메뉴 건너뛰기




Volumn 103, Issue 3, 2008, Pages 765-777

Nuclear localization of magphinins, alternative splicing products of the human trophinin gene

Author keywords

Alternative splicing; MAGE; Magphinin; Nuclear localization; Nuclear matrix; Trophinin

Indexed keywords

GENE PRODUCT; MAGPHININ ALPHA; MAGPHININ BETA; MAGPHININ DERIVATIVE; MAGPHININ GAMMA; PROTEIN; TRITON X 100; TROPHININ; UNCLASSIFIED DRUG;

EID: 39049127628     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.21446     Document Type: Article
Times cited : (6)

References (46)
  • 2
    • 0037086294 scopus 로고    scopus 로고
    • The MAGE proteins: Emerging roles in cell cycle progression, apoptosis, and neurogenetic disease
    • Barker PA, Salehi A. 2002. The MAGE proteins: Emerging roles in cell cycle progression, apoptosis, and neurogenetic disease. J Neurosci Res 67:705-712.
    • (2002) J Neurosci Res , vol.67 , pp. 705-712
    • Barker, P.A.1    Salehi, A.2
  • 3
    • 0029894726 scopus 로고    scopus 로고
    • Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay
    • Bogerd HP, Fridell RA, Benson RE, Hua J, Cullen BR. 1996. Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay. Mol Cell Biol 16:4207-4214.
    • (1996) Mol Cell Biol , vol.16 , pp. 4207-4214
    • Bogerd, H.P.1    Fridell, R.A.2    Benson, R.E.3    Hua, J.4    Cullen, B.R.5
  • 4
    • 0035879005 scopus 로고    scopus 로고
    • An overview of the MAGE gene family with the identification of all human members of the family
    • Chomez P, De Backer O, Bertrand M, De Plaen E, Boon T, Lucas S. 2001. An overview of the MAGE gene family with the identification of all human members of the family. Cancer Res 61:5544-5551.
    • (2001) Cancer Res , vol.61 , pp. 5544-5551
    • Chomez, P.1    De Backer, O.2    Bertrand, M.3    De Plaen, E.4    Boon, T.5    Lucas, S.6
  • 5
    • 0023919931 scopus 로고
    • Ribonucleoprotein particles in cellular processes
    • Dreyfuss G, Philipson L, Mattaj IW. 1988. Ribonucleoprotein particles in cellular processes. J Cell Biol 106:1419-1425.
    • (1988) J Cell Biol , vol.106 , pp. 1419-1425
    • Dreyfuss, G.1    Philipson, L.2    Mattaj, I.W.3
  • 6
    • 0032808053 scopus 로고    scopus 로고
    • Trophinin, tastin, and bystin: A complex mediating unique attachment between trophoblastic and endometrial epithelial cells at their respective apical cell membranes
    • Fukuda MN, Nozawa S. 1999. Trophinin, tastin, and bystin: A complex mediating unique attachment between trophoblastic and endometrial epithelial cells at their respective apical cell membranes. Semin Reprod Endocrinol 17:229-234.
    • (1999) Semin Reprod Endocrinol , vol.17 , pp. 229-234
    • Fukuda, M.N.1    Nozawa, S.2
  • 7
    • 0029002920 scopus 로고
    • Trophinin and tastin, a novel cell adhesion molecule complex with potential involvement in embryo implantation
    • Fukuda MN, Sato T, Nakayama J, Klier G, Mikami M, Aoki D, Nozawa S. 1995. Trophinin and tastin, a novel cell adhesion molecule complex with potential involvement in embryo implantation. Genes Dev 9:1199-1210.
    • (1995) Genes Dev , vol.9 , pp. 1199-1210
    • Fukuda, M.N.1    Sato, T.2    Nakayama, J.3    Klier, G.4    Mikami, M.5    Aoki, D.6    Nozawa, S.7
  • 9
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • He D, Nickerson JA, Penman S. 1990. Core filaments of the nuclear matrix. J Cell Biol 110:569-580.
    • (1990) J Cell Biol , vol.110 , pp. 569-580
    • He, D.1    Nickerson, J.A.2    Penman, S.3
  • 10
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson BR, Eleftheriou A. 2000. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp Cell Res 256:213-224.
    • (2000) Exp Cell Res , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 11
    • 0030997718 scopus 로고    scopus 로고
    • Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets
    • Hirao A, Hamaguchi I, Suda T, Yamaguchi N. 1997. Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets. EMBO J 16:2342-2351.
    • (1997) EMBO J , vol.16 , pp. 2342-2351
    • Hirao, A.1    Hamaguchi, I.2    Suda, T.3    Yamaguchi, N.4
  • 13
    • 2942640590 scopus 로고    scopus 로고
    • Trafficking of Lyn through the Golgi caveolin involves the charged residues on alphaE and alphaI helices in the kinase domain
    • Kasahara K, Nakayama Y, Ikeda K, Fukushima Y, Matsuda D, Horimoto S, Yamaguchi N. 2004. Trafficking of Lyn through the Golgi caveolin involves the charged residues on alphaE and alphaI helices in the kinase domain. J Cell Biol 165:641-652.
    • (2004) J Cell Biol , vol.165 , pp. 641-652
    • Kasahara, K.1    Nakayama, Y.2    Ikeda, K.3    Fukushima, Y.4    Matsuda, D.5    Horimoto, S.6    Yamaguchi, N.7
  • 15
    • 34247094761 scopus 로고    scopus 로고
    • Src signaling regulates completion of abscission in cytokinesis through Erk/MAPK activation at the midbody
    • Kasahara K, Nakayama Y, Nakazato Y, Ikeda K, Kuga T, Yamaguchi N. 2007b. Src signaling regulates completion of abscission in cytokinesis through Erk/MAPK activation at the midbody. J Biol Chem 282:5327-5339.
    • (2007) J Biol Chem , vol.282 , pp. 5327-5339
    • Kasahara, K.1    Nakayama, Y.2    Nakazato, Y.3    Ikeda, K.4    Kuga, T.5    Yamaguchi, N.6
  • 16
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box
    • Kiledjian N, Dreyfuss G. 1992. Primary structure and binding activity of the hnRNP U protein: Binding RNA through RGG box. EMBO J 11:2655-2664.
    • (1992) EMBO J , vol.11 , pp. 2655-2664
    • Kiledjian, N.1    Dreyfuss, G.2
  • 17
    • 0031968122 scopus 로고    scopus 로고
    • The immunogenic properties of melanoma-associated antigens recognized by cytotoxic T lymphocytes
    • Kirkin AF, Dzhandzhugazyan K, Zeuthen J. 1998. The immunogenic properties of melanoma-associated antigens recognized by cytotoxic T lymphocytes. Exp Clin Immunogenet 15:19-32.
    • (1998) Exp Clin Immunogenet , vol.15 , pp. 19-32
    • Kirkin, A.F.1    Dzhandzhugazyan, K.2    Zeuthen, J.3
  • 18
    • 0036829043 scopus 로고    scopus 로고
    • Ectopic expression of necdin induces differentiation of mouse neuroblastoma cells
    • Kobayashi M, Taniura H, Yoshikawa K. 2002. Ectopic expression of necdin induces differentiation of mouse neuroblastoma cells. J Biol Chem 277:42128-42135.
    • (2002) J Biol Chem , vol.277 , pp. 42128-42135
    • Kobayashi, M.1    Taniura, H.2    Yoshikawa, K.3
  • 19
    • 0347087481 scopus 로고    scopus 로고
    • Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor
    • Kuwako K, Taniura H, Yoshikawa K. 2004. Necdin-related MAGE proteins differentially interact with the E2F1 transcription factor and the p75 neurotrophin receptor. J Biol Chem 279:1703-1712.
    • (2004) J Biol Chem , vol.279 , pp. 1703-1712
    • Kuwako, K.1    Taniura, H.2    Yoshikawa, K.3
  • 20
    • 0033566760 scopus 로고    scopus 로고
    • A new MAGE gene with ubiquitous expression does not code for known MAGE antigens recognized by T cells
    • Lucas S, Brasseur F, Boon T. 1999. A new MAGE gene with ubiquitous expression does not code for known MAGE antigens recognized by T cells. Cancer Res 59:4100-4103.
    • (1999) Cancer Res , vol.59 , pp. 4100-4103
    • Lucas, S.1    Brasseur, F.2    Boon, T.3
  • 21
    • 0025871554 scopus 로고
    • A novel brain-specific mRNA encoding nuclear protein (necdin) expressed in neurally differentiated embryonal carcinoma cells
    • Maruyama K, Usami M, Aizawa T, Yoshikawa K. 1991. A novel brain-specific mRNA encoding nuclear protein (necdin) expressed in neurally differentiated embryonal carcinoma cells. Biochem Biophys Res Commun 178:291-296.
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 291-296
    • Maruyama, K.1    Usami, M.2    Aizawa, T.3    Yoshikawa, K.4
  • 22
    • 0035895892 scopus 로고    scopus 로고
    • Dlxin-1, a novel protein that binds Dlx5 and regulates its transcriptional function
    • Masuda Y, Sasaki A, Shibuya H, Ueno N, Ikeda K, Watanabe K. 2001. Dlxin-1, a novel protein that binds Dlx5 and regulates its transcriptional function. J Biol Chem 276:5331-5338.
    • (2001) J Biol Chem , vol.276 , pp. 5331-5338
    • Masuda, Y.1    Sasaki, A.2    Shibuya, H.3    Ueno, N.4    Ikeda, K.5    Watanabe, K.6
  • 23
    • 33645243620 scopus 로고    scopus 로고
    • Involvement of Golgi-associated Lyn tyrosine kinase in the translocation of annexin II to the endoplasmic reticulum under oxidative stress
    • Matsuda D, Nakayama Y, Horimoto S, Kuga T, Ikeda K, Kasahara K, Yamaguchi N. 2006. Involvement of Golgi-associated Lyn tyrosine kinase in the translocation of annexin II to the endoplasmic reticulum under oxidative stress. Exp Cell Res 312:1205-1217.
    • (2006) Exp Cell Res , vol.312 , pp. 1205-1217
    • Matsuda, D.1    Nakayama, Y.2    Horimoto, S.3    Kuga, T.4    Ikeda, K.5    Kasahara, K.6    Yamaguchi, N.7
  • 24
    • 0033060256 scopus 로고    scopus 로고
    • Induction of cell shape changes through activation of the interleukin-3 common beta chain receptor by the RON receptor-type tyrosine kinase
    • Mera A, Suga M, Ando M, Suda T, Yamaguchi N. 1999. Induction of cell shape changes through activation of the interleukin-3 common beta chain receptor by the RON receptor-type tyrosine kinase. J Biol Chem 274:15766-15774.
    • (1999) J Biol Chem , vol.274 , pp. 15766-15774
    • Mera, A.1    Suga, M.2    Ando, M.3    Suda, T.4    Yamaguchi, N.5
  • 25
    • 0036154922 scopus 로고    scopus 로고
    • Significant differences between mouse and human trophinins are revealed by their expression patterns and targeted disruption of mouse trophinin gene
    • Nadano D, Sugihara K, Paria BC, Saburi S, Copeland NG, Gilbert DJ, Jenkins NA, Nakayama J, Fukuda MN. 2002. Significant differences between mouse and human trophinins are revealed by their expression patterns and targeted disruption of mouse trophinin gene. Biol Reprod 66:313-321.
    • (2002) Biol Reprod , vol.66 , pp. 313-321
    • Nadano, D.1    Sugihara, K.2    Paria, B.C.3    Saburi, S.4    Copeland, N.G.5    Gilbert, D.J.6    Jenkins, N.A.7    Nakayama, J.8    Fukuda, M.N.9
  • 26
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K, Horton P. 1999. PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci 24:34-36.
    • (1999) Trends Biochem Sci , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 27
    • 14644433076 scopus 로고    scopus 로고
    • Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase
    • Nakayama Y, Yamaguchi N. 2005. Multi-lobulation of the nucleus in prolonged S phase by nuclear expression of Chk tyrosine kinase. Exp Cell Res 304:570-581.
    • (2005) Exp Cell Res , vol.304 , pp. 570-581
    • Nakayama, Y.1    Yamaguchi, N.2
  • 29
    • 33745226964 scopus 로고    scopus 로고
    • Involvement of the N-terminal unique domain of Chk tyrosine kinase in Chk-induced tyrosine phosphorylation in the nucleus
    • Nakayama Y, Kawana A, Igarashi A, Yamaguchi N. 2006. Involvement of the N-terminal unique domain of Chk tyrosine kinase in Chk-induced tyrosine phosphorylation in the nucleus. Exp Cell Res 312:2252-2263.
    • (2006) Exp Cell Res , vol.312 , pp. 2252-2263
    • Nakayama, Y.1    Kawana, A.2    Igarashi, A.3    Yamaguchi, N.4
  • 30
    • 0031424029 scopus 로고    scopus 로고
    • Assignment of trophoblast/endometrial epithelium cell adhesion molecule trophinin gene TRO to human chromosome bands Xp11.22 → p11.21 by in situ hybridization
    • Pack SD, Tanigami A, Ledbetter DH, Sato T, Fukuda MN. 1997. Assignment of trophoblast/endometrial epithelium cell adhesion molecule trophinin gene TRO to human chromosome bands Xp11.22 → p11.21 by in situ hybridization. Cytogenet Cell Genet 79:123-124.
    • (1997) Cytogenet Cell Genet , vol.79 , pp. 123-124
    • Pack, S.D.1    Tanigami, A.2    Ledbetter, D.H.3    Sato, T.4    Fukuda, M.N.5
  • 31
    • 0026737332 scopus 로고
    • Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements
    • Romig H, Fackelmayer FO, Renz A, Ramsperger U, Richter A. 1992. Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements. EMBO J 11:3431-3440.
    • (1992) EMBO J , vol.11 , pp. 3431-3440
    • Romig, H.1    Fackelmayer, F.O.2    Renz, A.3    Ramsperger, U.4    Richter, A.5
  • 32
    • 0035966108 scopus 로고    scopus 로고
    • The trophinin gene encodes a novel group of MAGE proteins, magphinins, and regulates cell proliferation during gametogenesis in the mouse
    • Saburi S, Nadano D, Akama TO, Hirama K, Yamanouchi K, Naito K, Tojo H, Tachi C, Fukuda MN. 2001. The trophinin gene encodes a novel group of MAGE proteins, magphinins, and regulates cell proliferation during gametogenesis in the mouse. J Biol Chem 276:49378-49389.
    • (2001) J Biol Chem , vol.276 , pp. 49378-49389
    • Saburi, S.1    Nadano, D.2    Akama, T.O.3    Hirama, K.4    Yamanouchi, K.5    Naito, K.6    Tojo, H.7    Tachi, C.8    Fukuda, M.N.9
  • 33
    • 0033695190 scopus 로고    scopus 로고
    • NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin receptor and facilitates nerve growth factor-dependent apoptosis
    • Salehi AH, Roux PP, Kubu CJ, Zeindler C, Bhakar A, Tannis LL, Verdi JM, Barker PA. 2000. NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin receptor and facilitates nerve growth factor-dependent apoptosis. Neuron 27:279-288.
    • (2000) Neuron , vol.27 , pp. 279-288
    • Salehi, A.H.1    Roux, P.P.2    Kubu, C.J.3    Zeindler, C.4    Bhakar, A.5    Tannis, L.L.6    Verdi, J.M.7    Barker, P.A.8
  • 34
    • 0037151106 scopus 로고    scopus 로고
    • A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1
    • Sasaki A, Masuda Y, Iwai K, Ikeda K, Watanabe K. 2002. A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1. J Biol Chem 277:22541-22546.
    • (2002) J Biol Chem , vol.277 , pp. 22541-22546
    • Sasaki, A.1    Masuda, Y.2    Iwai, K.3    Ikeda, K.4    Watanabe, K.5
  • 37
    • 0032574706 scopus 로고    scopus 로고
    • A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin mediated cell adhesion between trophoblast and endometrial epithelial cells
    • Suzuki N, Zara J, Sato T, Ong E, Bakhiet N, Oshima RG, Watson KL, Fukuda MN. 1998. A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin mediated cell adhesion between trophoblast and endometrial epithelial cells. Proc Natl Acad Sci USA 95:5027-5032.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5027-5032
    • Suzuki, N.1    Zara, J.2    Sato, T.3    Ong, E.4    Bakhiet, N.5    Oshima, R.G.6    Watson, K.L.7    Fukuda, M.N.8
  • 38
    • 0033152305 scopus 로고    scopus 로고
    • A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucin CD34 and CD43 in immature hematopoietic cells
    • Tada J, Omine M, Suda T, Yamaguchi N. 1999. A common signaling pathway via Syk and Lyn tyrosine kinases generated from capping of the sialomucin CD34 and CD43 in immature hematopoietic cells. Blood 93:3723-3735.
    • (1999) Blood , vol.93 , pp. 3723-3735
    • Tada, J.1    Omine, M.2    Suda, T.3    Yamaguchi, N.4
  • 39
    • 0034644744 scopus 로고    scopus 로고
    • The postmitotic growth suppressor necdin interacts with a calcium-binding protein (NEFA) in neuronal cytoplasm
    • Taniguchi N, Taniura H, Niinobe M, Takayama C, Tominaga-Yoshino K, Ogura A, Yoshikawa K. 2000. The postmitotic growth suppressor necdin interacts with a calcium-binding protein (NEFA) in neuronal cytoplasm. J Biol Chem 275:31674-31681.
    • (2000) J Biol Chem , vol.275 , pp. 31674-31681
    • Taniguchi, N.1    Taniura, H.2    Niinobe, M.3    Takayama, C.4    Tominaga-Yoshino, K.5    Ogura, A.6    Yoshikawa, K.7
  • 40
    • 0035703108 scopus 로고    scopus 로고
    • Necdin interacts with the ribonucleoprotein hnRNP U in the nuclear matrix
    • Taniura H, Yoshikawa K. 2002. Necdin interacts with the ribonucleoprotein hnRNP U in the nuclear matrix. J Cell Biochem 84:545-555.
    • (2002) J Cell Biochem , vol.84 , pp. 545-555
    • Taniura, H.1    Yoshikawa, K.2
  • 41
    • 0031964697 scopus 로고    scopus 로고
    • Necdin, a postmitotic neuron-specific growth suppressor, interacts with viral transforming proteins and cellular transcription factor E2 F1
    • Taniura H, Taniguchi N, Hara M, Yoshikawa K. 1998. Necdin, a postmitotic neuron-specific growth suppressor, interacts with viral transforming proteins and cellular transcription factor E2 F1. J Biol Chem 273:720-728.
    • (1998) J Biol Chem , vol.273 , pp. 720-728
    • Taniura, H.1    Taniguchi, N.2    Hara, M.3    Yoshikawa, K.4
  • 42
    • 0033522919 scopus 로고    scopus 로고
    • Physical and functional interactions of neuronal growth suppressor necdin with p53
    • Taniura H, Matsumoto K, Yoshikawa K. 1999. Physical and functional interactions of neuronal growth suppressor necdin with p53. J Biol Chem 274:16242-16248.
    • (1999) J Biol Chem , vol.274 , pp. 16242-16248
    • Taniura, H.1    Matsumoto, K.2    Yoshikawa, K.3
  • 43
    • 20444395224 scopus 로고    scopus 로고
    • Functional domains of necdin for protein-protein interaction, nuclear matrix targeting, and cell growth suppression
    • Taniura H, Kobayashi M, Yoshikawa K. 2005. Functional domains of necdin for protein-protein interaction, nuclear matrix targeting, and cell growth suppression. J Cell Biochem 94:804-815.
    • (2005) J Cell Biochem , vol.94 , pp. 804-815
    • Taniura, H.1    Kobayashi, M.2    Yoshikawa, K.3
  • 45
    • 0029067675 scopus 로고
    • Golgi retention mechanism of β-1,4-galactosyltransferase: Membrane-spanning domain-dependent homodimerization and association with α- and β-tubulins
    • Yamaguchi N, Fukuda MN. 1995. Golgi retention mechanism of β-1,4-galactosyltransferase: Membrane-spanning domain-dependent homodimerization and association with α- and β-tubulins. J Biol Chem 270:12170-12176.
    • (1995) J Biol Chem , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 46
    • 0035020726 scopus 로고    scopus 로고
    • Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: A possible role for chromosome-associated Chk in chromosome dynamics
    • Yamaguchi N, Nakayama Y, Urakami T, Suzuki S, Nakamura T, Suda T, Oku N. 2001. Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: A possible role for chromosome-associated Chk in chromosome dynamics. J Cell Sci 114:1631-1641.
    • (2001) J Cell Sci , vol.114 , pp. 1631-1641
    • Yamaguchi, N.1    Nakayama, Y.2    Urakami, T.3    Suzuki, S.4    Nakamura, T.5    Suda, T.6    Oku, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.