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Volumn 20, Issue 5, 2011, Pages 555-560

Structural mechanisms underlying the function of epithelial sodium channel/acid-sensing ion channel

Author keywords

acid sensing ion channel; epithelial sodium channel; gating

Indexed keywords

ACID SENSING ION CHANNEL; CHLORIDE; EPITHELIAL SODIUM CHANNEL; PROTON;

EID: 80051795268     PISSN: 10624821     EISSN: 14736543     Source Type: Journal    
DOI: 10.1097/MNH.0b013e328348bcac     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 33646489456 scopus 로고    scopus 로고
    • FMRFamide-gated sodium channel and ASIC channels: A new class of ionotropic receptors for FMRFamide and related peptides
    • Lingueglia E, Deval E, Lazdunski M. FMRFamide-gated sodium channel and ASIC channels: a new class of ionotropic receptors for FMRFamide and related peptides. Peptides 2006;27:1138-1152.
    • (2006) Peptides , vol.27 , pp. 1138-1152
    • Lingueglia, E.1    Deval, E.2    Lazdunski, M.3
  • 2
    • 33748797928 scopus 로고    scopus 로고
    • Acid-sensing ion channels: advances, questions and therapeutic opportunities
    • DOI 10.1016/j.tins.2006.06.014, PII S0166223606001706
    • Wemmie JA, Price MP, Welsh MJ. Acid-sensing ion channels: advances, questions and therapeuticopportunities. Trends Neurosci 2006;29:578-586. (Pubitemid 44416458)
    • (2006) Trends in Neurosciences , vol.29 , Issue.10 , pp. 578-586
    • Wemmie, J.A.1    Price, M.P.2    Welsh, M.J.3
  • 4
    • 0036307827 scopus 로고    scopus 로고
    • Epithelial sodium channel/degenerin family of ion channels: A variety of functions for a shared structure
    • Kellenberger S, Schild L. Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure. Physiol Rev 2002;82:735-767. (Pubitemid 34743337)
    • (2002) Physiological Reviews , vol.82 , Issue.3 , pp. 735-767
    • Kellenberger, S.1    Schild, L.2
  • 5
    • 2442718786 scopus 로고    scopus 로고
    • + absorption produces cystic fibrosis-like lung disease in mice
    • DOI 10.1038/nm1028
    • Mall M, Grubb BR, Harkema JR, et al. Increased airway epithelial Na+ absorption produces cystic fibrosis-like lung disease in mice. Nat Med 2004;10:487-493. (Pubitemid 38667907)
    • (2004) Nature Medicine , vol.10 , Issue.5 , pp. 487-493
    • Mall, M.1    Grubb, B.R.2    Harkema, J.R.3    O'Neal, W.K.4    Boucher, R.C.5
  • 6
    • 34548813656 scopus 로고    scopus 로고
    • Structure of acid-sensing ion channel 1 at 1.9 Aresolution and low pH
    • DOI 10.1038/nature06163, PII NATURE06163
    • Jasti J, Furukawa H, Gonzales EB, Gouaux E. Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH. Nature 2007;449:316-323. (Pubitemid 47443482)
    • (2007) Nature , vol.449 , Issue.7160 , pp. 316-323
    • Jasti, J.1    Furukawa, H.2    Gonzales, E.B.3    Gouaux, E.4
  • 7
    • 67949092829 scopus 로고    scopus 로고
    • Pore architecture and ion sites in acidsensing ion channels and P2X receptors
    • Gonzales EB, Kawate T, Gouaux E. Pore architecture and ion sites in acidsensing ion channels and P2X receptors. Nature 2009;460:599-604.
    • (2009) Nature , vol.460 , pp. 599-604
    • Gonzales, E.B.1    Kawate, T.2    Gouaux, E.3
  • 8
    • 0036023395 scopus 로고    scopus 로고
    • Na self inhibition of human epithelial Na channel: Temperature dependence and effect of extracellular proteases
    • DOI 10.1085/jgp.20028612
    • Chraibi A, Horisberger JD. Na self inhibition of human epithelial Na channel: temperature dependence and effect of extracellular proteases. J Gen Physiol 2002;120:133-145. (Pubitemid 34857964)
    • (2002) Journal of General Physiology , vol.120 , Issue.2 , pp. 133-145
    • Chraibi, A.1    Horisberger, J.-D.2
  • 9
    • 70350399476 scopus 로고    scopus 로고
    • Extracellular chloride regulates the epithelial sodium channel
    • Collier DM, Snyder PM. Extracellular chloride regulates the epithelial sodium channel. J Biol Chem 2009;284:29320-29325.
    • (2009) J Biol Chem , vol.284 , pp. 29320-29325
    • Collier, D.M.1    Snyder, P.M.2
  • 11
    • 68949094195 scopus 로고    scopus 로고
    • ENaC at the cutting edge: Regulation of epithelial sodium channels by proteases
    • Kleyman TR, Carattino MD, Hughey RP. ENaC at the cutting edge: regulation of epithelial sodium channels by proteases. J Biol Chem 2009;284:20447-20451.
    • (2009) J Biol Chem , vol.284 , pp. 20447-20451
    • Kleyman, T.R.1    Carattino, M.D.2    Hughey, R.P.3
  • 12
    • 0033695107 scopus 로고    scopus 로고
    • Neuropeptide FF and FMRFamide potentiate acid-evoked currents from sensory neurons and proton-gated DEG/ENaC channels
    • Askwith CC, Cheng C, Ikuma M, et al. Neuropeptide FF and FMRFamide potentiate acid-evoked currents from sensory neurons and proton-gated DEG/ENaC channels. Neuron 2000;26:133-141.
    • (2000) Neuron , vol.26 , pp. 133-141
    • Askwith, C.C.1    Cheng, C.2    Ikuma, M.3
  • 13
    • 38349137692 scopus 로고    scopus 로고
    • Endogenous arginine-phenylalanine-amiderelated peptides alter steady-state desensitization of ASIC1a
    • Sherwood TW, Askwith CC. Endogenous arginine-phenylalanine-amiderelated peptides alter steady-state desensitization of ASIC1a. J Biol Chem 2008;283:1818-1830.
    • (2008) J Biol Chem , vol.283 , pp. 1818-1830
    • Sherwood, T.W.1    Askwith, C.C.2
  • 14
    • 70449623627 scopus 로고    scopus 로고
    • Dynorphin opioid peptides enhance acid-sensing ion channel 1a activity and acidosis-induced neuronal death
    • Sherwood TW, Askwith CC. Dynorphin opioid peptides enhance acid-sensing ion channel 1a activity and acidosis-induced neuronal death. J Neurosci 2009;29:14371-14380.
    • (2009) J Neurosci , vol.29 , pp. 14371-14380
    • Sherwood, T.W.1    Askwith, C.C.2
  • 16
    • 58149335369 scopus 로고    scopus 로고
    • Physiologic regulation of the epithelial sodium channel by phosphatidylinositides
    • Pochynyuk O, Bugaj V, Stockand JD. Physiologic regulation of the epithelial sodium channel by phosphatidylinositides. Curr Opin Nephrol Hypertens 2008;17:533-540.
    • (2008) Curr Opin Nephrol Hypertens , vol.17 , pp. 533-540
    • Pochynyuk, O.1    Bugaj, V.2    Stockand, J.D.3
  • 17
    • 59449106459 scopus 로고    scopus 로고
    • Extracellular protons regulate human ENaC by modulating Na+ self-inhibition
    • Collier DM, Snyder PM. Extracellular protons regulate human ENaC by modulating Na+ self-inhibition. J Biol Chem 2009;284:792-798.
    • (2009) J Biol Chem , vol.284 , pp. 792-798
    • Collier, D.M.1    Snyder, P.M.2
  • 18
    • 38049100869 scopus 로고    scopus 로고
    • Candidate amino acids involved in H+ gating of acid-sensing ion channel 1a
    • Paukert M, Chen X, Polleichtner G, et al. Candidate amino acids involved in H+ gating of acid-sensing ion channel 1a. J Biol Chem 2008;283:572-581.
    • (2008) J Biol Chem , vol.283 , pp. 572-581
    • Paukert, M.1    Chen, X.2    Polleichtner, G.3
  • 19
    • 77952365948 scopus 로고    scopus 로고
    • A combined computational and functional approach identifies new residues involved in pH-dependent gating of ASIC1a
    • Liechti LA, Bernèche S, Bargeton B, et al. A combined computational and functional approach identifies new residues involved in pH-dependent gating of ASIC1a. J Biol Chem 2010;285:16315-16329.
    • (2010) J Biol Chem , vol.285 , pp. 16315-16329
    • Liechti, L.A.1    Bernèche, S.2    Bargeton, B.3
  • 20
    • 63249117189 scopus 로고    scopus 로고
    • Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels
    • Li T, Yang Y, Canessa CM. Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels. J Biol Chem 2009;284:4689-4694.
    • (2009) J Biol Chem , vol.284 , pp. 4689-4694
    • Li, T.1    Yang, Y.2    Canessa, C.M.3
  • 21
    • 70350441287 scopus 로고    scopus 로고
    • Identification of protein domains that control proton and calcium sensitivity of ASIC1a
    • Sherwood T, Franke R, Conneely S, et al. Identification of protein domains that control proton and calcium sensitivity of ASIC1a. J Biol Chem 2009;284:27899-27907.
    • (2009) J Biol Chem , vol.284 , pp. 27899-27907
    • Sherwood, T.1    Franke, R.2    Conneely, S.3
  • 22
    • 33947715893 scopus 로고    scopus 로고
    • A conformation change in the extracellular domain that accompanies desensitization of acid-sensing ion channel (ASIC) 3
    • DOI 10.1085/jgp.200709757
    • Cushman KA, Marsh-Haffner J, Adelman JP, McCleskey EW. A conformation change in the extracellular domain that accompanies desensitization of acidsensing ion channel (ASIC) 3. J Gen Physiol 2007;129:345-350. (Pubitemid 46506984)
    • (2007) Journal of General Physiology , vol.129 , Issue.4 , pp. 345-350
    • Cushman, K.A.1    Marsh-Haffner, J.2    Adelman, J.P.3    McCleskey, E.W.4
  • 23
    • 0242496525 scopus 로고    scopus 로고
    • The Extracellular Domain Determines the Kinetics of Desensitization in Acid-sensitive Ion Channel 1
    • DOI 10.1074/jbc.M304441200
    • Coric T, Zhang P, Todorovic N, Canessa CM. The extracellular domain determines the kinetics of desensitization in acid-sensitive ion channel 1. J Biol Chem 2003;278:45240-45247. (Pubitemid 37432658)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45240-45247
    • Coric, T.1    Zhang, P.2    Todorovic, N.3    Canessa, C.M.4
  • 24
    • 77957797513 scopus 로고    scopus 로고
    • Asn415 in the beta11-beta12 linker decreases proton-dependent desensitization of ASIC1
    • Li T, Yang Y, Canessa CM. Asn415 in the beta11-beta12 linker decreases proton-dependent desensitization of ASIC1. J Biol Chem 2010;285:31285-31291.
    • (2010) J Biol Chem , vol.285 , pp. 31285-31291
    • Li, T.1    Yang, Y.2    Canessa, C.M.3
  • 25
    • 77951523610 scopus 로고    scopus 로고
    • The contact region between three domains of the extracellular loop of ASIC1a is critical for channel function
    • Bargeton B, Kellenberger S. The contact region between three domains of the extracellular loop of ASIC1a is critical for channel function. J Biol Chem 2010;285:13816-13826.
    • (2010) J Biol Chem , vol.285 , pp. 13816-13826
    • Bargeton, B.1    Kellenberger, S.2
  • 26
    • 79955423693 scopus 로고    scopus 로고
    • Base of the thumb domain modulates epithelial sodium channel gating
    • Shi H, Ghosh DD, Okumura S, et al. Base of the thumb domain modulates epithelial sodium channel gating. J Biol Chem 2011;286:14753-14761.
    • (2011) J Biol Chem , vol.286 , pp. 14753-14761
    • Shi, H.1    Ghosh, D.D.2    Okumura, S.3
  • 31
    • 34547769366 scopus 로고    scopus 로고
    • Mechano-sensitivity of epithelial sodium channels (ENaCs): Laminar shear stress increases ion channel open probability
    • DOI 10.1096/fj.06-7694com
    • Althaus M, Bogdan R, Clauss WG, Fronius M. Mechano-sensitivity of epithelial sodium channels (ENaCs): laminar shear stress increases ion channel open probability. FASEB J 2007;21:2389-2399. (Pubitemid 47230669)
    • (2007) FASEB Journal , vol.21 , Issue.10 , pp. 2389-2399
    • Althaus, M.1    Bogdan, R.2    Clauss, W.G.3    Fronius, M.4
  • 32
    • 79955784697 scopus 로고    scopus 로고
    • Second transmembrane domain modulates epithelial sodium channel gating in response to shear stress
    • Abi-Antoun T, Shi S, Tolino LA, et al. Second transmembrane domain modulates epithelial sodium channel gating in response to shear stress. Am J Physiol Renal Physiol 2011;300:F1089-F1095.
    • (2011) Am J Physiol Renal Physiol , vol.300
    • Abi-Antoun, T.1    Shi, S.2    Tolino, L.A.3
  • 34
    • 73649085483 scopus 로고    scopus 로고
    • Conformational changes associated with proton-dependent gating of ASIC1a
    • Passero CJ, Okumura S, Carattino MD. Conformational changes associated with proton-dependent gating of ASIC1a. J Biol Chem 2009;284:36473-36481.
    • (2009) J Biol Chem , vol.284 , pp. 36473-36481
    • Passero, C.J.1    Okumura, S.2    Carattino, M.D.3
  • 35
    • 79955546832 scopus 로고    scopus 로고
    • Insights into the mechanism of pore opening of acid-sensing ion channel 1A
    • Tolino LA, Okumura S, Kashlan OB, Carattino MD. Insights into the mechanism of pore opening of acid-sensing ion channel 1A. J Biol Chem 2011;286:16297-16307. The permeation pathway of ASIC1a is constituted by the residues in the TM2 segments. To allow ion permeation the TM2 segments need to rotate, tilt, or both. Y424C-G428Csubunits were associated by intersubunit disulfide bonds formed at the outer vestibule of the pore. These double Cys mutant channels transit between the resting, open, and desensitized states following extracellular acidification. The results of this study indicate that a concerted rotation in the clockwise direction of the TM2 helices could increase the diameter of the pore of Y424C-G428C allowing ion permeation.
    • (2011) J Biol Chem , vol.286 , pp. 16297-16307
    • Tolino, L.A.1    Okumura, S.2    Kashlan, O.B.3    Carattino, M.D.4
  • 37
    • 78049373320 scopus 로고    scopus 로고
    • + channel through peptide binding at peripheral finger and thumb domains
    • + channel through peptide binding at peripheral finger and thumb domains. J Biol Chem 2010;285:35216-35223. Proteolytic processing of the a and γ ENaCsubunits releases inhibitory peptides and increases Po. Mutations in the a subunit finger-thumb interface affect apparent affinity of an 8-mer inhibitory peptide. This study suggests that the a inhibitory tract in noncleaved channels reduces Po by constraining motions within the thumb and finger domains.
    • (2010) J Biol Chem , vol.285 , pp. 35216-35223
    • Kashlan, O.B.1    Boyd, C.R.2    Argyropoulos, C.3
  • 38
    • 78650934293 scopus 로고    scopus 로고
    • + channel alpha subunit reveals a mechanism of channel activation by proteases
    • + channel alpha subunit reveals a mechanism of channel activation by proteases. J Biol Chem 2011;286:649-660.
    • (2011) J Biol Chem , vol.286 , pp. 649-660
    • Kashlan, O.B.1    Adelman, J.L.2    Okumura, S.3
  • 39
    • 0021012702 scopus 로고
    • Competitive blocking of epithelial sodium channels by organic cations: The relationship between macroscopic and microscopic inhibition constants
    • Li JH, Lindemann B. Competitive blocking of epithelial sodium channels by organic cations: the relationship between macroscopic and microscopic inhibition constants. J Membr Biol 1983;76:235-251. (Pubitemid 14201483)
    • (1983) Journal of Membrane Biology , vol.76 , Issue.3 , pp. 235-251
    • Li, J.H.Y.1    Lindemann, B.2
  • 42
    • 65549132928 scopus 로고    scopus 로고
    • Novel determinants of epithelial sodium channel gating within extracellular thumb domains
    • Maarouf AB, Sheng N, Chen J, et al. Novel determinants of epithelial sodium channel gating within extracellular thumb domains. J Biol Chem 2009;284:7756-7765.
    • (2009) J Biol Chem , vol.284 , pp. 7756-7765
    • Maarouf, A.B.1    Sheng, N.2    Chen, J.3
  • 44
    • 70450273065 scopus 로고    scopus 로고
    • Structural elements for the generation of sustained currents by the acid pain sensor ASIC3
    • Salinas M, Lazdunski M, Lingueglia E. Structural elements for the generation of sustained currents by the acid pain sensor ASIC3. J Biol Chem 2009;284:31851-31859.
    • (2009) J Biol Chem , vol.284 , pp. 31851-31859
    • Salinas, M.1    Lazdunski, M.2    Lingueglia, E.3
  • 45
    • 70350023553 scopus 로고    scopus 로고
    • + channel is masked by a conserved transmembrane domain tryptophan
    • + channel is masked by a conserved transmembrane domain tryptophan. J Biol Chem 2009;284:25512-25521.
    • (2009) J Biol Chem , vol.284 , pp. 25512-25521
    • Pochynyuk, O.1    Kucher, V.2    Boiko, N.3
  • 46
    • 77952943039 scopus 로고    scopus 로고
    • Extracellular chloride modulates the desensitization kinetics of acid-sensing ion channel 1a (ASIC1a)
    • Kusama N, Harding AM, Benson CJ. Extracellular chloride modulates the desensitization kinetics of acid-sensing ion channel 1a (ASIC1a). J Biol Chem 2010;285:17425-17431.
    • (2010) J Biol Chem , vol.285 , pp. 17425-17431
    • Kusama, N.1    Harding, A.M.2    Benson, C.J.3
  • 47
    • 79953169501 scopus 로고    scopus 로고
    • - inhibitory residues suggests a trimeric alpha gamma beta channel architecture
    • --binding sites suggest that ENaC subunits are arranged in an αγβ clockwise orientation when viewed from the extracellular side.
    • (2011) J Biol Chem , vol.286 , pp. 6027-6032
    • Collier, D.M.1    Snyder, P.M.2
  • 48
    • 54449088865 scopus 로고    scopus 로고
    • Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation
    • Carattino MD, Hughey RP, Kleyman TR. Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation. J Biol Chem 2008;283:25290-25295.
    • (2008) J Biol Chem , vol.283 , pp. 25290-25295
    • Carattino, M.D.1    Hughey, R.P.2    Kleyman, T.R.3
  • 49
    • 0037515623 scopus 로고    scopus 로고
    • Asymmetric organization of the pore region of the epithelial sodium channel
    • DOI 10.1074/jbc.M300149200
    • Li J, Sheng S, Perry CJ, Kleyman TR. Asymmetric organization of the pore region of the epithelial sodium channel. J Biol Chem 2003;278:13867-13874. (Pubitemid 36799926)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13867-13874
    • Li, J.1    Sheng, S.2    Perry, C.J.3    Kleyman, T.R.4


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