusion Proteins ,Molecular Sequence Data ,MESH: Sequence Alignment ,[SDV.BC]Life Sciences [q-bio]/Cellular Biology ,Biology ,Cell Line ,surface expression ,03 medical and health sciences ,MESH: Endoplasmic Reticulum ,Extracellular ,MESH: Recombinant Fusion Proteins ,Animals ,Humans ,MESH: Receptors, Purinergic P2 ,Amino Acid Sequence ,Molecular Biology ,030304 developmental biology ,polarization ,MESH: Humans ,MESH: Molecular Sequence Data ,Sequence Homology, Amino Acid ,Receptors, Purinergic P2 ,P2X receptors ,Cell Biology ,MESH: Cercopithecus aethiops ,Protein Structure, Tertiary ,Rats ,MESH: Cell Line ,Protein Subunits ,Membrane protein ,Sequence Alignment ,030217 neurology & neurosurgery ,Receptors, Purinergic P2X2 - Abstract
International audience; Extracellular ATP-gated channels (P2X receptors) define the third major family of ionotropic receptors, and they are expressed widely in nerve cells, muscles, and endocrine and exocrine glands. P2X subunits have two membrane-spanning domains, and a receptor is thought to be formed by oligomerization of three subunits. We have identified a conserved motif in the cytoplasmic C termini of P2X subunits that is necessary for their surface expression; mutations in this motif result in a marked reduction of the receptors at the plasma membrane because of a rapid internalization. Transfer of the motif to a reporter protein (CD(4)) enhances the surface expression of the chimera, indicating that this motif is likely involved in the stabilization of P2X receptor at the cell surface. In neurons, mutated P2X(2) subunits showed reduced membrane expression and an altered axodendritic distribution. This motif is also present in intracellular regions of other membrane proteins, such as in the third intracellular loop of some G protein-coupled receptors, suggesting that it might be involve in their cellular stabilization and polarization.
- Published
- 2004
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