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Volumn 307, Issue 12, 2014, Pages F1380-F1389

Akt recruits Dab2 to albumin endocytosis in the proximal tubule

Author keywords

Albumin; Endocytosis; Proximal tubule epithelial cells

Indexed keywords

AKT1 PROTEIN; AKT3 PROTEIN; ALBUMIN; AMINO ACID DERIVATIVE; PLECKSTRIN; PROTEIN KINASE B; PROTEIN KINASE B BETA; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; AKT1 PROTEIN, HUMAN; AKT1 PROTEIN, MOUSE; AKT2 PROTEIN, HUMAN; AKT2 PROTEIN, MOUSE; ALBUMINOID; DAB2 PROTEIN, HUMAN; DAB2 PROTEIN, MOUSE; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TUMOR SUPPRESSOR PROTEIN; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 84918790597     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00454.2014     Document Type: Article
Times cited : (24)

References (50)
  • 1
    • 33750736645 scopus 로고    scopus 로고
    • How does proteinuria cause progressive renal damage?
    • Abbate M, Zoja C, Remuzzi G. How does proteinuria cause progressive renal damage? J Am Soc Nephrol 17: 2974–2984, 2006.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 2974-2984
    • Abbate, M.1    Zoja, C.2    Remuzzi, G.3
  • 2
    • 0030590875 scopus 로고    scopus 로고
    • Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase
    • Alessi DR, Caudwell FB, Andjelkovic M, Hemmings BA, Cohen P. Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase. FEBS Lett 399: 333–338, 1996.
    • (1996) FEBS Lett , vol.399 , pp. 333-338
    • Alessi, D.R.1    Caudwell, F.B.2    Andjelkovic, M.3    Hemmings, B.A.4    Cohen, P.5
  • 6
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins. Getting in on the Akt
    • Brazil DP, Park J, Hemmings BA. PKB binding proteins. Getting in on the Akt. Cell 111: 293–303, 2002.
    • (2002) Cell , vol.111 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 14
    • 0029064922 scopus 로고
    • Renal expression of genes that promote interstitial inflammation and fibrosis in rats with protein-overload proteinuria
    • Eddy AA, Giachelli CM. Renal expression of genes that promote interstitial inflammation and fibrosis in rats with protein-overload proteinuria. Kidney Int 47: 1546–1557, 1995.
    • (1995) Kidney Int , vol.47 , pp. 1546-1557
    • Eddy, A.A.1    Giachelli, C.M.2
  • 15
    • 0025910792 scopus 로고
    • A relationship between proteinuria and acute tubulointerstitial disease in rats with experimental nephrotic syndrome
    • Eddy AA, McCulloch L, Liu E, Adams J. A relationship between proteinuria and acute tubulointerstitial disease in rats with experimental nephrotic syndrome. Am J Pathol 138: 1111–1123, 1991.
    • (1991) Am J Pathol , vol.138 , pp. 1111-1123
    • Eddy, A.A.1    McCulloch, L.2    Liu, E.3    Adams, J.4
  • 16
    • 0034990705 scopus 로고    scopus 로고
    • Albumin overload induces apoptosis in LLC-PK1 cells
    • Erkan E, De Leon M, Devarajan P. Albumin overload induces apoptosis in LLC-PK1 cells. Am J Physiol Renal Physiol 280: F1107–F1114, 2001.
    • (2001) Am J Physiol Renal Physiol , vol.280 , pp. F1107-F1114
    • Erkan, E.1    De Leon, M.2    Devarajan, P.3
  • 17
    • 34047212211 scopus 로고    scopus 로고
    • Mitochondria are the major targets in albumin-induced apoptosis in proximal tubule cells
    • Erkan E, Devarajan P, Schwartz GJ. Mitochondria are the major targets in albumin-induced apoptosis in proximal tubule cells. J Am Soc Nephrol 18: 1199–1208, 2007.
    • (2007) J Am Soc Nephrol , vol.18 , pp. 1199-1208
    • Erkan, E.1    Devarajan, P.2    Schwartz, G.J.3
  • 18
    • 20544433886 scopus 로고    scopus 로고
    • Induction of renal tubular cell apoptosis in focal segmental glomerulosclerosis: Roles of proteinuria and Fas-dependent pathways
    • Erkan E, Garcia CD, Patterson LT, Mishra J, Mitsnefes MM, Kaskel FJ, Devarajan P. Induction of renal tubular cell apoptosis in focal segmental glomerulosclerosis: roles of proteinuria and Fas-dependent pathways. J Am Soc Nephrol 16: 398–407, 2005.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 398-407
    • Erkan, E.1    Garcia, C.D.2    Patterson, L.T.3    Mishra, J.4    Mitsnefes, M.M.5    Kaskel, F.J.6    Devarajan, P.7
  • 20
    • 54949109808 scopus 로고    scopus 로고
    • PI3K/Akt: Getting it right matters
    • Franke TF. PI3K/Akt: getting it right matters. Oncogene 27: 6473–6488, 2008.
    • (2008) Oncogene , vol.27 , pp. 6473-6488
    • Franke, T.F.1
  • 21
    • 0030991386 scopus 로고    scopus 로고
    • High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity
    • Frech M, Andjelkovic M, Ingley E, Reddy KK, Falck JR, Hemmings BA. High affinity binding of inositol phosphates and phosphoinositides to the pleckstrin homology domain of RAC/protein kinase B and their influence on kinase activity. J Biol Chem 272: 8474–8481, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 8474-8481
    • Frech, M.1    Andjelkovic, M.2    Ingley, E.3    Reddy, K.K.4    Falck, J.R.5    Hemmings, B.A.6
  • 23
    • 69249208791 scopus 로고    scopus 로고
    • The Akt kinases: Isoform specificity in metabolism and cancer
    • Gonzalez E, McGraw TE. The Akt kinases: isoform specificity in metabolism and cancer. Cell Cycle 8: 2502–2508, 2009.
    • (2009) Cell Cycle , vol.8 , pp. 2502-2508
    • Gonzalez, E.1    McGraw, T.E.2
  • 25
    • 0033933777 scopus 로고    scopus 로고
    • Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase
    • Hallows KR, Raghuram V, Kemp BE, Witters LA, Foskett JK. 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.
    • (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
    • 79960716001 scopus 로고    scopus 로고
    • Akt signalling in health and disease
    • Hers I, Vincent EE, Tavare JM. Akt signalling in health and disease. Cell Signal 23: 1515–1527, 2011.
    • (2011) Cell Signal , vol.23 , pp. 1515-1527
    • Hers, I.1    Vincent, E.E.2    Tavare, J.M.3
  • 28
    • 84859269830 scopus 로고    scopus 로고
    • The interaction between megalin and ClC-5 is scaffolded by the Na+-H- exchanger regulatory factor 2 (NHERF2) in proximal tubule
    • Hryciw DH, Jenkin KA, Simcocks AC, Grinfeld E, McAinch AJ, Poronnik P. The interaction between megalin and ClC-5 is scaffolded by the Na+-H- exchanger regulatory factor 2 (NHERF2) in proximal tubule. Int J Biochem Cell Biol 44: 815–823, 2012.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 815-823
    • Hryciw, D.H.1    Jenkin, K.A.2    Simcocks, A.C.3    Grinfeld, E.4    McAinch, A.J.5    Poronnik, P.6
  • 31
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
    • James SR, Downes CP, Gigg R, Grove SJ, Holmes AB, Alessi DR. Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation. Biochem J 315: 709–713, 1996.
    • (1996) Biochem J , vol.315 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.4    Holmes, A.B.5    Alessi, D.R.6
  • 32
    • 0037934650 scopus 로고    scopus 로고
    • Insulin signaling through Akt/protein kinase B analyzed by small interfering RNA-mediated gene silencing
    • Jiang ZY, Zhou QL, Coleman KA, Chouinard M, Boese Q, Czech MP. Insulin signaling through Akt/protein kinase B analyzed by small interfering RNA-mediated gene silencing. Proc Natl Acad Sci USA 100: 7569–7574, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7569-7574
    • Jiang, Z.Y.1    Zhou, Q.L.2    Coleman, K.A.3    Chouinard, M.4    Boese, Q.5    Czech, M.P.6
  • 33
    • 33749455320 scopus 로고    scopus 로고
    • A single common portal for clathrin-mediated endocytosis of distinct cargo governed by cargo-selective adaptors
    • Keyel PA, Mishra SK, Roth R, Heuser JE, Watkins SC, Traub LM. A single common portal for clathrin-mediated endocytosis of distinct cargo governed by cargo-selective adaptors. Mol Biol Cell 17: 4300–4317, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 4300-4317
    • Keyel, P.A.1    Mishra, S.K.2    Roth, R.3    Heuser, J.E.4    Watkins, S.C.5    Traub, L.M.6
  • 35
    • 84859750844 scopus 로고    scopus 로고
    • PKB/Akt partners with Dab2 in albumin endocytosis
    • Koral K, Erkan E. PKB/Akt partners with Dab2 in albumin endocytosis. Am J Physiol Renal Physiol 302: F1013–F1024, 2012.
    • (2012) Am J Physiol Renal Physiol , vol.302 , pp. F1013-F1024
    • Koral, K.1    Erkan, E.2
  • 36
    • 77951766263 scopus 로고    scopus 로고
    • New loci associated with kidney function and chronic kidney disease
    • Kottgen A, Pattaro C, Boger CA, et al. New loci associated with kidney function and chronic kidney disease. Nat Genet 42: 376–384, 2010.
    • (2010) Nat Genet , vol.42 , pp. 376-384
    • Kottgen, A.1    Pattaro, C.2    Boger, C.A.3
  • 37
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: Navigating downstream
    • Manning BD, Cantley LC. AKT/PKB signaling: navigating downstream. Cell 129: 1261–1274, 2007.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 38
    • 33749487743 scopus 로고    scopus 로고
    • The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH
    • Maurer ME, Cooper JA. The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH. J Cell Sci 119: 4235–4246, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 4235-4246
    • Maurer, M.E.1    Cooper, J.A.2
  • 42
    • 0037007229 scopus 로고    scopus 로고
    • Dual roles for the Dab2 adaptor protein in embryonic development and kidney transport
    • Morris SM, Tallquist MD, Rock CO, Cooper JA. Dual roles for the Dab2 adaptor protein in embryonic development and kidney transport. EMBO J 21: 1555–1564, 2002.
    • (2002) EMBO J , vol.21 , pp. 1555-1564
    • Morris, S.M.1    Tallquist, M.D.2    Rock, C.O.3    Cooper, J.A.4
  • 45
    • 0037162293 scopus 로고    scopus 로고
    • High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol (3,4,5)-trisphosphate
    • Thomas CC, Deak M, Alessi DR, van Aalten DM. High-resolution structure of the pleckstrin homology domain of protein kinase B/Akt bound to phosphatidylinositol (3,4,5)-trisphosphate. Curr Biol 12: 1256–1262, 2002.
    • (2002) Curr Biol , vol.12 , pp. 1256-1262
    • Thomas, C.C.1    Deak, M.2    Alessi, D.R.3    Van Aalten, D.M.4
  • 46
    • 84918823140 scopus 로고    scopus 로고
    • Mechanisms of glomerular albumin filtration and tubular reabsorption
    • Epub before print
    • Tojo A, Kinugasa S. Mechanisms of glomerular albumin filtration and tubular reabsorption. Int J Nephrol [Epub before print].
    • Int J Nephrol
    • Tojo, A.1    Kinugasa, S.2
  • 48
    • 38549182470 scopus 로고    scopus 로고
    • Protein kinase B: Signalling roles and therapeutic targeting
    • Sale EM, Sale GJ. Protein kinase B: signalling roles and therapeutic targeting. Cell Mol Life Sci 65: 113–127, 2008.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 113-127
    • Sale, E.M.1    Sale, G.J.2
  • 49
    • 44949134110 scopus 로고    scopus 로고
    • Na/H exchange regulatory factor 1, a novel AKT-associating protein, regulates extracellular signal-regulated kinase signaling through a B-Raf mediated pathway
    • Wang B, Yang Y, Friedman PA. Na/H exchange regulatory factor 1, a novel AKT-associating protein, regulates extracellular signal-regulated kinase signaling through a B-Raf mediated pathway. Mol Biol Cell 19: 1637–1645, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 1637-1645
    • Wang, B.1    Yang, Y.2    Friedman, P.A.3
  • 50
    • 18744395794 scopus 로고    scopus 로고
    • Influence of genetic background and gender on hypertension and renal failure in COX-2-deficient mice
    • Yang T, Huang YG, Ye W, Hansen P, Schnermann JB, Briggs JP. Influence of genetic background and gender on hypertension and renal failure in COX-2-deficient mice. Am J Physiol Renal Physiol 288: F1125–F1132, 2005.
    • (2005) Am J Physiol Renal Physiol , vol.288 , pp. F1125-F1132
    • Yang, T.1    Huang, Y.G.2    Ye, W.3    Hansen, P.4    Schnermann, J.B.5    Briggs, J.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.