One SUMO is sufficient to silence the dimeric potassium channel K2P1

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 23, 2010, Pages 10743-10748

  Plant, Leigh D ^a   Dementieva, Irina S ^a   Kollewe, Astrid ^a   Olikara, Sonia ^a   Marks, Jeremy D ^a   Goldstein, Steve A N ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

KCNK1; SAE1; SENP1; TWIK1; Ubc9

Indexed keywords

AMINO ACID; POTASSIUM CHANNEL; POTASSIUM CHANNEL K2P1; SUMO 1 PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL MEMBRANE; CONFOCAL MICROSCOPY; CONJUGATION; CONTROLLED STUDY; DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENE SILENCING; HUMAN; HUMAN CELL; IMMUNOCYTOCHEMISTRY; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; CELL MEMBRANE; CELL SURVIVAL; CHO CELLS; CRICETINAE; CRICETULUS; HUMANS; POTASSIUM CHANNELS, TANDEM PORE DOMAIN; PROTEIN MULTIMERIZATION; SUMO-1 PROTEIN;

MAMMALIA;

EID: 77953798315     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1004712107     Document Type: Article

References (30)

1. Hay RT (2005) SUMO: A history of modification. Mol Cell 18:1-12.
2. Rajan S, Plant LD, Rabin ML, Butler MH, Goldstein SAN (2005) Sumoylation silences the plasma membrane leak K+ channel K2P1. Cell 121:37-47. (Pubitemid 40501166)
3. Benson MD, et al. (2007) SUMO modification regulates inactivation of the voltage-gated potassium channel Kv1.5. Proc Natl Acad Sci USA 104:1805-1810. (Pubitemid 46239860)
4. Dai XQ, Kolic J, Marchi P, Sipione S, Macdonald PE (2009) SUMOylation regulates Kv2.1 and modulates pancreatic β-cell excitability. J Cell Sci 122:775-779.
5. Martin S, Nishimune A, Mellor JR, Henley JM (2007) SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature 447:321-325. (Pubitemid 46788827)
6. Kruse M, et al. (2009) Impaired endocytosis of the ion channel TRPM4 is associated with human progressive familial heart block type I. J Clin Invest 119:2737-2744.
7. + channels? Cell 130:563-569.
8. Feliciangeli S, et al. (2010) Potassium channel silencing by constitutive endocytosis and intracellular sequestration. J Biol Chem 285:4798-4805.
9. Thomas D, Goldstein SAN (2009) Two-P-domain (K2P) potassium channels: Leak conductance regulators of excitability. Encyclopedia of Neuroscience, ed Squire LR (Elsevier, Academic Press, Oxford), Vol 9, pp 1207-1220.
10. Ketchum KA, Joiner WJ, Sellers AJ, Kaczmarek LK, Goldstein SAN (1995) A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem. Nature 376:690-695.
11. Goldstein SAN, Price LA, Rosenthal DN, Pausch MH (1996) ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 93:13256-13261.
12. Ilan N, Goldstein SAN (2001) Kcnkø: Single, cloned potassium leak channels are multiion pores. Biophys J 80:241-253.
13. Zilberberg N, Ilan N, Goldstein SA (2001) KCNKØ: Opening and closing the 2-P-domain potassium leak channel entails "C-type" gating of the outer pore. Neuron 32:635-648.
14. Talley EM, Lei QB, Sirois JE, Bayliss DA (2000) TASK-1, a two-pore domain K+ channel, is modulated by multiple neurotransmitters in motoneurons. Neuron 25:399-410.
15. Lopes CMB, Zilberberg N, Goldstein SAN (2001) Block of Kcnk3 by protons. Evidence that 2-P-domain potassium channel subunits function as homodimers. J Biol Chem 276:24449-24452. (Pubitemid 37412904)
16. Kollewe A, Lau AY, Sullivan A, Benoît Roux, Goldstein SAN (2009) A structural model for K2P potassium channels based on 23 pairs of interacting sites and continuum electrostatics. J Gen Physiol 134:53-68.
17. Berg AP, Talley EM, Manger JP, Bayliss DA (2004) Motoneurons express heteromeric TWIK-related acid-sensitive K+ (TASK) channels containing TASK-1 (KCNK3) and TASK-3 (KCNK9) subunits. J Neurosci 24:6693-6702.
18. Zlatkine P, Mehul B, Magee AI (1997) Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif. J Cell Sci 110:673-679. (Pubitemid 27153981)
19. Takahashi H, Hatakeyama S, Saitoh H, Nakayama KI (2005) Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. J Biol Chem 280:5611-5621. (Pubitemid 40280040)
20. Uchimura Y, Nakamura M, Sugasawa K, Nakao M, Saitoh H (2004) Overproduction of eukaryotic SUMO-1- and SUMO-2-conjugated proteins in Escherichia coli. Anal Biochem 331:204-206. (Pubitemid 38881579)
21. Knuesel M, Cheung HT, Hamady M, Barthel KKB, Liu X (2005) A method of mapping protein sumoylation sites by mass spectrometry using a modified small ubiquitin-like modifier 1 (SUMO-1) and a computational program. Mol Cell Proteomics 4:1626-1636.
22. Sampson DA, Wang M, Matunis MJ (2001) The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J Biol Chem 276:21664-21669.
23. Ulbrich MH, Isacoff EY (2007) Subunit counting in membrane-bound proteins. Nat Methods 4:319-321.
24. Johnson ES, Blobel G (1999) Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J Cell Biol 147:981-994.
25. Shen L, et al. (2006) SUMO protease SENP1 induces isomerization of the scissile peptide bond. Nat Struct Mol Biol 13:1069-1077.
26. Lesage F, et al. (1996) TWIK-1, a ubiquitous human weakly inward rectifying K+ channel with a novel structure. EMBO J 15:1004-1011.
27. Goldstein SAN, Wang KW, Ilan N, Pausch MH (1998) Sequence and function of the two P domain potassium channels: Implications of an emerging superfamily. J Mol Med 76:13-20.
28. O'Kelly I, Butler MH, Zilberberg N, Goldstein SA (2002) Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111:577-588.
29. Jakobs A, et al. (2007) Ubc9 fusion-directed SUMOylation (UFDS): A method to analyze function of protein SUMOylation. Nat Methods 4:245-250.
30. Plant LD, Zuniga L, Olikara S, Marks J, Goldstein SAN (2010) K2P1 assembles with K2P3 or K2P9 to form SUMO-regulated TASK background channels. Biophys J 98:710a.