메뉴 건너뛰기




Volumn 3 MAY, Issue , 2012, Pages

Role of βpix in the kidney

Author keywords

14 3 3; Cdc42; GEF; P21 activated kinase; Pix; Rac1; Small GTPase; Urothelium

Indexed keywords


EID: 84866422619     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2012.00154     Document Type: Review
Times cited : (11)

References (74)
  • 4
    • 28144436789 scopus 로고    scopus 로고
    • Serum- and glucocorticoid-regulated kinase 1 regulates ubiquitin ligase neural precursor cell-expressed, developmen-tally down-regulated protein 4-2 by inducing interaction with 14-3-3
    • Bhalla, V., Daidie, D., Li, H., Pao, A. C., LaGrange, L. P., Wang, J., Vande-walle, A., Stockand, J. D., Staub, O., and Pearce, D. (2005). Serum- and glucocorticoid-regulated kinase 1 regulates ubiquitin ligase neural precursor cell-expressed, developmen-tally down-regulated protein 4-2 by inducing interaction with 14-3-3. Mol. Endocrinol. 19, 3073-3084.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 3073-3084
    • Bhalla, V.1    Daidie, D.2    Li, H.3    Pao, A.C.4    LaGrange, L.P.5    Wang, J.6    Vande-walle, A.7    Stockand, J.D.8    Staub, O.9    Pearce, D.10
  • 5
    • 73949125284 scopus 로고    scopus 로고
    • Urothelial signaling
    • Birder, L. A. (2010). Urothelial signaling. Auton. Neurosci. 153, 33-40.
    • (2010) Auton. Neurosci. , vol.153 , pp. 33-40
    • Birder, L.A.1
  • 7
    • 0036261720 scopus 로고    scopus 로고
    • Leukemia-associated Rho guanine nucleotide exchange factor promotes Gαq-coupled activation of RhoA
    • Booden, M. A., Siderovski, D. P., and Der, C. J. (2002). Leukemia-associated Rho guanine nucleotide exchange factor promotes Gαq-coupled activation of RhoA. Mol. Cell Biol. 22, 4053-4061.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4053-4061
    • Booden, M.A.1    Siderovski, D.P.2    Der, C.J.3
  • 8
    • 30344437907 scopus 로고    scopus 로고
    • Characterization of the endogenous GIT1-βPIX complex and identification of its association to membranes
    • Botrugno, O. A., Paris, S., Za, L., Gual-doni, S., Cattaneo, A., Bachi, A., and de Curtis, I. (2006). Characterization of the endogenous GIT1-βPIX complex, and identification of its association to membranes. Eur. J. Cell Biol. 85, 35-46.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 35-46
    • Botrugno, O.A.1    Paris, S.2    Za, L.3    Gual-doni, S.4    Cattaneo, A.5    Bachi, A.6    de Curtis, I.7
  • 11
    • 12844258883 scopus 로고    scopus 로고
    • 1Pix translocation and Cdc42 activation via protein kinase A-dependent pathway
    • 1Pix translocation and Cdc42 activation via protein kinase A-dependent pathway. J. Biol. Chem. 280, 578-584.
    • (2005) J. Biol. Chem. , vol.280 , pp. 578-584
    • Chahdi, A.1    Miller, B.2    Sorokin, A.3
  • 13
    • 48749118026 scopus 로고    scopus 로고
    • Endothelin-1 couples βPix to p66Shc:role of βPix in cell proliferation through FOXO3a phosphorylation and p27kip1 down-regulation independently of Akt
    • Chahdi, A., and Sorokin, A. (2008a). Endothelin-1 couples βPix to p66Shc:role of βPix in cell proliferation through FOXO3a phosphorylation and p27kip1 down-regulation independently of Akt. Mol. Biol. Cell 19, 2609-2619.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2609-2619
    • Chahdi, A.1    Sorokin, A.2
  • 14
    • 40749160955 scopus 로고    scopus 로고
    • 1Pix gua-nine nucleotide exchange factor activity through 14-3-3 β binding
    • 1Pix gua-nine nucleotide exchange factor activity through 14-3-3 β binding. Mol. Cell Biol. 28, 1679-1687.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 1679-1687
    • Chahdi, A.1    Sorokin, A.2
  • 15
    • 70450222306 scopus 로고    scopus 로고
    • Endothelin-1 induces p66Shc activation through EGF receptor transac-tivation: role of (1Pix/G(i3 interaction Cell)
    • 1Pix/Gαi3 interaction. Cell. Signal. 22, 325-329
    • (2010) Signal , vol.22 , pp. 325-329
    • Chahdi, A.1    Sorokin, A.2
  • 16
    • 73949128415 scopus 로고    scopus 로고
    • The role of (1Pix/caveolin-1 interaction in endothelin signaling through G(subunits)
    • 1Pix/caveolin-1 interaction in endothelin signaling through Gαsubunits. Biochem. Biophys. Res. Commun. 391, 1330-1335.
    • (2010) Biochem. Biophys. Res. Commun , vol.391 , pp. 1330-1335
    • Chahdi, A.1    Sorokin, A.2
  • 18
    • 0028315992 scopus 로고
    • Mechanisms of progressive renal disease in glomerulonephritis
    • Couser, W. G., and Johnson, R. J. (1994). Mechanisms of progressive renal disease in glomerulonephritis. Am. J. Kidney Dis. 23, 193-198.
    • (1994) Am. J. Kidney Dis. , vol.23 , pp. 193-198
    • Couser, W.G.1    Johnson, R.J.2
  • 19
    • 0037085375 scopus 로고    scopus 로고
    • Regulation of the Cool/Pix proteins: key binding partners of the Cdc42/Rac targets, the p21-activated kinases
    • Feng, Q., Albeck, J. G., Cerione, R. A., and Yang, W. (2002). Regulation of the Cool/Pix proteins: key binding partners of the Cdc42/Rac targets, the p21-activated kinases. J. Biol. Chem. 277, 5644-5650.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5644-5650
    • Feng, Q.1    Albeck, J.G.2    Cerione, R.A.3    Yang, W.4
  • 23
  • 24
    • 0033933777 scopus 로고    scopus 로고
    • Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase
    • Hallows, K. R., Raghuram, V., Kemp, B. E., Witters, L. A., and Foskett, J. K. (2000). Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase. J. Clin. Invest. 105, 1711-1721.
    • (2000) J. Clin. Invest. , vol.105 , pp. 1711-1721
    • Hallows, K.R.1    Raghuram, V.2    Kemp, B.E.3    Witters, L.A.4    Foskett, J.K.5
  • 26
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman, S. J., and Ridley, A. J. (2008). Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 9, 690-701.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 27
    • 0037138364 scopus 로고    scopus 로고
    • Signaling to the Rho GTPases: networking with the DH domain
    • Hoffman, G. R., and Cerione, R. A. (2002). Signaling to the Rho GTPases: networking with the DH domain. FEBS Lett. 513, 85-91.
    • (2002) FEBS Lett , vol.513 , pp. 85-91
    • Hoffman, G.R.1    Cerione, R.A.2
  • 28
    • 33646782964 scopus 로고    scopus 로고
    • FOXO factors: a matter of life and death
    • Huang, H., and Tindall, D. J. (2006). FOXO factors: a matter of life and death. Future Oncol. 2, 83-89.
    • (2006) Future Oncol , vol.2 , pp. 83-89
    • Huang, H.1    Tindall, D.J.2
  • 33
    • 0035815617 scopus 로고    scopus 로고
    • Leucine zipper-mediated homodimerization of the p21-activated kinase-interacting factor βPix. Implication for a role in cytoskeletal reorganization
    • Kim, S., Lee, S. H., and Park, D. (2001). Leucine zipper-mediated homodimerization of the p21-activated kinase-interacting factor, βPix. Implication for a role in cytoskeletal reorganization. J. Biol. Chem. 276, 10581-10584.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10581-10584
    • Kim, S.1    Lee, S.H.2    Park, D.3
  • 34
    • 0034747401 scopus 로고    scopus 로고
    • 1PIX, the PAK-interacting exchange factor, requires localization via a coiled-coil region to promote microvillus-like structures and membrane ruffles
    • 1PIX, the PAK-interacting exchange factor, requires localization via a coiled-coil region to promote microvillus-like structures and membrane ruffles. J. Cell Sci. 114, 4239-4251.
    • (2001) J. Cell Sci. , vol.114 , pp. 4239-4251
    • Koh, C.G.1    Manser, E.2    Zhao, Z.S.3    Ng, C.P.4    Lim, L.5
  • 35
    • 78751672175 scopus 로고    scopus 로고
    • Regulation of blood pressure and salt homeostasis by endothelin
    • Kohan, D. E., Rossi, N. F., Inscho, E. W., and Pollock, D. M. (2011a). Regulation of blood pressure and salt homeostasis by endothelin. Physiol Rev. 91,1-77.
    • (2011) Physiol Rev , vol.91 , pp. 1-77
    • Kohan, D.E.1    Rossi, N.F.2    Inscho, E.W.3    Pollock, D.M.4
  • 40
    • 55549087214 scopus 로고    scopus 로고
    • An obligatory het-erodimer of 14-3-3β and 14-3-3ε is required for aldosterone regulation of the epithelial sodium channel
    • Liang, X., Butterworth, M. B., Peters, K. W., Walker, W H., and Frizzell, R. A. (2008). An obligatory het-erodimer of 14-3-3β and 14-3-3ε is required for aldosterone regulation of the epithelial sodium channel. J. Biol. Chem. 283,27418-27425.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27418-27425
    • Liang, X.1    Butterworth, M.B.2    Peters, K.W.3    Walker, W.H.4    Frizzell, R.A.5
  • 41
    • 33745218319 scopus 로고    scopus 로고
    • 14-3-3 Isoforms are induced by aldosterone and participate in its regulation of epithelial sodium channels
    • Liang, X., Peters, K. W, Butterworth, M. B., and Frizzell, R. A. (2006). 14-3-3 Isoforms are induced by aldosterone and participate in its regulation of epithelial sodium channels.J. Biol. Chem. 281, 16323-16332.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16323-16332
    • Liang, X.1    Peters, K.2    Butterworth, W.3    Frizzell, M.B.R.A.4
  • 43
    • 64149085069 scopus 로고    scopus 로고
    • Regulated sodium transport in the renal connecting tubule (CNT) via the epithelial sodium channel (ENaC)
    • Loffing, J., and Korbmacher, C. (2009). Regulated sodium transport in the renal connecting tubule (CNT) via the epithelial sodium channel (ENaC). Pflugers Arch. 458, 111-135.
    • (2009) Pflugers Arch , vol.458 , pp. 111-135
    • Loffing, J.1    Korbmacher, C.2
  • 44
    • 33646763902 scopus 로고    scopus 로고
    • Rho kinases in cardiovascular physiology and pathophysiology
    • Loirand, G., Guerin, P., and Pacaud, P. (2006). Rho kinases in cardiovascular physiology and pathophysiology. Circ. Res. 98, 322-334
    • (2006) Circ. Res , vol.98 , pp. 322-334
    • Loirand, G.1    Guerin, P.2    Pacaud, P.3
  • 45
    • 78049274198 scopus 로고    scopus 로고
    • The role of Rho protein signaling in hypertension
    • Loirand, G., and Pacaud, P. (2010). The role of Rho protein signaling in hypertension. Nat. Rev. Cardiol. 7, 637-647.
    • (2010) Nat. Rev. Cardiol , vol.7 , pp. 637-647
    • Loirand, G.1    Pacaud, P.2
  • 46
  • 47
    • 77949801479 scopus 로고    scopus 로고
    • Mechanisms of proximal tubule sodium transport regulation that link extracellular fluid volume and blood pressure
    • McDonough,A.A. (2010). Mechanisms of proximal tubule sodium transport regulation that link extracellular fluid volume and blood pressure. Am. J. Physiol. Regul. Integr. Comp. Physiol. 298, R851-R861.
    • (2010) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.298
    • McDonough, A.A.1
  • 48
    • 44349127316 scopus 로고    scopus 로고
    • βPIX Rho GTPase guanine nucleotide exchange factor regulates lymphocyte functions and antigen receptor signaling
    • Missy, K., Hu, B., Schilling, K., Haren-berg, A., Sakk, V., Kuchenbecker, K., Kutsche, K., and Fischer, K. D. (2008). βPIX Rho GTPase guanine nucleotide exchange factor regulates lymphocyte functions and antigen receptor signaling. Mol. Cell Biol. 28, 3776-3789.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 3776-3789
    • Missy, K.1    Hu, B.2    Schilling, K.3    Haren-berg, A.4    Sakk, V.5    Kuchenbecker, K.6    Kutsche, K.7    Fischer, K.D.8
  • 52
    • 0035164003 scopus 로고    scopus 로고
    • Segregation of heterotrimeric G proteins in cell surface microdomains. Gq binds caveolin to concentrate in caveolae, whereas Gi and Gs target lipid rafts by default
    • Oh, P., and Schnitzer, J. E. (2001). Segregation of heterotrimeric G proteins in cell surface microdomains. Gq binds caveolin to concentrate in caveolae, whereas Gi and Gs target lipid rafts by default. Mol. Biol. Cell 12, 685-698.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2
  • 53
    • 0031587921 scopus 로고    scopus 로고
    • Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion
    • Oh, W. K., Yoo, J. C., Jo, D., Song, Y. H., Kim, M. G., and Park, D. (1997). Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion. Biochem. Biophys. Res. Commun. 235, 794-798.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 794-798
    • Oh, W.K.1    Yoo, J.C.2    Jo, D.3    Song, Y.H.4    Kim, M.G.5    Park, D.6
  • 57
    • 34347217501 scopus 로고    scopus 로고
    • + channel toward the plasma membrane with total internal reflection fluorescence-fluorescence recovery after photobleaching
    • + channel toward the plasma membrane with total internal reflection fluorescence-fluorescence recovery after photobleaching. J. Biol. Chem. 282, 14576-14585.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14576-14585
    • Pochynyuk, O.1    Staruschenko, A.2    Bugaj, V.3    Lagrange, L.4    Stockand, J.D.5
  • 58
    • 35548947255 scopus 로고    scopus 로고
    • Ion channel regulation by Ras, Rho, and Rab small GTPases
    • Pochynyuk, O., Stockand, J. D., and Star-uschenko, A. (2007b). Ion channel regulation by Ras, Rho, and Rab small GTPases. Exp. Biol. Med. 232, 1258-1265.
    • (2007) Exp. Biol. Med. , vol.232 , pp. 1258-1265
    • Pochynyuk, O.1    Stockand, J.D.2    Star-uschenko, A.3
  • 59
    • 0037439424 scopus 로고    scopus 로고
    • Interaction of αPIX (ARHGEF6) with β-parvin (PARVB) suggests an involvement of αPIX in integrin-mediated signaling
    • Rosenberger, G., Jantke, I., Gal, A., and Kutsche, K. (2003). Interaction of αPIX (ARHGEF6) with β-parvin (PARVB) suggests an involvement of αPIX in integrin-mediated signaling. Hum. Mol. Genet. 12, 155-167.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 155-167
    • Rosenberger, G.1    Jantke, I.2    Gal, A.3    Kutsche, K.4
  • 60
    • 33644959986 scopus 로고    scopus 로고
    • αPIX and βPIX and their role in focal adhesion formation
    • Rosenberger, G., and Kutsche,K. (2006). αPIX and βPIX and their role in focal adhesion formation. Eur. J. Cell Biol. 85, 265-274.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 265-274
    • Rosenberger, G.1    Kutsche, K.2
  • 61
    • 59149097659 scopus 로고    scopus 로고
    • Structures of dimeric GIT1 and trimeric β-PIX and implications for GIT-PIX complex assembly
    • Schlenker, O., and Rittinger, K. (2009). Structures of dimeric GIT1 and trimeric β-PIX and implications for GIT-PIX complex assembly. J. Mol. Biol. 386, 280-289.
    • (2009) J. Mol. Biol. , vol.386 , pp. 280-289
    • Schlenker, O.1    Rittinger, K.2
  • 62
    • 33646877450 scopus 로고    scopus 로고
    • Cbl escapes Cdc42-mediated inhibition by downregulation of the adaptor molecule βPix
    • Schmidt, M. H., Husnjak, K., Szymkiewicz, I., Haglund, K., and Dikic, I. (2006). Cbl escapes Cdc42-mediated inhibition by downregulation of the adaptor molecule βPix. Oncogene 25, 3071-3078.
    • (2006) Oncogene , vol.25 , pp. 3071-3078
    • Schmidt, M.H.1    Husnjak, K.2    Szymkiewicz, I.3    Haglund, K.4    Dikic, I.5
  • 63
    • 0037223146 scopus 로고    scopus 로고
    • Signaling: focus on Rho in renal disease
    • Sharpe, C. C., and Hendry, B. M. (2003). Signaling: focus on Rho in renal disease. J. Am. Soc. Nephrol. 14, 261-264.
    • (2003) J. Am. Soc. Nephrol. , vol.14 , pp. 261-264
    • Sharpe, C.C.1    Hendry, B.M.2
  • 64
    • 84926129790 scopus 로고    scopus 로고
    • Endothelin signaling and actions in the renal mesangium
    • Sorokin, A. (2011). Endothelin signaling and actions in the renal mesangium. Contrib. Nephrol. 172, 50-62.
    • (2011) Contrib. Nephrol. , vol.172 , pp. 50-62
    • Sorokin, A.1
  • 65
    • 0036671215 scopus 로고    scopus 로고
    • Endothelin signalling and regulation of protein kinases in glomerular mesangial cells
    • Sorokin, A., Foschi, M., and Dunn, M. J. (2002). Endothelin signalling and regulation of protein kinases in glomerular mesangial cells. Clin. Sci. 103, 132S-136S.
    • (2002) Clin. Sci. , vol.103
    • Sorokin, A.1    Foschi, M.2    Dunn, M.J.3
  • 66
    • 0141813519 scopus 로고    scopus 로고
    • Physiology and pathology of endothelin-1 in renal mesangium
    • Sorokin, A., and Kohan, D. E. (2003). Physiology and pathology of endothelin-1 in renal mesangium. Am. J. Physiol. Renal Physiol. 285, F579-F589.
    • (2003) Am. J. Physiol. Renal Physiol. , vol.285
    • Sorokin, A.1    Kohan, D.E.2
  • 67
    • 77957258311 scopus 로고    scopus 로고
    • Role of epithelial sodium channels and their regulators in hypertension
    • Soundararajan, R., Pearce, D., Hughey, R. P., and Kleyman, T. R. (2010). Role of epithelial sodium channels and their regulators in hypertension. J. Biol. Chem. 285, 30363-30369.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30363-30369
    • Soundararajan, R.1    Pearce, D.2    Hughey, R.P.3    Kleyman, T.R.4
  • 68
    • 84862170060 scopus 로고    scopus 로고
    • Regulation of transport in the connecting tubule and cortical collecting duct
    • Staruschenko, A. (2012). Regulation of transport in the connecting tubule and cortical collecting duct. Compr. Physiol. 2, 1541-1584.
    • (2012) Compr. Physiol. , vol.2 , pp. 1541-1584
    • Staruschenko, A.1
  • 70
    • 34250353521 scopus 로고    scopus 로고
    • Induction of vascular permeability: βPIX and GIT1 scaffold the activation of extracellular signal-regulated kinase by PAK
    • Stockton, R., Reutershan, J., Scott, D., Sanders, J., Ley, K., and Schwartz, M. A. (2007). Induction of vascular permeability: βPIX and GIT1 scaffold the activation of extracellular signal-regulated kinase by PAK. Mol. Biol. Cell 18, 2346-2355.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2346-2355
    • Stockton, R.1    Reutershan, J.2    Scott, D.3    Sanders, J.4    Ley, K.5    Schwartz, M.A.6
  • 72
    • 79960672932 scopus 로고    scopus 로고
    • Diagnosis and management of urothelial carcinoma of the bladder
    • Tanaka, M. F., and Sonpavde, G. (2011). Diagnosis and management of urothelial carcinoma of the bladder. Postgrad. Med. 123, 43-55.
    • (2011) Postgrad. Med. , vol.123 , pp. 43-55
    • Tanaka, M.F.1    Sonpavde, G.2
  • 73
    • 0031888575 scopus 로고    scopus 로고
    • Cyclin D1, p16, and retinoblastoma gene regulate mitogenic signaling of endothelin in rat mesangial cells
    • Terada, Y., Inoshita, S., Nakashima, O., Yamada, T., Tamamori, M., Ito, H., Sasaki, S., and Marumo, F. (1998). Cyclin D1, p16, and retinoblastoma gene regulate mitogenic signaling of endothelin in rat mesangial cells. Kidney Int. 53, 76-83.
    • (1998) Kidney Int , vol.53 , pp. 76-83
    • Terada, Y.1    Inoshita, S.2    Nakashima, O.3    Yamada, T.4    Tamamori, M.5    Ito, H.6    Sasaki, S.7    Marumo, F.8
  • 74
    • 80055087415 scopus 로고    scopus 로고
    • Defining protein expression in the urothe-lium: a problem of more than transitional interest
    • Yu, W., and Hill, W. G. (2011). Defining protein expression in the urothe-lium: a problem of more than transitional interest. Am. J. Physiol. Renal Physiol. 301, F932-F942.
    • (2011) Am. J. Physiol. Renal Physiol. , vol.301
    • Yu, W.1    Hill, W.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.