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A unique sorting nexin regulates trafficking of potassium channels via a PDZ domain interaction

Lunn, Marie-Louise, Nassirpour, Rounak, Arrabit, Christine, Tan, Joshua, Mcleod, Ian, Arias, Carlos M, Sawchenko, Paul E, Yates, John R, Slesinger, Paul A·2007·Nature Neuroscience
DOI 10.1038/nn1953
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Abstract

G protein-gated potassium (Kir3) channels are important for controlling neuronal excitability in the brain. Using a proteomics approach, we have identified a unique rodent intracellular protein, sorting nexin 27 (SNX27), which regulates the trafficking of Kir3 channels. Like most sorting nexins, SNX27 possesses a functional PX domain that selectively binds the membrane phospholipid phosphatidylinositol-3-phosphate (PI3P) and is important for trafficking to the early endosome. SNX27, however, is the only sorting nexin to contain a PDZ domain. This PDZ domain discriminates between channels with similar class I PDZ-binding motifs, associating with the C-terminal end of Kir3.3 and Kir3.2c (-ESKV), but not with that of Kir2.1 (-ESEI) or Kv1.4 (-ETDV). SNX27 promotes the endosomal movement of Kir3 channels, leading to reduced surface expression, increased degradation and smaller Kir3 potassium currents. The regulation of endosomal trafficking via sorting nexins reveals a previously unknown mechanism for controlling potassium channel surface expression.

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  1. Lüscher, C., Jan, L.Y., Stoffel, M., Malenka, R.C. & Nicoll, R.A. G protein–coupled inwardly rectifying K+ channels (GIRKs) mediate postsynaptic, but not presynaptic transmitter actions in hippocampal neurons. Neuron 19, 687–695 (1997). · DOI
  2. Marker, C.L., Lujan, R., Loh, H.H. & Wickman, K. Spinal G protein–gated potassium channels contribute in a dose-dependent manner to the analgesic effect of μ- and δ-, but not κ-opioids. J. Neurosci. 25, 3551–3559 (2005). · DOI
  3. Cruz, H.G. et al. Bi-directional effects of GABAB receptor agonists on the mesolimbic dopamine system. Nat. Neurosci. 7, 153–159 (2004). · DOI
  4. Kobayashi, T. et al. Ethanol opens G protein–activated inwardly rectifying K+ channels. Nat. Neurosci. 2, 1091–1097 (1999). · DOI
  5. Stanfield, P.R., Nakajima, S. & Nakajima, Y. Constitutively active and G protein–coupled inward rectifier K+ channels: Kir2.0 and Kir3.0. Rev. Physiol. Biochem. Pharmacol. 145, 47–179 (2002). · DOI
  6. Jelacic, T.M., Sims, S.M. & Clapham, D.E. Functional expression and characterization of G protein–gated inwardly rectifying K+ channels containing GIRK3. J. Membr. Biol. 169, 123–129 (1999). · DOI
  7. Inanobe, A. et al. Characterization of G protein–gated K+ channels composed of Kir3.2 subunits in dopaminergic neurons of the substantia nigra. J. Neurosci. 19, 1006–1017 (1999). · DOI
  8. Clancy, S.M. et al. Pertussis toxin–sensitive Gα subunits selectively bind to C-terminal domain of neuronal GIRK channels: evidence for a heterotrimeric G protein channel complex. Mol. Cell. Neurosci. 28, 375–389 (2005). · DOI
  9. Peleg, S., Varon, D., Ivanina, T., Dessauer, C.W. & Dascal, N.G. αi controls the gating of the G protein–activated K+ channel, GIRK. Neuron 33, 87–99 (2002). · DOI
  10. Logothetis, D.E., Kurachi, Y., Galper, J., Neer, E.J. & Clapham, D.E. The βγ subunits of GTP-binding proteins activate the muscarinic K+ channel in heart. Nature 325, 321–326 (1987). · DOI
  11. Pfaffinger, P.J., Martin, J.M., Hunter, D.D., Nathanson, N.M. & Hille, B. GTP-binding proteins couple cardiac muscarinic receptors to a K channel. Nature 317, 536–538 (1985). · DOI
  12. Reuveny, E. et al. Activation of the cloned muscarinic potassium channel by G protein βγ subunits. Nature 370, 143–146 (1994). · DOI
  13. Wickman, K.D. et al. Recombinant G protein βγ subunits activate the muscarinic-gated atrial potassium channel. Nature 368, 255–257 (1994). · DOI
  14. Wiser, O. et al. Modulation of basal and receptor-induced GIRK potassium channel activity and neuronal excitability by the mammalian PINS homolog LGN. Neuron 50, 561–573 (2006). · DOI
  15. Chuang, H.-H., Yu, M., Jan, Y.N. & Jan, L.Y. Evidence that the nucleotide exchange and hydrolysis cycle of G proteins causes acute desensitization of G protein–gated inward rectifier K+ channels. Proc. Natl. Acad. Sci. USA 95, 11727–11732 (1998). · DOI
  16. DiMagno, L., Dascal, N., Davidson, N., Lester, H.A. & Schreibmayer, W. Serotonin and protein kinase C modulation of a rat brain inwardly rectifying K+ channel expressed in Xenopus oocytes. Pflügers Arch. 431, 335–340 (1996). · DOI
  17. Kim, E. & Sheng, M. PDZ domain proteins of synapses. Nat. Rev. Neurosci. 5, 771–781 (2004). · DOI
  18. Leonoudakis, D., Conti, L.R., Radeke, C.M., McGuire, L.M. & Vandenberg, C.A. A multiprotein trafficking complex composed of SAP97, CASK, Veli and Mint1 is associated with inward rectifier Kir2 potassium channels. J. Biol. Chem. 279, 19051–19063 (2004). · DOI
  19. Leyland, M.L. & Dart, C. An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the inwardly rectifying potassium channel, Kir2.1. J. Biol. Chem. 279, 43427–43436 (2004). · DOI
  20. Nehring, R.B. et al. Neuronal inwardly rectifying K+ channels differentially couple to PDZ proteins of the PSD-95/SAP90 family. J. Neurosci. 20, 156–162 (2000). · DOI
  21. Hibino, H. et al. Anchoring proteins confer G protein sensitivity to an inward-rectifier K(+) channel through the GK domain. EMBO J. 19, 78–83 (2000). · DOI
  22. Washburn, M.P., Wolters, D. & Yates, J.R., III Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242–247 (2001). · DOI
  23. Pegan, S. et al. Kir2.1 and Kir3.1 cytoplasmic domain structures reveal sites for modulating gating and rectification. Nat. Neurosci. 8, 279–287 (2005). · DOI
  24. Leonoudakis, D. et al. Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins. J. Biol. Chem. 279, 22331–22346 (2004). · DOI
  25. Carlton, J., Bujny, M., Rutherford, A. & Cullen, P. Sorting nexins—unifying trends and new perspectives. Traffic 6, 75–82 (2005). · DOI
  26. Kajii, Y. et al. A developmentally regulated and psychostimulant-inducible novel rat gene mrt1 encoding PDZ-PX proteins isolated in the neocortex. Mol. Psychiatry 8, 434–444 (2003). · DOI
  27. Joubert, L. et al. New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4a receptor splice variant: roles in receptor targeting. J. Cell Sci. 117, 5367–5379 (2004). · DOI
  28. Hung, A.Y. & Sheng, M. PDZ domains: structural modules for protein complex assembly. J. Biol. Chem. 277, 5699–5702 (2002). · DOI
  29. Zimmermann, P. et al. PIP2-PDZ domain binding controls the association of syntenin with the plasma membrane. Mol. Cell 9, 1215–1225 (2002). · DOI
  30. Bravo, J. et al. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol. Cell 8, 829–839 (2001). · DOI
  31. Ma, D. et al. Diverse trafficking patterns due to multiple traffic motifs in G protein–activated inwardly rectifying potassium channels from brain and heart. Neuron 33, 715–729 (2002). · DOI
  32. Karschin, C., Dissmann, E., Stuhmer, W. & Karschin, A. IRK(1–3) and GIRK(1–4) inwardly rectifying K+ channel mRNAs are differentially expressed in the adult rat brain. J. Neurosci. 16, 3559–3570 (1996). · DOI
  33. Slesinger, P.A., Stoffel, M., Jan, Y.N. & Jan, L.Y. Defective γ-aminobutyric acid type B receptor–activated inwardly rectifying K+ currents in cerebellar granule cells isolated from weaver and Girk2 null mutant mice. Proc. Natl. Acad. Sci. USA 94, 12210–12217 (1997). · DOI
  34. Sun, Q.-Q., Huguenard, J.R. & Prince, D.A. Neuropeptide Y receptors differentially modulate G protein–activated inwardly rectifying K+ channels and high voltage–activated Ca2+ channels in rat thalamic neurons. J. Physiol. (Lond.) 531, 67–79 (2001). · DOI
  35. Kurten, R.C., Cadena, D.L. & Gill, G.N. Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science 272, 1008–1010 (1996). · DOI · Paper page
  36. Gullapalli, A. et al. A role for sorting nexin 2 in epidermal growth factor receptor down-regulation: evidence for distinct functions of sorting nexin 1 and 2 in protein trafficking. Mol. Biol. Cell 15, 2143–2155 (2004). · DOI
  37. Gillooly, D.J. et al. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J. 19, 4577–4588 (2000). · DOI · Paper page
  38. Horazdovsky, B.F. et al. A sorting nexin-1 homologue, Vps5p, forms a complex with Vps17p and is required for recycling the vacuolar protein-sorting receptor. Mol. Biol. Cell 8, 1529–1541 (1997). · DOI
  39. Lesage, F. et al. Molecular properties of neuronal G protein–activated inwardly rectifying K+ channels. J. Biol. Chem. 270, 28660–28667 (1995). · DOI
  40. Kobayashi, T. et al. Molecular cloning of a mouse G protein–activated K+ channel (mGIRK1) and distinct distributions of three GIRK (GIRK1, 2 and 3) mRNAs in mouse brain. Biochem. Biophys. Res. Commun. 208, 1166–1173 (1995). · DOI
  41. Long, J.F. et al. Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95. J. Mol. Biol. 327, 203–214 (2003). · DOI
  42. Doyle, D.A. et al. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85, 1067–1076 (1996). · DOI
  43. Songyang, Z. et al. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 275, 73–77 (1997). · DOI · Paper page
  44. Huang, C.S. et al. Common molecular pathways mediate long-term potentiation of synaptic excitation and slow synaptic inhibition. Cell 123, 105–118 (2005). · DOI · Paper page
  45. Hall, R.A. et al. The β2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange. Nature 392, 626–630 (1998). · DOI
  46. Brewer, G.J., Torricelli, J.R., Evege, E.K. & Price, P.J. Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567–576 (1993). · DOI · Paper page

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Authors
Lunn, M.-L., Nassirpour, R., Arrabit, C., Tan, J., Mcleod, I., Arias, C. M., Sawchenko, P. E., Yates, J. R., & Slesinger, P. A.
Venue
Nature Neuroscience
Publisher
Springer Science and Business Media LLC
Published
2007-09-02
Volume
10
Issue
10
Pages
1249-1259
ISSN
  • 1097-6256
  • 1546-1726
DOI
10.1038/nn1953
Cited by
151
References
1
Language
en
Licence
www.springer.com/tdm (tdm)

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