메뉴 건너뛰기




Volumn 7, Issue 2, 2006, Pages 168-181

The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1

Author keywords

Annexin A2; K2P channels; Retention motif; S100 proteins

Indexed keywords

ADAPTOR PROTEIN; AMINO ACID; CD8 ANTIGEN; CELL PROTEIN; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; GLUTATHIONE TRANSFERASE; POTASSIUM CHANNEL; SMALL INTERFERING RNA; HYBRID PROTEIN; LIPOCORTIN 2; PROTEIN 14 3 3; PROTEIN S 100; S100 CALCIUM BINDING PROTEIN A10; TANDEM PORE DOMAIN POTASSIUM CHANNEL; TASK PROTEIN, RAT;

EID: 33645115319     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2005.00375.x     Document Type: Article
Times cited : (88)

References (56)
  • 1
    • 0035478067 scopus 로고    scopus 로고
    • CNS distribution of members of the two-pore-domain (KCNK) potassium channel family
    • Talley EM, Solorzano G, Lei Q, Kim D, Bayliss DA. CNS distribution of members of the two-pore-domain (KCNK) potassium channel family. J Neurosci 2001; 21: 7491-7505.
    • (2001) J Neurosci , vol.21 , pp. 7491-7505
    • Talley, E.M.1    Solorzano, G.2    Lei, Q.3    Kim, D.4    Bayliss, D.A.5
  • 3
    • 0037310538 scopus 로고    scopus 로고
    • Two-pore-Domain (KCNK) potassium channels: Dynamic roles in neuronal function
    • Talley EM, Sirois JE, Lei Q, Bayliss DA. Two-pore-Domain (KCNK) potassium channels: Dynamic roles in neuronal function. Neuroscientist 2003; 9: 46-56.
    • (2003) Neuroscientist , vol.9 , pp. 46-56
    • Talley, E.M.1    Sirois, J.E.2    Lei, Q.3    Bayliss, D.A.4
  • 4
    • 0033679959 scopus 로고    scopus 로고
    • Molecular and functional properties of two-pore-domain potassium channels
    • Lesage F, Lazdunski M. Molecular and functional properties of two-pore-domain potassium channels. Am J Physiol Renal Physiol 2000; 279: F793-F801.
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Lesage, F.1    Lazdunski, M.2
  • 6
    • 2542591643 scopus 로고    scopus 로고
    • Functional evidence of a role for two-pore domain potassium channels in rat mesenteric and pulmonary arteries
    • Gardener MJ, Johnson IT, Burnham MP, Edwards G, Heagerty AM, Weston AH. Functional evidence of a role for two-pore domain potassium channels in rat mesenteric and pulmonary arteries. Br J Pharmacol 2004; 142: 192-202.
    • (2004) Br J Pharmacol , vol.142 , pp. 192-202
    • Gardener, M.J.1    Johnson, I.T.2    Burnham, M.P.3    Edwards, G.4    Heagerty, A.M.5    Weston, A.H.6
  • 7
    • 8544257338 scopus 로고    scopus 로고
    • + channels couple angiotensin II receptors to membrane depolarization and aldosterone secretion in bovine adrenal glomerulosa cells
    • + channels couple angiotensin II receptors to membrane depolarization and aldosterone secretion in bovine adrenal glomerulosa cells. Am J Physiol Endocrinol Metab 2004; 287: E1154-E1165.
    • (2004) Am J Physiol Endocrinol Metab , vol.287
    • Enyeart, J.A.1    Danthi, S.J.2    Enyeart, J.J.3
  • 8
    • 12944294332 scopus 로고    scopus 로고
    • Molecular diversity and regulation of renal potassium channels
    • Hebert SC, Desir G, Giebisch G, Wang W. Molecular diversity and regulation of renal potassium channels. Physiol Rev 2005; 85: 319-371.
    • (2005) Physiol Rev , vol.85 , pp. 319-371
    • Hebert, S.C.1    Desir, G.2    Giebisch, G.3    Wang, W.4
  • 11
    • 0034737472 scopus 로고    scopus 로고
    • TASK-3, a new member of the tandem pore K(+) channel family
    • Kim Y, Bang H, Kim D. TASK-3, a new member of the tandem pore K(+) channel family. J Biol Chem 2000; 275: 9340-9347.
    • (2000) J Biol Chem , vol.275 , pp. 9340-9347
    • Kim, Y.1    Bang, H.2    Kim, D.3
  • 17
    • 0037144152 scopus 로고    scopus 로고
    • TASK-1, TASK-2, TASK-3 and TRAAK immunoreactivities in the rat carotid body
    • Yamamoto Y, Kummer W, Atoji Y, Suzuki Y. TASK-1, TASK-2, TASK-3 and TRAAK immunoreactivities in the rat carotid body. Brain Res 2002; 950: 304-307.
    • (2002) Brain Res , vol.950 , pp. 304-307
    • Yamamoto, Y.1    Kummer, W.2    Atoji, Y.3    Suzuki, Y.4
  • 19
    • 0033757904 scopus 로고    scopus 로고
    • + channel, is modulated by multiple neurotransmitters in motoneurons
    • + channel, is modulated by multiple neurotransmitters in motoneurons. Neuron 2000; 25: 399-410.
    • (2000) Neuron , vol.25 , pp. 399-410
    • Talley, E.M.1    Lei, Q.2    Sirois, J.E.3    Bayliss, D.A.4
  • 22
    • 0036188942 scopus 로고    scopus 로고
    • TASK-3 dominates the background potassium conductance in rat adrenal glomerulosa cells
    • Czirjak G, Enyedi P. TASK-3 dominates the background potassium conductance in rat adrenal glomerulosa cells. Mol Endocrinol 2002; 16: 621-629.
    • (2002) Mol Endocrinol , vol.16 , pp. 621-629
    • Czirjak, G.1    Enyedi, P.2
  • 24
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • O'Kelly I, Butler MH, Zilberberg N, Goldstein SA. Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 2002; 111: 577-588.
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 26
    • 4444246475 scopus 로고    scopus 로고
    • Determinants of voltage-gated potassium channel surface expression and localization in Mammalian neurons
    • Misonou H, Trimmer JS. Determinants of voltage-gated potassium channel surface expression and localization in Mammalian neurons. Crit Rev Biochem Mol Biol 2004; 39: 125-145.
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 125-145
    • Misonou, H.1    Trimmer, J.S.2
  • 28
    • 4644330118 scopus 로고    scopus 로고
    • S100 proteins and their influence on pro-survival pathways in cancer
    • Emberley ED, Murphy LC, Watson PH. S100 proteins and their influence on pro-survival pathways in cancer. Biochem Cell Biol 2004; 82: 508-515.
    • (2004) Biochem Cell Biol , vol.82 , pp. 508-515
    • Emberley, E.D.1    Murphy, L.C.2    Watson, P.H.3
  • 29
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke V, Moss SE. Annexins: From structure to function. Physiol Rev 2002; 82: 331-371.
    • (2002) Physiol Rev , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 30
    • 0030814032 scopus 로고    scopus 로고
    • P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2
    • Wu T, Angus CW, Yao XL, Logun C, Shelhamer JH. P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2. J Biol Chem 1997; 272: 17145-17153.
    • (1997) J Biol Chem , vol.272 , pp. 17145-17153
    • Wu, T.1    Angus, C.W.2    Yao, X.L.3    Logun, C.4    Shelhamer, J.H.5
  • 31
    • 2142721829 scopus 로고    scopus 로고
    • Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11
    • Hsu SY, Kaipia A, Zhu L, Hsueh AJ. Interference of BAD (Bcl-xL/ Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. Mol Endocrinol 1997; 11: 1858-1867.
    • (1997) Mol Endocrinol , vol.11 , pp. 1858-1867
    • Hsu, S.Y.1    Kaipia, A.2    Zhu, L.3    Hsueh, A.J.4
  • 32
  • 34
    • 0025784422 scopus 로고
    • Primary structure of human, chicken, and Xenopus laevis p11, a cellular ligand of the Src-kinase substrate, annexin II
    • Kube E, Weber K, Gerke V. Primary structure of human, chicken, and Xenopus laevis p11, a cellular ligand of the Src-kinase substrate, annexin II. Gene 1991; 102: 255-259.
    • (1991) Gene , vol.102 , pp. 255-259
    • Kube, E.1    Weber, K.2    Gerke, V.3
  • 35
    • 0025989485 scopus 로고
    • Primary structure and expression of the Xenopus laevis gene encoding annexin II
    • Gerke V, Koch W, Thiel C. Primary structure and expression of the Xenopus laevis gene encoding annexin II. Gene 1991; 104: 259-264.
    • (1991) Gene , vol.104 , pp. 259-264
    • Gerke, V.1    Koch, W.2    Thiel, C.3
  • 36
    • 0026075259 scopus 로고
    • Xenopus annexin II (calpactin I) heavy chain has a distinct amino terminus
    • Izant JG, Bryson LJ. Xenopus annexin II (calpactin I) heavy chain has a distinct amino terminus. J Biol Chem 1991; 266: 18560-18566.
    • (1991) J Biol Chem , vol.266 , pp. 18560-18566
    • Izant, J.G.1    Bryson, L.J.2
  • 37
    • 0027162018 scopus 로고
    • Involvement of annexin II in DNA replication: Evidence from cell-free extracts of Xenopus eggs
    • Vishwanatha JK, Kumble S. Involvement of annexin II in DNA replication: evidence from cell-free extracts of Xenopus eggs. J Cell Sci 1993; 105 (Pt 2): 533-540.
    • (1993) J Cell Sci , vol.105 , Issue.PART 2 , pp. 533-540
    • Vishwanatha, J.K.1    Kumble, S.2
  • 38
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA (B) receptor heterodimerization
    • Margeta-Mitrovic M, Jan YN, Jan LY. A trafficking checkpoint controls GABA (B) receptor heterodimerization. Neuron 2000; 27: 97-106.
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 40
    • 0030859482 scopus 로고    scopus 로고
    • Delta and kappa opioid receptors are differentially regulated by dynamin-dependent endocytosis when activated by the same alkaloid agonist
    • Chu P, Murray S, Lissin D, von Zastrow M. Delta and kappa opioid receptors are differentially regulated by dynamin-dependent endocytosis when activated by the same alkaloid agonist. J Biol Chem 1997; 272: 27124-27130.
    • (1997) J Biol Chem , vol.272 , pp. 27124-27130
    • Chu, P.1    Murray, S.2    Lissin, D.3    von Zastrow, M.4
  • 42
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson MR, Nilsson T, Peterson PA. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J 1990; 9: 3153-3162.
    • (1990) EMBO J , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 43
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman I, Warren G. The road taken: Past and future foundations of membrane traffic. Cell 2000; 100: 99-112.
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 44
    • 0036293722 scopus 로고    scopus 로고
    • Lysine can be replaced by histidine but not by arginine as the ER retrieval motif for type I membrane proteins
    • Hardt B, Bause E. Lysine can be replaced by histidine but not by arginine as the ER retrieval motif for type I membrane proteins. Biochem Biophys Res Commun 2002; 291: 751-757.
    • (2002) Biochem Biophys Res Commun , vol.291 , pp. 751-757
    • Hardt, B.1    Bause, E.2
  • 45
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca+ signalling to membrane dynamics
    • Gerke V, Creutz CE, Moss SE. Annexins: Linking Ca+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 2005; 6: 449-461.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 46
    • 0036789972 scopus 로고    scopus 로고
    • The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release
    • Beaton AR, Rodriguez J, Reddy YK, Roy P. The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release. Proc Natl Acad Sci USA 2002; 99: 13154-13159.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13154-13159
    • Beaton, A.R.1    Rodriguez, J.2    Reddy, Y.K.3    Roy, P.4
  • 49
    • 0035908953 scopus 로고    scopus 로고
    • Apical membrane proteins are transported in distinct vesicular carriers
    • Jacob R, Naim HY. Apical membrane proteins are transported in distinct vesicular carriers. Curr Biol 2001; 11: 1444-1450.
    • (2001) Curr Biol , vol.11 , pp. 1444-1450
    • Jacob, R.1    Naim, H.Y.2
  • 50
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection
    • Albritton LM, Tseng L, Scadden D, Cunningham JM. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection. Cell 1989; 57: 659-666.
    • (1989) Cell , vol.57 , pp. 659-666
    • Albritton, L.M.1    Tseng, L.2    Scadden, D.3    Cunningham, J.M.4
  • 51
    • 0030802747 scopus 로고    scopus 로고
    • In vitro binding of purified murine ecotropic retrovirus envelope surface protein to its receptor, MCAT-1
    • Davey RA, Hamson CA, Healey JJ, Cunningham JM. In vitro binding of purified murine ecotropic retrovirus envelope surface protein to its receptor, MCAT-1. J Virol 1997; 71: 8096-8102.
    • (1997) J Virol , vol.71 , pp. 8096-8102
    • Davey, R.A.1    Hamson, C.A.2    Healey, J.J.3    Cunningham, J.M.4
  • 52
    • 0034608802 scopus 로고    scopus 로고
    • Exploring the sequence space for tetracycline-dependent transcriptional activators: Novel mutations yield expanded range and sensitivity
    • Urlinger S, Baron U, Thellmann M, Hasan MT, Bujard H, Hillen W. Exploring the sequence space for tetracycline-dependent transcriptional activators: Novel mutations yield expanded range and sensitivity. Proc Natl Acad Sci U S A 2000; 97: 7963-7968.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7963-7968
    • Urlinger, S.1    Baron, U.2    Thellmann, M.3    Hasan, M.T.4    Bujard, H.5    Hillen, W.6
  • 54
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • Zerangue N, Schwappach B, Jan YN, Jan LY. A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron 1999; 22: 537-548.
    • (1999) Neuron , vol.22 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4
  • 55
    • 0344012479 scopus 로고    scopus 로고
    • The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes
    • Zobiack N, Rescher U, Ludwig C, Zeuschner D, Gerke V. The annexin 2/ S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes. Mol Biol Cell 2003; 14: 4896-4908.
    • (2003) Mol Biol Cell , vol.14 , pp. 4896-4908
    • Zobiack, N.1    Rescher, U.2    Ludwig, C.3    Zeuschner, D.4    Gerke, V.5
  • 56
    • 0023897690 scopus 로고
    • The submembranous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ
    • Osborn M, Johnsson N, Wehland J, Weber K. The submembranous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ. Exp Cell Res 1988; 175: 81-96.
    • (1988) Exp Cell Res , vol.175 , pp. 81-96
    • Osborn, M.1    Johnsson, N.2    Wehland, J.3    Weber, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.