메뉴 건너뛰기




Volumn 293, Issue 1, 2007, Pages

Loss of calcineurin homologous protein-1 in chicken B lymphoma DT40 cells destabilizes Na+/H+ exchanger isoform-1 protein

Author keywords

Antiporter; Degradation; Membrane protein; Quality control; Transporter

Indexed keywords

CALCINEURIN HOMOLOGOUS PROTEIN 1; CALCIUM ION; CELL PROTEIN; ISOPROTEIN; MESSENGER RNA; PROTON; SODIUM ION; SODIUM PROTON EXCHANGE PROTEIN; SODIUM PROTON EXCHANGE PROTEIN 1; UNCLASSIFIED DRUG;

EID: 34547129817     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00464.2006     Document Type: Article
Times cited : (27)

References (50)
  • 1
    • 10644272564 scopus 로고    scopus 로고
    • Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules
    • Andrade J, Pearce ST, Zhao H, Barroso M. Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules. Biochem J 384: 327-336, 2004.
    • (2004) Biochem J , vol.384 , pp. 327-336
    • Andrade, J.1    Pearce, S.T.2    Zhao, H.3    Barroso, M.4
  • 3
    • 0021972902 scopus 로고
    • Cell lines derived from avian lymphomas exhibit two distinct phenotypes
    • Baba TW, Giroir BP, Humphries EH. Cell lines derived from avian lymphomas exhibit two distinct phenotypes. Virology 144: 139-151, 1985.
    • (1985) Virology , vol.144 , pp. 139-151
    • Baba, T.W.1    Giroir, B.P.2    Humphries, E.H.3
  • 6
    • 0033638350 scopus 로고    scopus 로고
    • The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae
    • Bowers K, Levi BP, Patel FI, Stevens TH. The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae. Mol Biol Cell 11: 4277-4294, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 4277-4294
    • Bowers, K.1    Levi, B.P.2    Patel, F.I.3    Stevens, T.H.4
  • 7
    • 0040735606 scopus 로고    scopus 로고
    • The expanding family of eucaryotic Na(+)/H(+) exchangers
    • Counillon L, Pouyssegur J. The expanding family of eucaryotic Na(+)/H(+) exchangers. J Biol Chem 275: 1-4, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 1-4
    • Counillon, L.1    Pouyssegur, J.2
  • 8
    • 0027931588 scopus 로고
    • + exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain
    • + exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain. Biochemistry 33: 10463-10469, 1994.
    • (1994) Biochemistry , vol.33 , pp. 10463-10469
    • Counillon, L.1    Pouyssegur, J.2    Reithmeier, R.A.3
  • 9
    • 0029905493 scopus 로고    scopus 로고
    • Intracellular pH regulation during spreading of human neutrophils
    • Demaurex N, Downey GP, Waddell TK, Grinstein S. Intracellular pH regulation during spreading of human neutrophils. J Cell Biol 133: 1391-1402, 1996.
    • (1996) J Cell Biol , vol.133 , pp. 1391-1402
    • Demaurex, N.1    Downey, G.P.2    Waddell, T.K.3    Grinstein, S.4
  • 10
    • 0028535169 scopus 로고
    • + antiport: Modulation by ATP and role in cell volume regulation
    • + antiport: modulation by ATP and role in cell volume regulation. J Exp Biol 196: 389-404, 1994.
    • (1994) J Exp Biol , vol.196 , pp. 389-404
    • Demaurex, N.1    Grinstein, S.2
  • 11
    • 0034503095 scopus 로고    scopus 로고
    • Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation
    • Denker SP, Huang DC, Orlowski J, Furthmayr H, Barber DL. Direct binding of the Na-H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation. Mol Cell 6: 1425-1436, 2000.
    • (2000) Mol Cell , vol.6 , pp. 1425-1436
    • Denker, S.P.1    Huang, D.C.2    Orlowski, J.3    Furthmayr, H.4    Barber, D.L.5
  • 12
    • 33644893341 scopus 로고    scopus 로고
    • Heterologous expression of mammalian Na/H antiporters in Saccharomyces cerevisiae
    • Flegelova H, Haguenauer-Tsapis R, Sychrova H. Heterologous expression of mammalian Na/H antiporters in Saccharomyces cerevisiae. Biochim Biophys Acta 1760: 504-516, 2006.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 504-516
    • Flegelova, H.1    Haguenauer-Tsapis, R.2    Sychrova, H.3
  • 14
    • 0020775644 scopus 로고
    • Intracellular pH plays a role in regulating protein synthesis in Xenopus oocytes
    • Houle JG, Wasserman WJ. Intracellular pH plays a role in regulating protein synthesis in Xenopus oocytes. Dev Biol 97: 302-312, 1983.
    • (1983) Dev Biol , vol.97 , pp. 302-312
    • Houle, J.G.1    Wasserman, W.J.2
  • 16
    • 0017118955 scopus 로고
    • Intracellular pH and activation of sea urchin eggs after fertilisation
    • Johnson JD, Epel D. Intracellular pH and activation of sea urchin eggs after fertilisation. Nature 262: 661-664, 1976.
    • (1976) Nature , vol.262 , pp. 661-664
    • Johnson, J.D.1    Epel, D.2
  • 17
    • 0018096851 scopus 로고
    • Establishment and characterization of a cell line from the American opossum (Didelphys virginiana)
    • Koyama H, Goodpasture C, Miller MM, Teplitz RL, Riggs AD. Establishment and characterization of a cell line from the American opossum (Didelphys virginiana). In Vitro 14: 239-246, 1978.
    • (1978) In Vitro , vol.14 , pp. 239-246
    • Koyama, H.1    Goodpasture, C.2    Miller, M.M.3    Teplitz, R.L.4    Riggs, A.D.5
  • 18
    • 0141591541 scopus 로고    scopus 로고
    • The apoptosis-inducing protein kinase DRAK2 is inhibited in a calcium-dependent manner by the calcium-binding protein CHP
    • Kuwahara H, Kamei J, Nakamura N, Matsumoto M, Inoue H, Kanazawa H. The apoptosis-inducing protein kinase DRAK2 is inhibited in a calcium-dependent manner by the calcium-binding protein CHP. J Biochem (Tokyo) 134: 245-250, 2003.
    • (2003) J Biochem (Tokyo) , vol.134 , pp. 245-250
    • Kuwahara, H.1    Kamei, J.2    Nakamura, N.3    Matsumoto, M.4    Inoue, H.5    Kanazawa, H.6
  • 19
    • 0029981094 scopus 로고    scopus 로고
    • A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange
    • Lin X, Barber DL. A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange. Proc Natl Acad Sci USA 93: 12631-12636, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12631-12636
    • Lin, X.1    Barber, D.L.2
  • 20
    • 0033579413 scopus 로고    scopus 로고
    • Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein
    • Lin X, Sikkink RA, Rusnak F, Barber DL. Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein. J Biol Chem 274: 36125-36131, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 36125-36131
    • Lin, X.1    Sikkink, R.A.2    Rusnak, F.3    Barber, D.L.4
  • 22
    • 1642327748 scopus 로고    scopus 로고
    • A novel kinesin-like protein, KIF1Bbeta3 is involved in the movement of lysosomes to the cell periphery in non-neuronal cells
    • Matsushita M, Tanaka S, Nakamura N, Inoue H, Kanazawa H. A novel kinesin-like protein, KIF1Bbeta3 is involved in the movement of lysosomes to the cell periphery in non-neuronal cells. Traffic 5: 140-151, 2004.
    • (2004) Traffic , vol.5 , pp. 140-151
    • Matsushita, M.1    Tanaka, S.2    Nakamura, N.3    Inoue, H.4    Kanazawa, H.5
  • 25
    • 12544258841 scopus 로고    scopus 로고
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation
    • + exchanger isoforms are distributed to Golgi and post-Golgi compartments and are involved in organelle pH regulation. J Biol Chem 280: 1561-1572, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 1561-1572
    • Nakamura, N.1    Tanaka, S.2    Teko, Y.3    Mitsui, K.4    Kanazawa, H.5
  • 28
    • 0035907355 scopus 로고    scopus 로고
    • + exchanger localized to the trans-Golgi network
    • + exchanger localized to the trans-Golgi network. J Biol Chem 276: 17387-17394, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 17387-17394
    • Numata, M.1    Orlowski, J.2
  • 30
    • 0027282066 scopus 로고
    • Heterologous expression and functional properties of amiloride high affinity (NHE-1) and low affinity (NHE-3) isoforms of the rat Na/H exchanger
    • Orlowski J. Heterologous expression and functional properties of amiloride high affinity (NHE-1) and low affinity (NHE-3) isoforms of the rat Na/H exchanger. J Biol Chem 268: 16369-16377, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 16369-16377
    • Orlowski, J.1
  • 31
    • 1242272754 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • Orlowski J, Grinstein S. Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflügers Arch 447: 549-565, 2004.
    • (2004) Pflügers Arch , vol.447 , pp. 549-565
    • Orlowski, J.1    Grinstein, S.2
  • 32
    • 0026806528 scopus 로고
    • Molecular cloning of putative members of the Na/H exchanger gene family. cDNA cloning, deduced amino acid sequence, and mRNA tissue expression of the rat Na/H exchanger NHE-1 and two structurally related proteins
    • Orlowski J, Kandasamy RA, Shull GE. Molecular cloning of putative members of the Na/H exchanger gene family. cDNA cloning, deduced amino acid sequence, and mRNA tissue expression of the rat Na/H exchanger NHE-1 and two structurally related proteins. J Biol Chem 267: 9331-9339, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 9331-9339
    • Orlowski, J.1    Kandasamy, R.A.2    Shull, G.E.3
  • 36
    • 0015799842 scopus 로고
    • ++ in the regulation of DNA synthesis in cultures of chick embryo cells
    • ++ in the regulation of DNA synthesis in cultures of chick embryo cells. J Cell Physiol 82: 231-238, 1973.
    • (1973) J Cell Physiol , vol.82 , pp. 231-238
    • Rubin, H.1
  • 41
    • 0034529158 scopus 로고    scopus 로고
    • Regulation of the epithelial Na(+)/H(+) exchanger isoform by the cytoskeleton
    • Szaszi K, Grinstein S, Orlowski J, Kapus A. Regulation of the epithelial Na(+)/H(+) exchanger isoform by the cytoskeleton. Cell Physiol Biochem 10: 265-272, 2000.
    • (2000) Cell Physiol Biochem , vol.10 , pp. 265-272
    • Szaszi, K.1    Grinstein, S.2    Orlowski, J.3    Kapus, A.4
  • 43
    • 0032830852 scopus 로고    scopus 로고
    • The EF-hand Ca(2+)-binding protein p22 associates with microtubules in an N-myristoylation-dependent manner
    • Timm S, Titus B, Bernd K, Barroso M. The EF-hand Ca(2+)-binding protein p22 associates with microtubules in an N-myristoylation-dependent manner. Mol Biol Cell 10: 3473-3488, 1999.
    • (1999) Mol Biol Cell , vol.10 , pp. 3473-3488
    • Timm, S.1    Titus, B.2    Bernd, K.3    Barroso, M.4
  • 44
    • 0035221927 scopus 로고    scopus 로고
    • +-dependent recovery of intracellular pH from acid loading in mouse colonic crypt cells
    • +-dependent recovery of intracellular pH from acid loading in mouse colonic crypt cells. Tohoku J Exp Med 193: 1-11, 2001.
    • (2001) Tohoku J Exp Med , vol.193 , pp. 1-11
    • Tsuchiya, Y.1    Hayashi, H.2    Suzuki, Y.3
  • 47
    • 0034677758 scopus 로고    scopus 로고
    • A novel topology model of the human Na(+)/H(+) exchanger isoform 1
    • Wakabayashi S, Pang T, Su X, Shigekawa M. A novel topology model of the human Na(+)/H(+) exchanger isoform 1. J Biol Chem 275: 7942-7949, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 7942-7949
    • Wakabayashi, S.1    Pang, T.2    Su, X.3    Shigekawa, M.4
  • 48
    • 0035282862 scopus 로고    scopus 로고
    • The chicken B cell line DT40: A novel tool for gene disruption experiments
    • Winding P, Berchtold MW. The chicken B cell line DT40: a novel tool for gene disruption experiments. J Immunol Methods 249: 1-16, 2001.
    • (2001) J Immunol Methods , vol.249 , pp. 1-16
    • Winding, P.1    Berchtold, M.W.2
  • 49
    • 2342539803 scopus 로고    scopus 로고
    • O-GlcNAc modification: A nutritional sensor that modulates proteasome function
    • Zachara NE, Hart GW. O-GlcNAc modification: a nutritional sensor that modulates proteasome function. Trends Cell Biol 14: 218-221, 2004.
    • (2004) Trends Cell Biol , vol.14 , pp. 218-221
    • Zachara, N.E.1    Hart, G.W.2
  • 50
    • 3042534011 scopus 로고    scopus 로고
    • Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells
    • Zachara NE, O'Donnell N, Cheung WD, Mercer JJ, Marth JD, Hart GW. Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells. J Biol Chem 279: 30133-30142, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 30133-30142
    • Zachara, N.E.1    O'Donnell, N.2    Cheung, W.D.3    Mercer, J.J.4    Marth, J.D.5    Hart, G.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.