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Volumn 16, Issue 1, 2004, Pages 73-79

Multiple and surprising new functions for emerin, a nuclear membrane protein

Author keywords

40 residue folded motif shared by LAP2, emerin and MAN1; (nuclear) inner membrane; BAF; Barrier to autointegration factor; EDMD; Emery Dreifuss muscular dystrophy; Fluorescence recovery after photobleaching; FRAP; GCL; Germ cell less; IM; LEM domain; MEF

Indexed keywords

EMERIN; F ACTIN; LAMIN; MEMBRANE PROTEIN; MYOSIN I;

EID: 1542382269     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2003.11.012     Document Type: Review
Times cited : (113)

References (54)
  • 1
    • 0037382801 scopus 로고    scopus 로고
    • Nuclear envelope proteins and neuromuscular diseases
    • Analysis of laminopathy-causing mutations in a structural context, providing a clear overview of animal and cell culture models currently used to study laminopathies.
    • Östlund C., Worman H.J. Nuclear envelope proteins and neuromuscular diseases. Muscle Nerve. 27:2003;393-406 Analysis of laminopathy-causing mutations in a structural context, providing a clear overview of animal and cell culture models currently used to study laminopathies.
    • (2003) Muscle Nerve , vol.27 , pp. 393-406
    • Östlund, C.1    Worman, H.J.2
  • 2
    • 0032928462 scopus 로고    scopus 로고
    • Emerin and cardiomyopathy in Emery-Dreifuss muscular dystrophy
    • Funakoshi M., Tsuchiya Y., Arahata K. Emerin and cardiomyopathy in Emery-Dreifuss muscular dystrophy. Neuromuscul. Disord. 9:1999;108-114.
    • (1999) Neuromuscul. Disord. , vol.9 , pp. 108-114
    • Funakoshi, M.1    Tsuchiya, Y.2    Arahata, K.3
  • 4
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: Building blocks or regulators of gene expression?
    • Hutchison C.J. Lamins: building blocks or regulators of gene expression? Nat. Rev. Mol. Cell. Biol. 3:2002;848-858.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 5
    • 0035694237 scopus 로고    scopus 로고
    • Identification of essential genes in cultured mammalian cells using small interfering RNAs
    • The siRNA method was used to downregulate emerin in HeLa cells. Loss of emerin did not compromise cell viability, in contrast to loss of lamin B1 or B2, which were both essential.
    • Harborth J., Elbashir S.M., Bechert K., Tuschl T., Weber K. Identification of essential genes in cultured mammalian cells using small interfering RNAs. J. Cell. Sci. 114:2001;4557-4565 The siRNA method was used to downregulate emerin in HeLa cells. Loss of emerin did not compromise cell viability, in contrast to loss of lamin B1 or B2, which were both essential.
    • (2001) J. Cell. Sci. , vol.114 , pp. 4557-4565
    • Harborth, J.1    Elbashir, S.M.2    Bechert, K.3    Tuschl, T.4    Weber, K.5
  • 6
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • A thoughtful and well-illustrated summary of the nuclear envelope and its constituent proteins from a laminopathy perspective.
    • Burke B., Stewart C.L. Life at the edge: the nuclear envelope and human disease. Nat. Rev. Mol. Cell. Biol. 3:2002;575-585 A thoughtful and well-illustrated summary of the nuclear envelope and its constituent proteins from a laminopathy perspective.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 7
    • 0037673950 scopus 로고    scopus 로고
    • Recurrent de novo point mutations in lamin a cause Hutchinson-Gilford progeria syndrome
    • Certain mutations in A-type lamins cause this devastating syndrome, and raise the question of whether emerin function might also be compromised in these patients.
    • Eriksson M., Brown W.T., Gordon L.B., Glynn M.W., Singer J., Scott L., Erdos M.R., Robbins C.M., Moses T.Y., Berglund P.et al. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature. 423:2003;293-298 Certain mutations in A-type lamins cause this devastating syndrome, and raise the question of whether emerin function might also be compromised in these patients.
    • (2003) Nature , vol.423 , pp. 293-298
    • Eriksson, M.1    Brown, W.T.2    Gordon, L.B.3    Glynn, M.W.4    Singer, J.5    Scott, L.6    Erdos, M.R.7    Robbins, C.M.8    Moses, T.Y.9    Berglund, P.10
  • 9
    • 0035696932 scopus 로고    scopus 로고
    • Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy
    • Lamins A and C mutants L85R and N195K (which cause dilated cardiomyopathy), L530P (which causes EDMD) and R492W (which causes lipodystrophy) were analyzed by transfection into HeLa cells and LMNA-null mouse embryo fibroblasts (MEFs). L85R, N195K and L530P cause partial mislocalization of emerin in vivo, and reduced in vitro binding to emerin relative to wildtype lamin A.
    • Raharjo W.H., Enarson P., Sullivan T., Stewart C.L., Burke B. Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy. J. Cell. Sci. 114:2001;4447-4457 Lamins A and C mutants L85R and N195K (which cause dilated cardiomyopathy), L530P (which causes EDMD) and R492W (which causes lipodystrophy) were analyzed by transfection into HeLa cells and LMNA-null mouse embryo fibroblasts (MEFs). L85R, N195K and L530P cause partial mislocalization of emerin in vivo, and reduced in vitro binding to emerin relative to wildtype lamin A.
    • (2001) J. Cell. Sci. , vol.114 , pp. 4447-4457
    • Raharjo, W.H.1    Enarson, P.2    Sullivan, T.3    Stewart, C.L.4    Burke, B.5
  • 10
    • 0043172367 scopus 로고    scopus 로고
    • Effect of pathogenic mis-sense mutations in lamin a on its interaction with emerin in vivo
    • Three EDMD-causing mutations in lamin A (R453W, W520S and R527P) and lipodystrophy-causing mutation R482Q are located in the lamin A tail domain. Other EDMD-causing mutations (E358K, M371K and R386K) are in the rod domain of lamin A, along with cardiomyopathy mutations, L85R and N195K. Each lamin A mutant was expressed in LMNA-null MEFs to ask if they recruited emerin to the NE. Three mutants (E358K, M371K and R482Q) retained emerin at the NE, suggesting that the relevant (disease-affected) protein is not emerin.
    • Holt I., Östlund C., Stewart C.L., Man N., Worman H.J., Morris G.E. Effect of pathogenic mis-sense mutations in lamin A on its interaction with emerin in vivo. J. Cell. Sci. 116:2003;3027-3035 Three EDMD-causing mutations in lamin A (R453W, W520S and R527P) and lipodystrophy-causing mutation R482Q are located in the lamin A tail domain. Other EDMD-causing mutations (E358K, M371K and R386K) are in the rod domain of lamin A, along with cardiomyopathy mutations, L85R and N195K. Each lamin A mutant was expressed in LMNA-null MEFs to ask if they recruited emerin to the NE. Three mutants (E358K, M371K and R482Q) retained emerin at the NE, suggesting that the relevant (disease-affected) protein is not emerin.
    • (2003) J. Cell. Sci. , vol.116 , pp. 3027-3035
    • Holt, I.1    Östlund, C.2    Stewart, C.L.3    Man, N.4    Worman, H.J.5    Morris, G.E.6
  • 11
    • 0035697055 scopus 로고    scopus 로고
    • Properties of lamin a mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy
    • Lamin A mutants R60G, L85R, N195K and E203G (which cause cardiomyopathy), mutants E358K, M371K, R386K, R453W, W520S, R527P, T528K and L530P (which cause EDMD), and mutants R482Q, R482W and K486N (which cause lipodystrophy) were transfected into C2C12 cells. In cells overexpressing mutants N195K, M371K and R386K, endogenous emerin was lost from the NE.
    • Östlund C., Bonne G., Schwartz K., Worman H.J. Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy. J. Cell. Sci. 114:2001;4435-4445 Lamin A mutants R60G, L85R, N195K and E203G (which cause cardiomyopathy), mutants E358K, M371K, R386K, R453W, W520S, R527P, T528K and L530P (which cause EDMD), and mutants R482Q, R482W and K486N (which cause lipodystrophy) were transfected into C2C12 cells. In cells overexpressing mutants N195K, M371K and R386K, endogenous emerin was lost from the NE.
    • (2001) J. Cell. Sci. , vol.114 , pp. 4435-4445
    • Östlund, C.1    Bonne, G.2    Schwartz, K.3    Worman, H.J.4
  • 12
    • 0037447893 scopus 로고    scopus 로고
    • Effects of expressing lamin a mutant protein causing Emery-Dreifuss muscular dystrophy and familial partial lipodystrophy in HeLa cells
    • Lamin A mutants G465D and R482L (which cause lipodystrophy) and R527P (causing EDMD) were transfected into HeLa cells. Overexpression of these mutants caused emerin to mislocalize into intranuclear aggregates.
    • Bechert K., Lagos-Quintana M., Harborth J., Weber K., Osborn M. Effects of expressing lamin A mutant protein causing Emery-Dreifuss muscular dystrophy and familial partial lipodystrophy in HeLa cells. Exp. Cell. Res. 286: 2003;75-86 Lamin A mutants G465D and R482L (which cause lipodystrophy) and R527P (causing EDMD) were transfected into HeLa cells. Overexpression of these mutants caused emerin to mislocalize into intranuclear aggregates.
    • (2003) Exp. Cell. Res. , vol.286 , pp. 75-86
    • Bechert, K.1    Lagos-Quintana, M.2    Harborth, J.3    Weber, K.4    Osborn, M.5
  • 13
    • 0037225049 scopus 로고    scopus 로고
    • Expression of lamin a mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy
    • Lamin A mutants R453W (EDMD) and R482W (lipodystrophy) were overexpressed in myoblasts (C2C12 cells), preadipocytes (3T3F442A cells) and a precursor fibroblast cell line (10T1/2 cells). Both mutants disrupted nuclear structure in all three cell lines, but did not disrupt emerin's localization.
    • Favreau C., Dubosclard E., Östlund C., Vigouroux C., Capeau J., Wehnert M., Higuet D., Worman H.J., Courvalin J.C., Buendia B. Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Exp. Cell. Res. 282:2003;14-23 Lamin A mutants R453W (EDMD) and R482W (lipodystrophy) were overexpressed in myoblasts (C2C12 cells), preadipocytes (3T3F442A cells) and a precursor fibroblast cell line (10T1/2 cells). Both mutants disrupted nuclear structure in all three cell lines, but did not disrupt emerin's localization.
    • (2003) Exp. Cell. Res. , vol.282 , pp. 14-23
    • Favreau, C.1    Dubosclard, E.2    Östlund, C.3    Vigouroux, C.4    Capeau, J.5    Wehnert, M.6    Higuet, D.7    Worman, H.J.8    Courvalin, J.C.9    Buendia, B.10
  • 14
    • 0242365630 scopus 로고    scopus 로고
    • Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: Altered inter-molecular interaction with emerin and implications for gene transcription
    • Endogenous lamin A mutants R482L (lipodystrophy) or R401C (EDMD) were examined in fibroblasts cultured from patients with each mutation. Antibodies against emerin pulled down lamin C, but not lamin A, from lipodystrophy fibroblast lysates. The same co-immunoprecipitation from EDMD and control fibroblasts pulled down both lamins C and A. Thus, emerin specifically fails to bind lamin A in lipodystrophy cells.
    • Capanni C., Cenni V., Mattioli E., Sabatelli P., Ognibene A., Columbaro A., Parnaik V.K., Wehnert M., Maraldi N.M., Squarzoni S.et al. Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered inter-molecular interaction with emerin and implications for gene transcription. Exp. Cell. Res. 291:2003;122-134 Endogenous lamin A mutants R482L (lipodystrophy) or R401C (EDMD) were examined in fibroblasts cultured from patients with each mutation. Antibodies against emerin pulled down lamin C, but not lamin A, from lipodystrophy fibroblast lysates. The same co-immunoprecipitation from EDMD and control fibroblasts pulled down both lamins C and A. Thus, emerin specifically fails to bind lamin A in lipodystrophy cells.
    • (2003) Exp. Cell. Res. , vol.291 , pp. 122-134
    • Capanni, C.1    Cenni, V.2    Mattioli, E.3    Sabatelli, P.4    Ognibene, A.5    Columbaro, A.6    Parnaik, V.K.7    Wehnert, M.8    Maraldi, N.M.9    Squarzoni, S.10
  • 15
    • 0036966367 scopus 로고    scopus 로고
    • Increased solubility of lamins and redistribution of lamin C in X-linked Emery-Dreifuss muscular dystrophy fibroblasts
    • Endogenous emerin and all lamins are more easily extracted from skin fibroblasts from heterogenous X-EDMD carriers. Lamin C is more abundant in the nuclear interior in emerin-null cells, suggesting that lamin C depends on emerin for its localization.
    • Markiewicz E., Venables R., Mauricio Alvarez R., Quinlan R., Dorobek M., Hausmanowa-Petrucewicz I., Hutchison C.J. Increased solubility of lamins and redistribution of lamin C in X-linked Emery-Dreifuss muscular dystrophy fibroblasts. J. Struct. Biol. 140:2002;241-253 Endogenous emerin and all lamins are more easily extracted from skin fibroblasts from heterogenous X-EDMD carriers. Lamin C is more abundant in the nuclear interior in emerin-null cells, suggesting that lamin C depends on emerin for its localization.
    • (2002) J. Struct. Biol. , vol.140 , pp. 241-253
    • Markiewicz, E.1    Venables, R.2    Mauricio Alvarez, R.3    Quinlan, R.4    Dorobek, M.5    Hausmanowa-Petrucewicz, I.6    Hutchison, C.J.7
  • 16
    • 0037405331 scopus 로고    scopus 로고
    • Functional consequences of an LMNA mutation associated with a new cardiac and non-cardiac phenotype
    • Lamin A mutant R377H (dilated cardiomyopathy), when overexpressed in COS7 and C2C12 cells, causes endogenous emerin to mislocalize.
    • Charniot J.C., Pascal C., Bouchier C., Sebillon P., Salama J., Duboscq-Bidot L., Peuchmaurd M., Desnos M., Artigou J.Y., Komajda M. Functional consequences of an LMNA mutation associated with a new cardiac and non-cardiac phenotype. Hum. Mutat. 21:2003;473-481 Lamin A mutant R377H (dilated cardiomyopathy), when overexpressed in COS7 and C2C12 cells, causes endogenous emerin to mislocalize.
    • (2003) Hum. Mutat. , vol.21 , pp. 473-481
    • Charniot, J.C.1    Pascal, C.2    Bouchier, C.3    Sebillon, P.4    Salama, J.5    Duboscq-Bidot, L.6    Peuchmaurd, M.7    Desnos, M.8    Artigou, J.Y.9    Komajda, M.10
  • 17
    • 1642403318 scopus 로고    scopus 로고
    • Cell cycle dynamics of the nuclear envelope
    • A comprehensive review of characterized nuclear membrane proteins and lamins, and their behavior during the cell cycle.
    • Foisner R. Cell cycle dynamics of the nuclear envelope. Scientific World Journal. 3:2003;1-20 A comprehensive review of characterized nuclear membrane proteins and lamins, and their behavior during the cell cycle.
    • (2003) Scientific World Journal , vol.3 , pp. 1-20
    • Foisner, R.1
  • 18
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • An impressive proteomic study of rat liver nuclear envelopes. Approximately 67 potential new nuclear membrane proteins were discovered, including two new potential LEM-domain proteins.
    • Schirmer E.C., Florens L., Guan T., Yates J.R.I., Gerace L. Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science. 301:2003;1380-1382 An impressive proteomic study of rat liver nuclear envelopes. Approximately 67 potential new nuclear membrane proteins were discovered, including two new potential LEM-domain proteins.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.I.4    Gerace, L.5
  • 19
    • 0035919768 scopus 로고    scopus 로고
    • Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy
    • Wolff N., Gilquin B., Courchay K., Callebaut I., Worman H.J., Zinn-Justin S. Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy. FEBS Lett. 501:2001;171-176.
    • (2001) FEBS Lett. , vol.501 , pp. 171-176
    • Wolff, N.1    Gilquin, B.2    Courchay, K.3    Callebaut, I.4    Worman, H.J.5    Zinn-Justin, S.6
  • 20
    • 0035794643 scopus 로고    scopus 로고
    • LAP2 binds to BAF-DNA complexes: Requirement for the LEM domain and modulation by variable regions
    • Shumaker D.K., Lee K.K., Tanhehco Y.C., Craigie R., Wilson K.L. LAP2 binds to BAF-DNA complexes: requirement for the LEM domain and modulation by variable regions. EMBO J. 20:2001;1754-1764.
    • (2001) EMBO J. , vol.20 , pp. 1754-1764
    • Shumaker, D.K.1    Lee, K.K.2    Tanhehco, Y.C.3    Craigie, R.4    Wilson, K.L.5
  • 21
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin a and DNA-bridging protein BAF
    • A large collection of alanine-substitution mutations in emerin was used to map its binding sites for lamin A and BAF.
    • Lee K.K., Haraguchi T., Lee R.S., Koujin T., Hiraoka Y., Wilson K.L. Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J. Cell. Sci. 114:2001;4567-4573 A large collection of alanine-substitution mutations in emerin was used to map its binding sites for lamin A and BAF.
    • (2001) J. Cell. Sci. , vol.114 , pp. 4567-4573
    • Lee, K.K.1    Haraguchi, T.2    Lee, R.S.3    Koujin, T.4    Hiraoka, Y.5    Wilson, K.L.6
  • 22
    • 0034255236 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex
    • Zheng R., Ghirlando R., Lee M.S., Mizuuchi K., Krause M., Craigie R. Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc. Natl. Acad. Sci. U S A. 97:2000;8997-9002.
    • (2000) Proc. Natl. Acad. Sci. U S a , vol.97 , pp. 8997-9002
    • Zheng, R.1    Ghirlando, R.2    Lee, M.S.3    Mizuuchi, K.4    Krause, M.5    Craigie, R.6
  • 23
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly
    • Segura-Totten M., Kowalski A.K., Craigie R., Wilson K.L. Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J. Cell. Biol. 158:2002;475-485.
    • (2002) J. Cell. Biol. , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 25
    • 0036500323 scopus 로고    scopus 로고
    • The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans
    • Gruenbaum Y., Lee K.K., Liu J., Cohen M., Wilson K.L. The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans. J. Cell. Sci. 115:2002;923-929.
    • (2002) J. Cell. Sci. , vol.115 , pp. 923-929
    • Gruenbaum, Y.1    Lee, K.K.2    Liu, J.3    Cohen, M.4    Wilson, K.L.5
  • 26
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans
    • To test the hypothesis that LEM-domain proteins have overlapping functions, MAN1 expression was RNAi-reduced by ∼90% in normal or emerin-deficient embryos. Results suggest that MAN1 itself is an essential gene; however, emerin compensated for 90%-reduced levels of MAN1, because embryos reduced for both proteins died by the 100-cell stage.
    • Liu J., Lee K.K., Segura-Totten M., Neufeld E., Wilson K.L., Gruenbaum Y. MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U S A. 100:2003;4598-4603 To test the hypothesis that LEM-domain proteins have overlapping functions, MAN1 expression was RNAi-reduced by ∼90% in normal or emerin-deficient embryos. Results suggest that MAN1 itself is an essential gene; however, emerin compensated for 90%-reduced levels of MAN1, because embryos reduced for both proteins died by the 100-cell stage.
    • (2003) Proc. Natl. Acad. Sci. U S a , vol.100 , pp. 4598-4603
    • Liu, J.1    Lee, K.K.2    Segura-Totten, M.3    Neufeld, E.4    Wilson, K.L.5    Gruenbaum, Y.6
  • 27
    • 0037081564 scopus 로고    scopus 로고
    • The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype
    • Fairley E.A., Riddell A., Ellis J.A., Kendrick-Jones J. The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype. J. Cell. Sci. 115:2002;341-354.
    • (2002) J. Cell. Sci. , vol.115 , pp. 341-354
    • Fairley, E.A.1    Riddell, A.2    Ellis, J.A.3    Kendrick-Jones, J.4
  • 28
    • 0036966281 scopus 로고    scopus 로고
    • Investigation of nuclear architecture with a domain-presenting expression system
    • A novel approach to probe nuclear structure and detect protein-protein interactions in living cells.
    • Dreger C.K., Konig A.R., Spring H., Lichter P., Herrmann H. Investigation of nuclear architecture with a domain-presenting expression system. J. Struct. Biol. 140:2002;100-115 A novel approach to probe nuclear structure and detect protein-protein interactions in living cells.
    • (2002) J. Struct. Biol. , vol.140 , pp. 100-115
    • Dreger, C.K.1    Konig, A.R.2    Spring, H.3    Lichter, P.4    Herrmann, H.5
  • 29
    • 0034176682 scopus 로고    scopus 로고
    • The nuclear envelope, muscular dystrophy and gene expression
    • Here, it is hypothesized that highly specialized tissues in the mesenchymal stem-cell lineage (muscle, fat, bone, cartilage, tendons and other connective tissues) would be particularly sensitive to mutations in A-type lamins.
    • Wilson K.L. The nuclear envelope, muscular dystrophy and gene expression. Trends Cell. Biol. 10:2000;125-129 Here, it is hypothesized that highly specialized tissues in the mesenchymal stem-cell lineage (muscle, fat, bone, cartilage, tendons and other connective tissues) would be particularly sensitive to mutations in A-type lamins.
    • (2000) Trends Cell. Biol. , vol.10 , pp. 125-129
    • Wilson, K.L.1
  • 30
    • 0038159312 scopus 로고    scopus 로고
    • The lamina-associated polypeptide 2 (LAP2) isoforms β, γ and ω of zebrafish: Developmental expression and behavior during the cell cycle
    • This work shows that LAP2 isoforms are differentially expressed during zebrafish development, and also have different behaviors during the cell cycle.
    • Schoft V.K., Beauvais A.J., Lang C., Gajewski A., Prufert K., Winkler C., Akimenko M.A., Paulin-Levasseur M., Krohne G. The lamina-associated polypeptide 2 (LAP2) isoforms β, γ and ω of zebrafish: developmental expression and behavior during the cell cycle. J. Cell. Sci. 116:2003;2505-2517 This work shows that LAP2 isoforms are differentially expressed during zebrafish development, and also have different behaviors during the cell cycle.
    • (2003) J. Cell. Sci. , vol.116 , pp. 2505-2517
    • Schoft, V.K.1    Beauvais, A.J.2    Lang, C.3    Gajewski, A.4    Prufert, K.5    Winkler, C.6    Akimenko, M.A.7    Paulin-Levasseur, M.8    Krohne, G.9
  • 31
    • 0035881480 scopus 로고    scopus 로고
    • Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: One binds BAF and the other binds DNA
    • Cai M., Huang Y., Ghirlando R., Wilson K.L., Craigie R., Clore G.M. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. EMBO J. 20:2001;4399-4407.
    • (2001) EMBO J. , vol.20 , pp. 4399-4407
    • Cai, M.1    Huang, Y.2    Ghirlando, R.3    Wilson, K.L.4    Craigie, R.5    Clore, G.M.6
  • 32
    • 0035696958 scopus 로고    scopus 로고
    • BAF is required for emerin assembly into the reforming nuclear envelope
    • HeLa cells, expressing either wild-type or mutated emerins (GFP-tagged) show that emerin's LEM-domain is essential for the interaction with BAF early in nuclear assembly, and for emerin to reassemble into the NE after mitosis.
    • Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y., Yoneda Y., Wilson K.L., Hiraoka Y. BAF is required for emerin assembly into the reforming nuclear envelope. J. Cell. Sci. 114:2001;4575-4585 HeLa cells, expressing either wild-type or mutated emerins (GFP-tagged) show that emerin's LEM-domain is essential for the interaction with BAF early in nuclear assembly, and for emerin to reassemble into the NE after mitosis.
    • (2001) J. Cell. Sci. , vol.114 , pp. 4575-4585
    • Haraguchi, T.1    Koujin, T.2    Segura-Totten, M.3    Lee, K.K.4    Matsuoka, Y.5    Yoneda, Y.6    Wilson, K.L.7    Hiraoka, Y.8
  • 33
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP. FLIP and FRET analyses in living HeLa cells
    • in press.
    • Shimi T, Koujin T, Segura-Totten M, Wilson KL, Hiraoka Y, Haraguchi T: Dynamic interaction between BAF and emerin revealed by FRAP. FLIP and FRET analyses in living HeLa cells. J Struct Biol, in press. The first direct demonstration of binding between BAF and emerin in live cells, and the surprising discovery that BAF is highly mobile at all its locations (cytoplasm, NE, nuclear interior) during interphase.
    • J Struct Biol
    • Shimi, T.1    Koujin, T.2    Segura-Totten, M.3    Wilson, K.L.4    Hiraoka, Y.5    Haraguchi, T.6
  • 34
    • 0037077382 scopus 로고    scopus 로고
    • Nesprin-1α self-associates and binds directly to emerin and lamin a in vitro
    • Biochemical analysis showing that emerin can bind with 4 nM affinity to nesprin-1α, a fellow IM protein.
    • Mislow J.M., Holaska J.M., Kim M.S., Lee K.K., Segura-Totten M., Wilson K.L., McNally E.M. Nesprin-1α self-associates and binds directly to emerin and lamin A in vitro. FEBS Lett. 525:2002;135-140 Biochemical analysis showing that emerin can bind with 4 nM affinity to nesprin-1α, a fellow IM protein.
    • (2002) FEBS Lett. , vol.525 , pp. 135-140
    • Mislow, J.M.1    Holaska, J.M.2    Kim, M.S.3    Lee, K.K.4    Segura-Totten, M.5    Wilson, K.L.6    McNally, E.M.7
  • 36
    • 0036429266 scopus 로고    scopus 로고
    • The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300
    • This paper summarizes and clarifies the confusing world of nesprin isoforms, which have many other names, including Syne, Myne, ANC and NUANCE, in the literature. A consistent (nesprin-based?) nomenclature would be appreciated.
    • Zhang Q., Ragnauth C., Greener M.J., Shanahan C.M., Roberts R.G. The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300. Genomics. 80:2002;473-481 This paper summarizes and clarifies the confusing world of nesprin isoforms, which have many other names, including Syne, Myne, ANC and NUANCE, in the literature. A consistent (nesprin-based?) nomenclature would be appreciated.
    • (2002) Genomics , vol.80 , pp. 473-481
    • Zhang, Q.1    Ragnauth, C.2    Greener, M.J.3    Shanahan, C.M.4    Roberts, R.G.5
  • 37
    • 0036155776 scopus 로고    scopus 로고
    • Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C
    • Mislow J.M., Kim M.S., Davis D.B., McNally E.M. Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C. J. Cell. Sci. 115:2002;61-70.
    • (2002) J. Cell. Sci. , vol.115 , pp. 61-70
    • Mislow, J.M.1    Kim, M.S.2    Davis, D.B.3    McNally, E.M.4
  • 38
    • 0034644646 scopus 로고    scopus 로고
    • Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction
    • Apel E.D., Lewis R.M., Grady R.M., Sanes J.R. Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction. J. Biol. Chem. 275:2000;31986-31995.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31986-31995
    • Apel, E.D.1    Lewis, R.M.2    Grady, R.M.3    Sanes, J.R.4
  • 39
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • A stimulating review of nuclear actin with historical perspective and biochemical insight.
    • Pederson T., Aebi U. Actin in the nucleus: what form and what for? J. Struct. Biol. 140:2002;3-9 A stimulating review of nuclear actin with historical perspective and biochemical insight.
    • (2002) J. Struct. Biol. , vol.140 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 40
    • 0037684765 scopus 로고    scopus 로고
    • The nucleoskeleton: Lamins and actin are major players in essential nuclear functions
    • Shumaker D.K., Kuczmarski E.R., Goldman R.D. The nucleoskeleton: lamins and actin are major players in essential nuclear functions. Curr. Opin. Cell. Biol. 15:2003;358-366.
    • (2003) Curr. Opin. Cell. Biol. , vol.15 , pp. 358-366
    • Shumaker, D.K.1    Kuczmarski, E.R.2    Goldman, R.D.3
  • 41
    • 0036837219 scopus 로고    scopus 로고
    • Functional domains of the nucleus: Implications for Emery-Dreifuss muscular dystrophy
    • The nuclear matrix revisited, with interesting models and speculations about nuclear actin.
    • Maraldi N.M., Lattanzi G., Sabatelli P., Ognibene A., Squarzoni S. Functional domains of the nucleus: implications for Emery-Dreifuss muscular dystrophy. Neuromuscul. Disord. 12:2002;815-823 The nuclear matrix revisited, with interesting models and speculations about nuclear actin.
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 815-823
    • Maraldi, N.M.1    Lattanzi, G.2    Sabatelli, P.3    Ognibene, A.4    Squarzoni, S.5
  • 42
    • 0344211826 scopus 로고    scopus 로고
    • Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts
    • Actin, emerin and lamins A and C co-immunoprecipitate from nuclear extracts, and the actin-emerin association appears to be regulated via phosphorylation.
    • Lattanzi G., Cenni V., Marmiroli S., Capanni C., Mattioli E., Merlini L., Squarzoni S., Maraldi N.M. Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts. Biochem. Biophys. Res. Commun. 303:2003;764-770 Actin, emerin and lamins A and C co-immunoprecipitate from nuclear extracts, and the actin-emerin association appears to be regulated via phosphorylation.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 764-770
    • Lattanzi, G.1    Cenni, V.2    Marmiroli, S.3    Capanni, C.4    Mattioli, E.5    Merlini, L.6    Squarzoni, S.7    Maraldi, N.M.8
  • 43
    • 0042164479 scopus 로고    scopus 로고
    • 108th ENMC International Workshop, 3rd Workshop of the MYO-CLUSTER project: EUROMEN, 7th International Emery-Dreifuss Muscular Dystrophy (EDMD) Workshop: 2002 Sept 13-15; Naarden, the Netherlands
    • This meeting report summarizes recent or unpublished research on X-EDMD from many laboratories.
    • Bonne G., Yaou R.B., Beroud C., Boriani G., Brown S., de Visser M., Duboc D., Ellis J., Hausmanowa-Petrusewicz I., Lattanzi G.et al. 108th ENMC International Workshop, 3rd Workshop of the MYO-CLUSTER project: EUROMEN, 7th International Emery-Dreifuss Muscular Dystrophy (EDMD) Workshop: 2002 Sept 13-15; Naarden, The Netherlands. Neuromuscul. Disord. 13:2003;508-515 This meeting report summarizes recent or unpublished research on X-EDMD from many laboratories.
    • (2003) Neuromuscul. Disord. , vol.13 , pp. 508-515
    • Bonne, G.1    Yaou, R.B.2    Beroud, C.3    Boriani, G.4    Brown, S.5    De Visser, M.6    Duboc, D.7    Ellis, J.8    Hausmanowa-Petrusewicz, I.9    Lattanzi, G.10
  • 44
    • 11244286392 scopus 로고    scopus 로고
    • Nuclear AKAPs in muscle differentiation: Redistribution of PKA in myotubes and regulation of AKAP149 expression by MAPK/ERK pathway
    • submitted.
    • Mattioli E, Cenni V, Capanni C, Columbaro M, Ognibene A, Squarzoni S, Maraldi NM, Lattanzi G: Nuclear AKAPs in muscle differentiation: redistribution of PKA in myotubes and regulation of AKAP149 expression by MAPK/ERK pathway. FEBS Lett, submitted. Evidence that emerin interacts with the regulatory subunit of PKA (cAMP dependent protein kinase) in myotubes.
    • FEBS Lett
    • Mattioli, E.1    Cenni, V.2    Capanni, C.3    Columbaro, M.4    Ognibene, A.5    Squarzoni, S.6    Maraldi, N.M.7    Lattanzi, G.8
  • 46
    • 0034777991 scopus 로고    scopus 로고
    • Nuclear membrane protein LAP2β mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less)
    • This was the first study to show that a nuclear membrane protein (LAP2β) directly regulates gene expression.
    • Nili E., Cojocaru G.S., Kalma Y., Ginsberg D., Copeland N.G., Gilbert D.J., Jenkins N.A., Berger R., Shaklai S., Amariglio N.et al. Nuclear membrane protein LAP2β mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less). J. Cell. Sci. 114:2001;3297-3307 This was the first study to show that a nuclear membrane protein (LAP2β) directly regulates gene expression.
    • (2001) J. Cell. Sci. , vol.114 , pp. 3297-3307
    • Nili, E.1    Cojocaru, G.S.2    Kalma, Y.3    Ginsberg, D.4    Copeland, N.G.5    Gilbert, D.J.6    Jenkins, N.A.7    Berger, R.8    Shaklai, S.9    Amariglio, N.10
  • 47
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • A significant biochemical analysis that measures binding affinities and shows that emerin and lamin A unite to form at least two distinct types of ternary complexes, containing either GCL or BAF in vitro.
    • Holaska J.M., Lee K.K., Kowalski A.K., Wilson K.L. Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J. Biol. Chem. 278:2003;6969-6975 A significant biochemical analysis that measures binding affinities and shows that emerin and lamin A unite to form at least two distinct types of ternary complexes, containing either GCL or BAF in vitro.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 49
    • 0033008195 scopus 로고    scopus 로고
    • Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins
    • Kasof G.M., Goyal L., White E. Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins. Mol. Cell. Biol. 19:1999;4390-4404.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4390-4404
    • Kasof, G.M.1    Goyal, L.2    White, E.3
  • 50
    • 18744413894 scopus 로고    scopus 로고
    • Fate of the nuclear lamina during Caenorhabditis elegans apoptosis
    • Tzur Y.B., Hersh B.M., Horvitz H.R., Gruenbaum Y. Fate of the nuclear lamina during Caenorhabditis elegans apoptosis. J. Struct. Biol. 137:2002;146-153.
    • (2002) J. Struct. Biol. , vol.137 , pp. 146-153
    • Tzur, Y.B.1    Hersh, B.M.2    Horvitz, H.R.3    Gruenbaum, Y.4
  • 51
    • 0033708899 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2α
    • Gotzmann J., Vlcek S., Foisner R. Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2α J. Cell. Sci. 113:2000;3769-3780.
    • (2000) J. Cell. Sci. , vol.113 , pp. 3769-3780
    • Gotzmann, J.1    Vlcek, S.2    Foisner, R.3
  • 52
    • 0035861884 scopus 로고    scopus 로고
    • Staurosporine treatment and serum starvation promote the cleavage of emerin in cultured mouse myoblasts: Involvement of a caspase-dependent mechanism
    • Columbaro M., Mattioli E., Lattanzi G., Rutigliano C., Ognibene A., Maraldi N.M., Squarzoni S. Staurosporine treatment and serum starvation promote the cleavage of emerin in cultured mouse myoblasts: involvement of a caspase-dependent mechanism. FEBS Lett. 509:2001;423-429.
    • (2001) FEBS Lett. , vol.509 , pp. 423-429
    • Columbaro, M.1    Mattioli, E.2    Lattanzi, G.3    Rutigliano, C.4    Ognibene, A.5    Maraldi, N.M.6    Squarzoni, S.7
  • 53
    • 0036263036 scopus 로고    scopus 로고
    • CDNA microarray analysis of gene expression in fibroblasts of patients with X-linked Emery-Dreifuss muscular dystrophy
    • A comparative study, showing that loss of emerin correlates with altered expression of 60 genes, including several that encode interaction partners of emerin.
    • Tsukahara T., Tsujino S., Arahata K. CDNA microarray analysis of gene expression in fibroblasts of patients with X-linked Emery-Dreifuss muscular dystrophy. Muscle Nerve. 25:2002;898-901 A comparative study, showing that loss of emerin correlates with altered expression of 60 genes, including several that encode interaction partners of emerin.
    • (2002) Muscle Nerve , vol.25 , pp. 898-901
    • Tsukahara, T.1    Tsujino, S.2    Arahata, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.