메뉴 건너뛰기




Volumn 1811, Issue 6, 2011, Pages 377-385

CTP:phosphocholine cytidylyltransferase α (CCTα) and lamins alter nuclear membrane structure without affecting phosphatidylcholine synthesis

Author keywords

CCT ; Choline transport; Hutchinson Gilford progeria syndrome; Lamins; Nucleoplasmic reticulum; Phosphatidylcholine

Indexed keywords

CHOLINE; CHOLINE PHOSPHATE CYTIDYLYLTRANSFERASE; ETHANOLAMINE PHOSPHOTRANSFERASE; HEMICHOLINIUM 3; LAMIN; LAMIN A; LAMIN C; PHOSPHATIDYLCHOLINE; PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE ALPHA; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 79955752139     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2011.04.001     Document Type: Article
Times cited : (17)

References (38)
  • 1
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • DOI 10.1128/MCB.26.10.3738-3751.2006
    • F. Haque, D.J. Lloyd, D.T. Smallwood, C.L. Dent, C.M. Shanahan, A.M. Fry, R.C. Trembath, and S. Shackleton SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton Mol. Cell. Biol. 26 2006 3738 3751 (Pubitemid 43726392)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.10 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3    Dent, C.L.4    Shanahan, C.M.5    Fry, A.M.6    Trembath, R.C.7    Shackleton, S.8
  • 3
    • 33645962474 scopus 로고    scopus 로고
    • Nuclear pores form de novo from both sides of the nuclear envelope
    • M.A. D'Angelo, D.J. Anderson, E. Richard, and M.W. Hetzer Nuclear pores form de novo from both sides of the nuclear envelope Science 312 2006 440 443
    • (2006) Science , vol.312 , pp. 440-443
    • D'Angelo, M.A.1    Anderson, D.J.2    Richard, E.3    Hetzer, M.W.4
  • 4
    • 0031051629 scopus 로고    scopus 로고
    • Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope
    • DOI 10.1083/jcb.136.3.531
    • M. Fricker, M. Hollinshead, N. White, and D. Vaux Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope J. Cell Biol. 136 1997 531 544 (Pubitemid 27083756)
    • (1997) Journal of Cell Biology , vol.136 , Issue.3 , pp. 531-544
    • Fricker, M.1    Hollinshead, M.2    White, N.3    Vaux, D.4
  • 5
    • 0037718604 scopus 로고    scopus 로고
    • Regulation of calcium signals in the nucleus by a nucleoplasmic reticulum
    • DOI 10.1038/ncb980
    • W. Echevarria, M.F. Leite, M.T. Guerra, W.R. Zipfel, and M.H. Nathanson Regulation of calcium signals in the nucleus by a nucleoplasmic reticulum Nat. Cell Biol. 5 2003 440 446 (Pubitemid 36592267)
    • (2003) Nature Cell Biology , vol.5 , Issue.5 , pp. 440-446
    • Echevarria, W.1    Leite, M.F.2    Guerra, M.T.3    Zipfel, W.R.4    Nathanson, M.H.5
  • 6
    • 29444441912 scopus 로고    scopus 로고
    • Calcium release from ryanodine receptors in the nucleoplasmic reticulum
    • DOI 10.1016/j.ceca.2005.09.010, PII S0143416005001867
    • P. Marius, M.T. Guerra, M.H. Nathanson, B.E. Ehrlich, and M.F. Leite Calcium release from ryanodine receptors in the nucleoplasmic reticulum Cell Calcium 39 2006 65 73 (Pubitemid 43009886)
    • (2006) Cell Calcium , vol.39 , Issue.1 , pp. 65-73
    • Marius, P.1    Guerra, M.T.2    Nathanson, M.H.3    Ehrlich, B.E.4    Leite, M.F.5
  • 7
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • DOI 10.1093/hmg/5.6.801
    • S. Manilal, T.M. Nguyen, C.A. Sewry, and G.E. Morris The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein Hum. Mol. Genet. 5 1996 801 808 (Pubitemid 26171704)
    • (1996) Human Molecular Genetics , vol.5 , Issue.6 , pp. 801-808
    • Manilal, S.1    Nguyen, T.M.2    Sewry, C.A.3    Morris, G.E.4
  • 8
    • 0033950898 scopus 로고    scopus 로고
    • Pushing the envelope on lipodystrophy
    • DOI 10.1038/72734
    • J.S. Flier Pushing the envelope on lipodystrophy Nat. Genet. 24 2000 103 104 (Pubitemid 30094704)
    • (2000) Nature Genetics , vol.24 , Issue.2 , pp. 103-104
    • Flier, J.S.1
  • 11
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
    • DOI 10.1038/sj.emboj.7600672
    • H. Santos-Rosa, J. Leung, N. Grimsey, S. Peak-Chew, and S. Siniossoglou The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth EMBO J. 24 2005 1931 1941 (Pubitemid 40896165)
    • (2005) EMBO Journal , vol.24 , Issue.11 , pp. 1931-1941
    • Santos-Rosa, H.1    Leung, J.2    Grimsey, N.3    Peak-Chew, S.4    Siniossoglou, S.5
  • 12
    • 37549018969 scopus 로고    scopus 로고
    • The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity
    • G.S. Han, S. Siniossoglou, and G.M. Carman The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity J. Biol. Chem. 282 2007 37026 37035
    • (2007) J. Biol. Chem. , vol.282 , pp. 37026-37035
    • Han, G.S.1    Siniossoglou, S.2    Carman, G.M.3
  • 13
    • 33747853190 scopus 로고    scopus 로고
    • Lipin 1 is an inducible amplifier of the hepatic PGC-1α/PPARα regulatory pathway
    • DOI 10.1016/j.cmet.2006.08.005, PII S1550413106002750
    • B.N. Finck, M.C. Gropler, Z. Chen, T.C. Leone, M.A. Croce, T.E. Harris, J.C. Lawrence Jr., and D.P. Kelly Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha regulatory pathway Cell Metab. 4 2006 199 210 (Pubitemid 44283957)
    • (2006) Cell Metabolism , vol.4 , Issue.3 , pp. 199-210
    • Finck, B.N.1    Gropler, M.C.2    Chen, Z.3    Leone, T.C.4    Croce, M.A.5    Harris, T.E.6    Lawrence Jr., J.C.7    Kelly, D.P.8
  • 14
    • 25444465996 scopus 로고    scopus 로고
    • Alternatively spliced lipin isoforms exhibit distinct expression pattern, subcellular localization, and role in adipogenesis
    • DOI 10.1074/jbc.M503885200
    • M. Peterfy, J. Phan, and K. Reue Alternatively spliced lipin isoforms exhibit distinct expression pattern, subcellular localization, and role in adipogenesis J. Biol. Chem. 280 2005 32883 32889 (Pubitemid 41368337)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.38 , pp. 32883-32889
    • Peterfy, M.1    Phan, J.2    Reue, K.3
  • 16
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties
    • DOI 10.2174/138920306779025675
    • R.B. Cornell, and S.G. Taneva Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties Curr. Protein Pept. Sci. 7 2006 539 552 (Pubitemid 44883931)
    • (2006) Current Protein and Peptide Science , vol.7 , Issue.6 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 17
    • 0027415175 scopus 로고
    • Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase
    • Y. Wang, T.D. Sweitzer, P.A. Weinhold, and C. Kent Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase J. Biol. Chem. 268 1993 5899 5904 (Pubitemid 23090925)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.8 , pp. 5899-5904
    • Wang, Y.1    Sweitzer, T.D.2    Weinhold, P.A.3    Kent, C.4
  • 18
    • 0028816963 scopus 로고
    • Identification of the nuclear localization signal of rat liver CTP:phosphocholine cytidylyltransferase
    • Y. Wang, J.I. MacDonald, and C. Kent Identification of the nuclear localization signal of rat liver CTP:phosphocholine cytidylyltransferase J. Biol. Chem. 270 1995 354 360
    • (1995) J. Biol. Chem. , vol.270 , pp. 354-360
    • Wang, Y.1    MacDonald, J.I.2    Kent, C.3
  • 19
    • 14844301707 scopus 로고    scopus 로고
    • The rate-limiting enzyme in phosphatidylcholine synthesis regulates proliferation of the nucleoplasmic reticulum
    • DOI 10.1091/mbc.E04-10-0874
    • T.A. Lagace, and N.D. Ridgway The rate-limiting enzyme in phosphatidylcholine synthesis regulates proliferation of the nucleoplasmic reticulum Mol. Biol. Cell 16 2005 1120 1130 (Pubitemid 40349550)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.3 , pp. 1120-1130
    • Lagace, T.A.1    Ridgway, N.D.2
  • 20
    • 38749103064 scopus 로고    scopus 로고
    • Expansion of the nucleoplasmic reticulum requires the coordinated activity of lamins and CTP:Phosphocholine cytidylyltransferase α
    • DOI 10.1091/mbc.E07-02-0179
    • K. Gehrig, R.B. Cornell, and N.D. Ridgway Expansion of the nucleoplasmic reticulum requires the coordinated activity of lamins and CTP:phosphocholine cytidylyltransferase a Mol. Biol. Cell 19 2008 237 247 (Pubitemid 351186149)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.1 , pp. 237-247
    • Gehrig, K.1    Cornell, R.B.2    Ridgway, N.D.3
  • 21
    • 0033578749 scopus 로고    scopus 로고
    • Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant
    • A. Lykidis, I. Baburina, and S. Jackowski Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant J. Biol. Chem. 274 1999 26992 27001
    • (1999) J. Biol. Chem. , vol.274 , pp. 26992-27001
    • Lykidis, A.1    Baburina, I.2    Jackowski, S.3
  • 22
    • 0036734611 scopus 로고    scopus 로고
    • The major sites of cellular phospholipid synthesis and molecular determinants of fatty acid and lipid head group specificity
    • DOI 10.1091/mbc.01-11-0540
    • A.L. Henneberry, M.M. Wright, and C.R. McMaster The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity Mol. Biol. Cell 13 2002 3148 3161 (Pubitemid 35034252)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.9 , pp. 3148-3161
    • Henneberry, A.L.1    Wright, M.M.2    McMaster, C.R.3
  • 23
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of low-density lipoprotein in cultured cells
    • J.L. Goldstein, S.K. Basu, and M.S. Brown, Receptor mediated endocytosis of low-density lipoprotein in cultured cells. Methods Enzymol. 98 1983 241 260 (Pubitemid 14219888)
    • (1983) Methods in Enzymology , vol.VOL. 98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 24
    • 0030942333 scopus 로고    scopus 로고
    • Decreased phosphatidylcholine biosynthesis and abnormal distribution of CTP:phosphocholine cytidylyltransferase in cholesterol auxotrophic Chinese hamster ovary cells
    • M.K. Storey, D.M. Byers, H.W. Cook, and N.D. Ridgway Decreased phosphatidylcholine biosynthesis and abnormal distribution of CTP:phosphocholine cytidylyltransferase in cholesterol auxotrophic Chinese hamster ovary cells J. Lipid Res. 38 1997 711 722 (Pubitemid 27194922)
    • (1997) Journal of Lipid Research , vol.38 , Issue.4 , pp. 711-722
    • Storey, M.K.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 25
    • 0037160130 scopus 로고    scopus 로고
    • Single nucleotide polymorphism of the human high affinity choline transporter alters transport rate
    • DOI 10.1074/jbc.M207742200
    • T. Okuda, M. Okamura, C. Kaitsuka, T. Haga, and D. Gurwitz Single nucleotide polymorphism of the human high affinity choline transporter alters transport rate J. Biol. Chem. 277 2002 45315 45322 (Pubitemid 36159138)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45315-45322
    • Okuda, T.1    Okamura, M.2    Kaitsuka, C.3    Haga, T.4    Gurwitz, D.5
  • 26
    • 5044223023 scopus 로고    scopus 로고
    • Identification and expression of a mouse muscle-specific CTL1 gene
    • DOI 10.1016/j.gene.2004.07.042, PII S0378111904004482
    • Z. Yuan, L. Wagner, A. Poloumienko, and M. Bakovic Identification and expression of a mouse muscle-specific CTL1 gene Gene 341 2004 305 312 (Pubitemid 39335905)
    • (2004) Gene , vol.341 , Issue.1-2 , pp. 305-312
    • Yuan, Z.1    Wagner, L.2    Poloumienko, A.3    Bakovic, M.4
  • 27
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • E.M. Manders, J. Stap, G.J. Brakenhoff, R. van Driel, and J.A. Aten Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy J. Cell Sci. 103 Pt 3 1992 857 862 (Pubitemid 23023255)
    • (1992) Journal of Cell Science , vol.103 , Issue.3 , pp. 857-862
    • Manders, E.M.M.1    Stap, J.2    Brakenhoff, G.J.3    Van Driel, R.4    Aten, J.A.5
  • 30
    • 0033636843 scopus 로고    scopus 로고
    • Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin A and C but not lamin B structure in mammalian cells
    • M. Izumi, O.A. Vaughan, C.J. Hutchison, and D.M. Gilbert Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin A and C but not lamin B structure in mammalian cells Mol. Biol. Cell 11 2000 4323 4337
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4323-4337
    • Izumi, M.1    Vaughan, O.A.2    Hutchison, C.J.3    Gilbert, D.M.4
  • 31
    • 0030863126 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis
    • DOI 10.1083/jcb.136.6.1201
    • T.P. Spann, R.D. Moir, A.E. Goldman, R. Stick, and R.D. Goldman Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis J. Cell Biol. 136 1997 1201 1212 (Pubitemid 27421909)
    • (1997) Journal of Cell Biology , vol.136 , Issue.6 , pp. 1201-1212
    • Spann, T.P.1    Moir, R.D.2    Goldman, A.E.3    Stick, R.4    Goldman, R.D.5
  • 32
    • 34249788998 scopus 로고    scopus 로고
    • 'Laminopathies': A wide spectrum of human diseases
    • DOI 10.1016/j.yexcr.2007.03.028, PII S0014482707001279
    • H.J. Worman, and G. Bonne "Laminopathies": a wide spectrum of human diseases Exp. Cell Res. 313 2007 2121 2133 (Pubitemid 46850729)
    • (2007) Experimental Cell Research , vol.313 , Issue.10 , pp. 2121-2133
    • Worman, H.J.1    Bonne, G.2
  • 37
    • 43149124203 scopus 로고    scopus 로고
    • Lamin A-dependent misregulation of adult stem cells associated with accelerated ageing
    • P. Scaffidi, and T. Misteli Lamin A-dependent misregulation of adult stem cells associated with accelerated ageing Nat. Cell Biol. 10 2008 452 459
    • (2008) Nat. Cell Biol. , vol.10 , pp. 452-459
    • Scaffidi, P.1    Misteli, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.