메뉴 건너뛰기




Volumn 305, Issue 12, 2013, Pages

Activation of the cAMP/PKA pathway induces UT-A1 urea transporter monoubiquitination and targets it for lysosomal degradation

Author keywords

Endocy tosis; Membrane protein; Phosphorylation; Trafficking; Vasopressin

Indexed keywords

CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; FORSKOLIN; PROTEIN; UNCLASSIFIED DRUG; UREA TRANSPORTER A1 PROTEIN; VASOPRESSIN;

EID: 84890349504     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00393.2013     Document Type: Article
Times cited : (12)

References (37)
  • 2
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal R, Deveraux Q, Xia G, Rechsteiner M, Pickart C. Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc Natl Acad Sci USA 93: 861-866, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3    Rechsteiner, M.4    Pickart, C.5
  • 3
    • 49949101889 scopus 로고    scopus 로고
    • Phosphorylation of UT-A1 urea transporter at serines 486 and 499 is important for vasopressin-regulated activity and membrane accumulation
    • Blount MA, Mistry AC, Fröhlich O, Price SR, Chen G, Sands JM, Klein JD. Phosphorylation of UT-A1 urea transporter at serines 486 and 499 is important for vasopressin-regulated activity and membrane accumulation. Am J Physiol Renal Physiol 295: F295-F299, 2008.
    • (2008) Am J Physiol Renal Physiol , vol.295
    • Blount, M.A.1    Mistry, A.C.2    Fröhlich, O.3    Price, S.R.4    Chen, G.5    Sands, J.M.6    Klein, J.D.7
  • 4
    • 38049177658 scopus 로고    scopus 로고
    • The deubiquitinating enzyme UCH-L3 regulates the apical membrane recycling of the epithelial sodium channel
    • Butterworth MB, Edinger RS, Ovaa H, Burg D, Johnson JP, Frizzell RA. The deubiquitinating enzyme UCH-L3 regulates the apical membrane recycling of the epithelial sodium channel. J Biol Chem 282, 37885-37893, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 37885-37893
    • Butterworth, M.B.1    Edinger, R.S.2    Ovaa, H.3    Burg, D.4    Johnson, J.P.5    Frizzell, R.A.6
  • 5
    • 33748749047 scopus 로고    scopus 로고
    • Loss of N-linked glycosylation reduces urea transporter UT-A1 response to vasopressin
    • Chen G, Fröhlich O, Yang Y, Klein JD, Sands JM. Loss of N-linked glycosylation reduces urea transporter UT-A1 response to vasopressin. J Biol Chem 281: 27436-27442, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 27436-27442
    • Chen, G.1    Fröhlich, O.2    Yang, Y.3    Klein, J.D.4    Sands, J.M.5
  • 6
    • 82655181502 scopus 로고    scopus 로고
    • Mature N-linked glycans facilitate UT-A1 urea transporter lipid raft compartmen-talization
    • Chen G, Howe AG, Xu G, Fröhlich O, Klein JD, Sands JM. Mature N-linked glycans facilitate UT-A1 urea transporter lipid raft compartmen-talization. FASEB J 25: 4531-4539, 2011.
    • (2011) FASEB J , vol.25 , pp. 4531-4539
    • Chen, G.1    Howe, A.G.2    Xu, G.3    Fröhlich, O.4    Klein, J.D.5    Sands, J.M.6
  • 9
    • 84855979997 scopus 로고    scopus 로고
    • The role of EGF receptor ubiquitination in regulating its intracellular traffic
    • Eden ER, Huang F, Sorkin A, Futter CE. The role of EGF receptor ubiquitination in regulating its intracellular traffic. Traffic 13: 329-337, 2012.
    • (2012) Traffic , vol.13 , pp. 329-337
    • Eden, E.R.1    Huang, F.2    Sorkin, A.3    Futter, C.E.4
  • 10
    • 77956234556 scopus 로고    scopus 로고
    • Postendocytic sorting of constitutively internalized dopamine transporter in cell lines and dopaminergic neurons
    • Eriksen J, Bjørn-Yoshimoto WE, Jørgensen TN, Newman AH, Gether U. Postendocytic sorting of constitutively internalized dopamine transporter in cell lines and dopaminergic neurons. J Biol Chem 285: 27289-27301, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 27289-27301
    • Eriksen, J.1    Bjørn-Yoshimoto, W.E.2    Jørgensen, T.N.3    Newman, A.H.4    Gether, U.5
  • 11
    • 2442555092 scopus 로고    scopus 로고
    • Urinary concentrating defect in mice with selective deletion of phloretin-sensitive urea transporters in the renal collecting duct
    • Fenton RA, Chou CL, Stewart GS, Smith CP, Knepper MA. Urinary concentrating defect in mice with selective deletion of phloretin-sensitive urea transporters in the renal collecting duct. Proc Natl Acad Sci USA 101: 7469-7474, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7469-7474
    • Fenton, R.A.1    Chou, C.L.2    Stewart, G.S.3    Smith, C.P.4    Knepper, M.A.5
  • 13
    • 0028070372 scopus 로고
    • Production and characterisation of monoclonal antibodies specific to multiubiquitin chains of polyubiq-uitinated proteins
    • Fujimuro M, Sawada H, Yokosawa H. Production and characterisation of monoclonal antibodies specific to multiubiquitin chains of polyubiq-uitinated proteins. FEBS Lett 349: 173-180, 1994.
    • (1994) FEBS Lett , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 14
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82: 373-428, 2002.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 18
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke L. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol 9: 107-112, 1999.
    • (1999) Trends Cell Biol , vol.9 , pp. 107-112
    • Hicke, L.1
  • 19
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L, Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19: 141-172, 2003.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 20
    • 78649924903 scopus 로고    scopus 로고
    • Internalization of UT-A1 urea transporter is dynamin dependent and mediated by both caveolae- and clathrin-coated pit pathways
    • Huang H, Feng X, Zhuang J, Fröhlich O, Klein JD, Cai H, Sands JM, Chen G. Internalization of UT-A1 urea transporter is dynamin dependent and mediated by both caveolae- and clathrin-coated pit pathways. Am J Physiol Renal Physiol 299: F1389-F1395, 2010.
    • (2010) Am J Physiol Renal Physiol , vol.299
    • Huang, H.1    Feng, X.2    Zhuang, J.3    Fröhlich, O.4    Klein, J.D.5    Cai, H.6    Sands, J.M.7    Chen, G.8
  • 21
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D. The emerging complexity of protein ubiquitination. Biochem Soc Trans 37: 937-953, 2009.
    • (2009) Biochem Soc Trans , vol.37 , pp. 937-953
    • Komander, D.1
  • 22
    • 84890346397 scopus 로고    scopus 로고
    • Ubiquitin ligase adaptors: Regulators of ubiquitylation and endocytosis of plasma membrane proteins
    • Leon S, Haguenauer-Tsapis R. Ubiquitin ligase adaptors: regulators of ubiquitylation and endocytosis of plasma membrane proteins. Exp Cell
    • Exp Cell
    • Leon, S.1    Haguenauer-Tsapis, R.2
  • 23
    • 33744792036 scopus 로고    scopus 로고
    • Regulation of epithelial sodium channels by the ubiquitin-proteasome proteolytic pathway
    • Malik B, Price SR, Mitch WE, Yue Q, Eaton DC. Regulation of epithelial sodium channels by the ubiquitin-proteasome proteolytic pathway. Am J Physiol Renal Physiol 290: F1285-F1294, 2006.
    • (2006) Am J Physiol Renal Physiol , vol.290
    • Malik, B.1    Price, S.R.2    Mitch, W.E.3    Yue, Q.4    Eaton, D.C.5
  • 24
    • 45549109608 scopus 로고    scopus 로고
    • Volume expansion stimulates monoubiquitination and endocytosis of surface-expressed skate anion-exchanger isoform
    • Musch MW, Puffer AB, Goldstein L. Volume expansion stimulates monoubiquitination and endocytosis of surface-expressed skate anion-exchanger isoform. Am J Physiol Regul Integr Comp Physiol 294: R1657-R1665, 2008.
    • (2008) Am J Physiol Regul Integr Comp Physiol , vol.294
    • Musch, M.W.1    Puffer, A.B.2    Goldstein, L.3
  • 26
    • 80755132190 scopus 로고    scopus 로고
    • Endosomal transport via ubiquitination
    • Pickart CM, Fushman D. Endosomal transport via ubiquitination. Trends Cell Biol 21: 647-655, 2011.
    • (2011) Trends Cell Biol , vol.21 , pp. 647-655
    • Pickart, C.M.1    Fushman, D.2
  • 27
    • 0041427914 scopus 로고    scopus 로고
    • Molecular mechanisms of urea transport
    • Sands JM. Molecular mechanisms of urea transport. J Membr Biol 191: 149-163, 2003.
    • (2003) J Membr Biol , vol.191 , pp. 149-163
    • Sands, J.M.1
  • 28
    • 52749083023 scopus 로고    scopus 로고
    • Ubiquitination regulates the plasma membrane expression of renal UT-A urea transporters
    • Stewart GS, O'Brien JH, Smith CP. Ubiquitination regulates the plasma membrane expression of renal UT-A urea transporters. Am J Physiol Cell Physiol 295: C121-C129, 2008.
    • (2008) Am J Physiol Cell Physiol , vol.295
    • Stewart, G.S.1    O'Brien, J.H.2    Smith, C.P.3
  • 29
    • 84868361307 scopus 로고    scopus 로고
    • Forskolin stimulation promotes urea transporter UT-A1 ubiquitination, endocytosis, and degradation
    • Su H, Carter BC, Laur O, Sands JM, Chen G. Forskolin stimulation promotes urea transporter UT-A1 ubiquitination, endocytosis, and degradation. Am J Physiol Renal Physiol 303: F1325-F1332, 2012.
    • (2012) Am J Physiol Renal Physiol , vol.303
    • Su, H.1    Carter, B.C.2    Laur, O.3    Sands, J.M.4    Chen, G.5
  • 31
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell J, Shih S, Dunn R, Hicke L. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol Cell 1: 193-202, 1998.
    • (1998) Mol Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 35
    • 77956238947 scopus 로고    scopus 로고
    • c-Cbl facilitates endocytosis and lysosomal degradation of cystic fibrosis transmembrane conductance regulator in human airway epithelial cells
    • Ye S, Cihil K, Stolz DB, Pilewski JM, Stanton BA, Swiatecka-Urban A. c-Cbl facilitates endocytosis and lysosomal degradation of cystic fibrosis transmembrane conductance regulator in human airway epithelial cells. J Biol Chem 285: 27008-27018, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 27008-27018
    • Ye, S.1    Cihil, K.2    Stolz, D.B.3    Pilewski, J.M.4    Stanton, B.A.5    Swiatecka-Urban, A.6
  • 36
    • 0036079910 scopus 로고    scopus 로고
    • Vasopressin rapidly increases phosphorylation of UT-A1 urea transporter in rat IMCDs through PKA
    • Zhang C, Sands JM, Klein JD. Vasopressin rapidly increases phosphorylation of UT-A1 urea transporter in rat IMCDs through PKA. Am J Physiol Renal Physiol 282: F85-F90, 2002.
    • (2002) Am J Physiol Renal Physiol , vol.282
    • Zhang, C.1    Sands, J.M.2    Klein, J.D.3
  • 37
    • 84871545704 scopus 로고    scopus 로고
    • Lysine 48-linked polyubiquitination of organic anion transporter-1 is essential for its protein kinase C-regulated endocytosis
    • Zhang Q, Li S, Patterson C, You G. Lysine 48-linked polyubiquitination of organic anion transporter-1 is essential for its protein kinase C-regulated endocytosis. Mol Pharmacol 83: 217-224, 2013.
    • (2013) Mol Pharmacol , vol.83 , pp. 217-224
    • Zhang, Q.1    Li, S.2    Patterson, C.3    You, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.