메뉴 건너뛰기




Volumn 7, Issue 8, 2006, Pages 787-793

The versatile nature of the calcium-permeable cation channel TRPP2

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CALCIUM ION; CATION CHANNEL; POLYCYSTIN 1; POLYCYSTIN 2; TRANSIENT RECEPTOR POTENTIAL CHANNEL;

EID: 33747769976     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400745     Document Type: Review
Times cited : (96)

References (67)
  • 2
    • 0033598394 scopus 로고    scopus 로고
    • A polycystic kidney-disease gene homologue required for male mating behaviour in C. elegans
    • Barr MM, Sternberg PW (1999) A polycystic kidney-disease gene homologue required for male mating behaviour in C. elegans. Nature 401: 386-389
    • (1999) Nature , vol.401 , pp. 386-389
    • Barr, M.M.1    Sternberg, P.W.2
  • 3
    • 0035806961 scopus 로고    scopus 로고
    • The Caenorhabditis elegans autosomal dominant polycystic kidney disease gene homologs lov-1 and pkd-2 act in the same pathway
    • Barr MM, DeModena J, Braun D, Nguyen CQ, Hall DH, Sternberg PW (2001) The Caenorhabditis elegans autosomal dominant polycystic kidney disease gene homologs lov-1 and pkd-2 act in the same pathway. Curr Biol 11: 1341-1346
    • (2001) Curr Biol , vol.11 , pp. 1341-1346
    • Barr, M.M.1    DeModena, J.2    Braun, D.3    Nguyen, C.Q.4    Hall, D.H.5    Sternberg, P.W.6
  • 4
    • 0037133954 scopus 로고    scopus 로고
    • PKD1 induces p21(waf1) and regulation of the cell cycle via direct activation of the JAK-STAT signaling pathway in a process requiring PKD2
    • Bhunia AK, Piontek K, Boletta A, Liu L, Qian F, Xu PN, Germino FJ, Germino GG (2002) PKD1 induces p21(waf1) and regulation of the cell cycle via direct activation of the JAK-STAT signaling pathway in a process requiring PKD2. Cell 109: 157-168
    • (2002) Cell , vol.109 , pp. 157-168
    • Bhunia, A.K.1    Piontek, K.2    Boletta, A.3    Liu, L.4    Qian, F.5    Xu, P.N.6    Germino, F.J.7    Germino, G.G.8
  • 6
    • 2442605494 scopus 로고    scopus 로고
    • Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812
    • Cai Y et al (2004) Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812. J Biol Chem 279: 19987-19995
    • (2004) J Biol Chem , vol.279 , pp. 19987-19995
    • Cai, Y.1
  • 7
    • 85047694216 scopus 로고    scopus 로고
    • Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus
    • Chauvet V et al (2004) Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus. J Clin Invest 114: 1433-1443
    • (2004) J Clin Invest , vol.114 , pp. 1433-1443
    • Chauvet, V.1
  • 9
    • 29844451971 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels
    • Clapham DE, Julius D, Montell C, Schultz G (2005) International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels. Pharmacol Rev 57: 427-450
    • (2005) Pharmacol Rev , vol.57 , pp. 427-450
    • Clapham, D.E.1    Julius, D.2    Montell, C.3    Schultz, G.4
  • 10
    • 3242728834 scopus 로고    scopus 로고
    • Polycystins: From mechanosensation to gene regulation
    • Delmas P (2004a) Polycystins: From mechanosensation to gene regulation. Cell 118: 145-148
    • (2004) Cell , vol.118 , pp. 145-148
    • Delmas, P.1
  • 11
    • 2342573670 scopus 로고    scopus 로고
    • Assembly and gating of TRPC channels in signalling microdomains
    • 75-89; discussion 89-102
    • Delmas P (2004b) Assembly and gating of TRPC channels in signalling microdomains. Novartis Found Symp 258: 75-89; discussion 89-102, 263-266
    • (2004) Novartis Found Symp , vol.258 , pp. 263-266
    • Delmas, P.1
  • 12
    • 24644485135 scopus 로고    scopus 로고
    • Polycystins: Polymodal receptor/ion-channel cellular sensors
    • Delmas P (2005) Polycystins: Polymodal receptor/ion-channel cellular sensors. Pflugers Arch 451: 264-276
    • (2005) Pflugers Arch , vol.451 , pp. 264-276
    • Delmas, P.1
  • 13
    • 0037192763 scopus 로고    scopus 로고
    • Constitutive activation of G-proteins by polycystin-1 is antagonized by polycystin-2
    • Delmas P et al (2002) Constitutive activation of G-proteins by polycystin-1 is antagonized by polycystin-2. J Biol Chem 277: 11276-11283
    • (2002) J Biol Chem , vol.277 , pp. 11276-11283
    • Delmas, P.1
  • 17
    • 0345772211 scopus 로고    scopus 로고
    • PKD2 cation channel is required for directional sperm movement and male fertility
    • Gao Z, Ruden DM, Lu X (2003) PKD2 cation channel is required for directional sperm movement and male fertility. Curr Biol 13: 2175-2178
    • (2003) Curr Biol , vol.13 , pp. 2175-2178
    • Gao, Z.1    Ruden, D.M.2    Lu, X.3
  • 18
    • 33646764178 scopus 로고    scopus 로고
    • Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif
    • Geng L, Okuhara D, Yu Z, Tian X, Cai Y, Shibazaki S, Somlo S (2006) Polycystin-2 traffics to cilia independently of polycystin-1 by using an N-terminal RVxP motif. J Cell Sci 119: 1383-1395
    • (2006) J Cell Sci , vol.119 , pp. 1383-1395
    • Geng, L.1    Okuhara, D.2    Yu, Z.3    Tian, X.4    Cai, Y.5    Shibazaki, S.6    Somlo, S.7
  • 21
    • 4544321242 scopus 로고    scopus 로고
    • PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2
    • Hidaka S, Konecke V, Osten L, Witzgall R (2004) PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2. J Biol Chem 279: 35009-35016
    • (2004) J Biol Chem , vol.279 , pp. 35009-35016
    • Hidaka, S.1    Konecke, V.2    Osten, L.3    Witzgall, R.4
  • 22
    • 0037059738 scopus 로고    scopus 로고
    • 2+ channels involved in triggering the sea urchin sperm acrosome reaction
    • 2+ channels involved in triggering the sea urchin sperm acrosome reaction. J Biol Chem 277: 1182-1189
    • (2002) J Biol Chem , vol.277 , pp. 1182-1189
    • Hirohashi, N.1    Vacquier, V.D.2
  • 23
    • 0036707893 scopus 로고    scopus 로고
    • Genetics and pathogenesis of polycystic kidney disease
    • Igarashi P, Somlo S (2002) Genetics and pathogenesis of polycystic kidney disease. J Am Soc Nephrol 13: 2384-2398
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2384-2398
    • Igarashi, P.1    Somlo, S.2
  • 24
    • 33645950434 scopus 로고    scopus 로고
    • Lack of a laterality phenotype in Pkd1 knock-out embryos correlates with absence of polycystin-1 in nodal cilia
    • Karcher C, Fischer A, Schweickert A, Bitzer E, Horie S, Witzgall R, Blum M (2005) Lack of a laterality phenotype in Pkd1 knock-out embryos correlates with absence of polycystin-1 in nodal cilia. Differentiation 73: 425-432
    • (2005) Differentiation , vol.73 , pp. 425-432
    • Karcher, C.1    Fischer, A.2    Schweickert, A.3    Bitzer, E.4    Horie, S.5    Witzgall, R.6    Blum, M.7
  • 25
    • 26444598978 scopus 로고    scopus 로고
    • Subcellular localization and trafficking of polycystins
    • Köttgen M, Walz G (2005) Subcellular localization and trafficking of polycystins. Pflugers Arch 451: 286-293
    • (2005) Pflugers Arch , vol.451 , pp. 286-293
    • Köttgen, M.1    Walz, G.2
  • 26
    • 20144383835 scopus 로고    scopus 로고
    • Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation
    • Köttgen M et al (2005a) Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. EMBO J 24: 705-716
    • (2005) EMBO J , vol.24 , pp. 705-716
    • Köttgen, M.1
  • 27
    • 33747801008 scopus 로고    scopus 로고
    • Polycystin-2 and TRPV4 form a functional heteromultimeric complex that might act as a cilial mechanosensor
    • Köttgen M et al (2005b) Polycystin-2 and TRPV4 form a functional heteromultimeric complex that might act as a cilial mechanosensor. J Am Soc Nephrol 16: TH-FC116
    • (2005) J Am Soc Nephrol , vol.16
    • Köttgen, M.1
  • 30
    • 0037051960 scopus 로고    scopus 로고
    • The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation
    • Li Q, Liu Y, Zhao W, Chen XZ (2002) The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation. FEBS Lett 516: 270-278
    • (2002) FEBS Lett , vol.516 , pp. 270-278
    • Li, Q.1    Liu, Y.2    Zhao, W.3    Chen, X.Z.4
  • 31
    • 28544433252 scopus 로고    scopus 로고
    • Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor ld2
    • Li X, Luo Y, Starremans PG, McNamara CA, Pei Y, Zhou J (2005) Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor ld2. Nat Cell Biol 7: 1102-1112
    • (2005) Nat Cell Biol , vol.7 , pp. 1102-1112
    • Li, X.1    Luo, Y.2    Starremans, P.G.3    McNamara, C.A.4    Pei, Y.5    Zhou, J.6
  • 35
    • 24344482068 scopus 로고    scopus 로고
    • PKD2 functions as an epidermal growth factor-activated plasma membrane channel
    • Ma R, Li WP, Rundle D, Kong J, Akbarali HI, Tsiokas L (2005) PKD2 functions as an epidermal growth factor-activated plasma membrane channel. Mol Cell Biol 18: 8285-8298
    • (2005) Mol Cell Biol , vol.18 , pp. 8285-8298
    • Ma, R.1    Li, W.P.2    Rundle, D.3    Kong, J.4    Akbarali, H.I.5    Tsiokas, L.6
  • 37
    • 0038784537 scopus 로고    scopus 로고
    • Two populations of node monocilia initiate left-right asymmetry in the mouse
    • McGrath J, Somlo S, Makova S, Tian X, Brueckner M (2003) Two populations of node monocilia initiate left-right asymmetry in the mouse. Cell 114: 61-73
    • (2003) Cell , vol.114 , pp. 61-73
    • McGrath, J.1    Somlo, S.2    Makova, S.3    Tian, X.4    Brueckner, M.5
  • 38
    • 0002230688 scopus 로고    scopus 로고
    • suREJ proteins: New signalling molecules in sea urchin spermatozoa
    • Mengerink KJ, Moy GW, Vacquier VD (2000) suREJ proteins: New signalling molecules in sea urchin spermatozoa. Zygote 8 (Suppl 1): S28-S30
    • (2000) Zygote , vol.8 , Issue.SUPPL. 1
    • Mengerink, K.J.1    Moy, G.W.2    Vacquier, V.D.3
  • 39
    • 33644875032 scopus 로고    scopus 로고
    • The TRP superfamily of cation channels
    • Montell C (2005) The TRP superfamily of cation channels. Sci STKE 2005: re3
    • (2005) Sci STKE , vol.2005
    • Montell, C.1
  • 40
    • 0029977293 scopus 로고    scopus 로고
    • The sea urchin sperm receptor for egg jelly is a modular protein with extensive homology to the human polycystic kidney disease protein, PKD1
    • Moy GW, Mendoza LM, Schulz JR, Swanson WJ, Glabe CG, Vacquier VD (1996) The sea urchin sperm receptor for egg jelly is a modular protein with extensive homology to the human polycystic kidney disease protein, PKD1. J Cell Biol 133: 809-817
    • (1996) J Cell Biol , vol.133 , pp. 809-817
    • Moy, G.W.1    Mendoza, L.M.2    Schulz, J.R.3    Swanson, W.J.4    Glabe, C.G.5    Vacquier, V.D.6
  • 41
    • 0242266967 scopus 로고    scopus 로고
    • TRPV2 is a component of osmotically sensitive cation channels in murine aortic myocytes
    • Muraki K, Iwata Y, Katanosaka Y, Ito T, Ohya S, Shigekawa M, Imaizumi Y (2003) TRPV2 is a component of osmotically sensitive cation channels in murine aortic myocytes. Circ Res 93: 829-838
    • (2003) Circ Res , vol.93 , pp. 829-838
    • Muraki, K.1    Iwata, Y.2    Katanosaka, Y.3    Ito, T.4    Ohya, S.5    Shigekawa, M.6    Imaizumi, Y.7
  • 42
    • 4344672618 scopus 로고    scopus 로고
    • Polycystins and mechanosensation in renal and nodal cilia
    • Nauli SM, Zhou J (2004) Polycystins and mechanosensation in renal and nodal cilia. Bioessays 26: 844-856
    • (2004) Bioessays , vol.26 , pp. 844-856
    • Nauli, S.M.1    Zhou, J.2
  • 43
    • 0037317302 scopus 로고    scopus 로고
    • Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells
    • Nauli SM et al (2003) Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nat Genet 33: 129-137
    • (2003) Nat Genet , vol.33 , pp. 129-137
    • Nauli, S.M.1
  • 44
    • 1542286234 scopus 로고    scopus 로고
    • Polycystin-2 associates with the polycystin-1 homolog, suREJ3, and localizes to the acrosomal region of sea urchin spermatozoa
    • Neill AT, Moy GW, Vacquier VD (2004) Polycystin-2 associates with the polycystin-1 homolog, suREJ3, and localizes to the acrosomal region of sea urchin spermatozoa. Mol Reprod Dev 67: 472-477
    • (2004) Mol Reprod Dev , vol.67 , pp. 472-477
    • Neill, A.T.1    Moy, G.W.2    Vacquier, V.D.3
  • 45
    • 0037036350 scopus 로고    scopus 로고
    • Identification characterization, and localization of a novel kidney polycystin-1-polycystin-2 complex
    • Newby LJ, Streets AJ, Zhao Y, Harris PC, Ward CJ, Ong AC (2002) Identification, characterization, and localization of a novel kidney polycystin-1-polycystin-2 complex. J Biol Chem 277: 20763-20773
    • (2002) J Biol Chem , vol.277 , pp. 20763-20773
    • Newby, L.J.1    Streets, A.J.2    Zhao, Y.3    Harris, P.C.4    Ward, C.J.5    Ong, A.C.6
  • 46
    • 26444591482 scopus 로고    scopus 로고
    • TRP channels: aTR(I)P through a world of multifunctional cation channels
    • Nilius B, Voets T (2005) TRP channels: ATR(I)P through a world of multifunctional cation channels. Pflugers Arch 451: 1-10
    • (2005) Pflugers Arch , vol.451 , pp. 1-10
    • Nilius, B.1    Voets, T.2
  • 47
    • 26444496051 scopus 로고    scopus 로고
    • The mechanosensitive nature of TRPV channels
    • O'Neil RG, Heller S (2005) The mechanosensitive nature of TRPV channels. Pflugers Arch 451: 193-203
    • (2005) Pflugers Arch , vol.451 , pp. 193-203
    • O'Neil, R.G.1    Heller, S.2
  • 48
    • 0037019017 scopus 로고    scopus 로고
    • Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease
    • Pazour GJ, San Agustin JT, Follit JA, Rosenbaum JL, Witman GB (2002) Polycystin-2 localizes to kidney cilia and the ciliary level is elevated in orpk mice with polycystic kidney disease. Curr Biol 12: R378-R380
    • (2002) Curr Biol , vol.12
    • Pazour, G.J.1    San Agustin, J.T.2    Follit, J.A.3    Rosenbaum, J.L.4    Witman, G.B.5
  • 51
    • 0035498717 scopus 로고    scopus 로고
    • Bending the MDCK cell primary cilium increases intracellular calcium
    • Praetorius HA, Spring KR (2001) Bending the MDCK cell primary cilium increases intracellular calcium. J Membr Biol 184: 71-79
    • (2001) J Membr Biol , vol.184 , pp. 71-79
    • Praetorius, H.A.1    Spring, K.R.2
  • 52
    • 0037557518 scopus 로고    scopus 로고
    • Removal of the MDCK cell primary cilium abolishes flow sensing
    • Praetorius HA, Spring KR (2003) Removal of the MDCK cell primary cilium abolishes flow sensing. J Membr Biol 191: 69-76
    • (2003) J Membr Biol , vol.191 , pp. 69-76
    • Praetorius, H.A.1    Spring, K.R.2
  • 55
    • 28844435249 scopus 로고    scopus 로고
    • The nanomechanics of polycystin-1 extracellular region
    • Qian F, Wei W, Germino G, Oberhauser A (2005) The nanomechanics of polycystin-1 extracellular region. J Biol Chem 280: 40723-40730
    • (2005) J Biol Chem , vol.280 , pp. 40723-40730
    • Qian, F.1    Wei, W.2    Germino, G.3    Oberhauser, A.4
  • 58
    • 3142707455 scopus 로고    scopus 로고
    • PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: Role of mDia1 in PKD2 localization to mitotic spindles
    • Rundle DR, Gorbsky G, Tsiokas L (2004) PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: Role of mDia1 in PKD2 localization to mitotic spindles. J Biol Chem 279: 29728-29739
    • (2004) J Biol Chem , vol.279 , pp. 29728-29739
    • Rundle, D.R.1    Gorbsky, G.2    Tsiokas, L.3
  • 60
    • 33646155954 scopus 로고    scopus 로고
    • Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro
    • Streets AJ, Moon DJ, Kane ME, Obara T, Ong AC (2006). Identification of an N-terminal glycogen synthase kinase 3 phosphorylation site which regulates the functional localization of polycystin-2 in vivo and in vitro. Hum Mol Genet 15: 1465-1473
    • (2006) Hum Mol Genet , vol.15 , pp. 1465-1473
    • Streets, A.J.1    Moon, D.J.2    Kane, M.E.3    Obara, T.4    Ong, A.C.5
  • 62
    • 0030979629 scopus 로고    scopus 로고
    • Homo-and heterodimeric interactions between the gene products of PKD1 and PKD2
    • Tsiokas L, Kim E, Arnould T, Sukhatme VP, Walz G (1997) Homo-and heterodimeric interactions between the gene products of PKD1 and PKD2. Proc Natl Acad Sci USA 94: 6965-6970
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6965-6970
    • Tsiokas, L.1    Kim, E.2    Arnould, T.3    Sukhatme, V.P.4    Walz, G.5
  • 64
    • 0034810681 scopus 로고    scopus 로고
    • 2+ homeostasis in polycystic kidney disease
    • 2+ homeostasis in polycystic kidney disease. Biochem Biophys Res Commun 282: 341-350
    • (2001) Biochem Biophys Res Commun , vol.282 , pp. 341-350
    • Vassilev, P.M.1
  • 65
    • 0346403328 scopus 로고    scopus 로고
    • A flagellar polycystin-2 homolog required for male fertility in Drosophila
    • Watnick TJ, Jin Y, Matunis E, Kernan MJ, Montell C (2003) A flagellar polycystin-2 homolog required for male fertility in Drosophila. Curr Biol 13: 2179-2184
    • (2003) Curr Biol , vol.13 , pp. 2179-2184
    • Watnick, T.J.1    Jin, Y.2    Matunis, E.3    Kernan, M.J.4    Montell, C.5
  • 67
    • 0036785149 scopus 로고    scopus 로고
    • The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia
    • Yoder BK, Hou X, Guay-Woodford LM (2002) The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia. J Am Soc Nephrol 13: 2508-2516
    • (2002) J Am Soc Nephrol , vol.13 , pp. 2508-2516
    • Yoder, B.K.1    Hou, X.2    Guay-Woodford, L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.