메뉴 건너뛰기




Volumn 10, Issue 12, 2010, Pages 2337-2347

Proteomic analysis reveals novel binding partners of MIP-T3 in human cells

Author keywords

Actin; Cell biology; HSPA8; Interacting proteins; MIP T3

Indexed keywords

ACTIN; ALPHA TUBULIN; BINDING PROTEIN; CHAPERONE; MICROTUBULE PROTEIN; NUCLEIC ACID; PHOSPHOTRANSFERASE; PROTEIN HSPA8; PROTEIN MIP T3; TUBULIN; UNCLASSIFIED DRUG;

EID: 77953844836     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000130     Document Type: Article
Times cited : (14)

References (46)
  • 1
    • 0034604714 scopus 로고    scopus 로고
    • MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network
    • DOI 10.1074/jbc.M001095200
    • Ling, L., Goeddel, D. V., MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network. J. Biol. Chem. 2000, 275, 23852-23860. (Pubitemid 30624672)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 23852-23860
    • Ling, L.1    Goeddel, D.V.2
  • 2
    • 0037766786 scopus 로고    scopus 로고
    • DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: Regulation and loss of interaction with mutation
    • DOI 10.1093/hmg/ddg162
    • Morris, J. A., Kandpal, G., Ma, L., Austin, C. P., DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. Hum. Mol. Genet. 2003, 12, 1591-1608. (Pubitemid 36857306)
    • (2003) Human Molecular Genetics , vol.12 , Issue.13 , pp. 1591-1608
    • Morris, J.A.1    Kandpal, G.2    Ma, L.3    Austin, C.P.4
  • 3
    • 62149083806 scopus 로고    scopus 로고
    • Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation via modulation of GSK3beta/beta-catenin signaling
    • Mao, Y., Ge, X., Frank, C. L., Madison, J. M. et al., Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation via modulation of GSK3beta/beta-catenin signaling. Cell 2009, 136, 1017-1031.
    • (2009) Cell , vol.136 , pp. 1017-1031
    • Mao, Y.1    Ge, X.2    Frank, C.L.3    Madison, J.M.4
  • 5
    • 41949085600 scopus 로고    scopus 로고
    • An essential role for DYF-11/MIP-T3 in assembling functional intraflagellar transport complexes
    • Li, C., Inglis, P. N., Leitch, C. C., Efimenko, E. et al., An essential role for DYF-11/MIP-T3 in assembling functional intraflagellar transport complexes. PLoS Genet. 2008, 4, e1000044.
    • (2008) PLoS Genet. , vol.4
    • Li, C.1    Inglis, P.N.2    Leitch, C.C.3    Efimenko, E.4
  • 6
    • 34248214629 scopus 로고    scopus 로고
    • Sensory ciliogenesis in Caenorhabditis elegans: Assignment of IFT components into distinct modules based on transport and phenotypic profiles
    • Ou, G., Koga, M., Blacque, O. E., Murayama, T. et al., Sensory ciliogenesis in Caenorhabditis elegans: assignment of IFT components into distinct modules based on transport and phenotypic profiles. Mol. Biol. Cell 2007, 18, 1554-1569.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1554-1569
    • Ou, G.1    Koga, M.2    Blacque, O.E.3    Murayama, T.4
  • 7
    • 43149102968 scopus 로고    scopus 로고
    • Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8
    • Omori, Y., Zhao, C., Saras, A., Mukhopadhyay, S. et al., Elipsa is an early determinant of ciliogenesis that links the IFT particle to membrane-associated small GTPase Rab8. Nat. Cell Biol. 2008, 10, 437-444.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 437-444
    • Omori, Y.1    Zhao, C.2    Saras, A.3    Mukhopadhyay, S.4
  • 11
    • 2342501364 scopus 로고    scopus 로고
    • Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene
    • Li, J. B., Gerdes, J. M., Haycraft, C. J., Fan, Y. et al., Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene. Cell 2004, 117, 541-552.
    • (2004) Cell , vol.117 , pp. 541-552
    • Li, J.B.1    Gerdes, J.M.2    Haycraft, C.J.3    Fan, Y.4
  • 12
    • 2342657884 scopus 로고    scopus 로고
    • Decoding cilia function: Defining specialized genes required for compartmentalized cilia biogenesis
    • DOI 10.1016/S0092-8674(04)00412-X, PII S009286740400412X
    • Avidor-Reiss, T., Maer, A. M., Koundakjian, E., Polyanovsky, A. et al., Decoding cilia function: defining specialized genes required for compartmentalized cilia biogenesis. Cell 2004, 117, 527-539. (Pubitemid 38610237)
    • (2004) Cell , vol.117 , Issue.4 , pp. 527-539
    • Avidor-Reiss, T.1    Maer, A.M.2    Koundakjian, E.3    Polyanovsky, A.4    Keil, T.5    Subramaniam, S.6    Zuker, C.S.7
  • 13
    • 33745496759 scopus 로고    scopus 로고
    • The Emerging Complexity of the Vertebrate Cilium: New Functional Roles for an Ancient Organelle
    • DOI 10.1016/j.devcel.2006.06.009, PII S1534580706002772
    • Davis, E. E., Brueckner, M., Katsanis, N., The emerging complexity of the vertebrate cilium: new functional roles for an ancient organelle. Dev. Cell 2006, 11, 9-19. (Pubitemid 43960809)
    • (2006) Developmental Cell , vol.11 , Issue.1 , pp. 9-19
    • Davis, E.E.1    Brueckner, M.2    Katsanis, N.3
  • 14
    • 20944435539 scopus 로고    scopus 로고
    • Inversin, the gene product mutated in nephronophthisis type II, functions as a molecular switch between Wnt signaling pathways
    • Simons, M., Gloy, J., Ganner, A., Bullerkotte, A. et al., Inversin, the gene product mutated in nephronophthisis type II, functions as a molecular switch between Wnt signaling pathways. Nat. Genet. 2005, 37, 537-543.
    • (2005) Nat. Genet. , vol.37 , pp. 537-543
    • Simons, M.1    Gloy, J.2    Ganner, A.3    Bullerkotte, A.4
  • 15
    • 35648985644 scopus 로고    scopus 로고
    • Disruption of the basal body compromises proteasomal function and perturbs intracellular Wnt response
    • Gerdes, J. M., Liu, Y., Zaghloul, N. A., Leitch, C. C. et al., Disruption of the basal body compromises proteasomal function and perturbs intracellular Wnt response. Nat. Genet. 2007, 39, 1350-1360.
    • (2007) Nat. Genet. , vol.39 , pp. 1350-1360
    • Gerdes, J.M.1    Liu, Y.2    Zaghloul, N.A.3    Leitch, C.C.4
  • 16
    • 0042622356 scopus 로고    scopus 로고
    • Disrupted-In-Schizophrenia 1, a candidate gene for schizophrenia, participates in neurite outgrowth
    • Miyoshi, K., Honda, A., Baba, K., Taniguchi, M. et al., Disrupted-In-Schizophrenia 1, a candidate gene for schizophrenia, participates in neurite outgrowth. Mol. Psychiatry 2003, 8, 685-694.
    • (2003) Mol. Psychiatry , vol.8 , pp. 685-694
    • Miyoshi, K.1    Honda, A.2    Baba, K.3    Taniguchi, M.4
  • 17
    • 14644391578 scopus 로고    scopus 로고
    • Essential role for the Prader-Willi syndrome protein necdin in axonal outgrowth
    • Lee, S., Walker, C. L., Karten, B., Kuny, S. L. et al., Essential role for the Prader-Willi syndrome protein necdin in axonal outgrowth. Hum. Mol. Genet. 2005, 14, 627-637.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 627-637
    • Lee, S.1    Walker, C.L.2    Karten, B.3    Kuny, S.L.4
  • 18
    • 0142134225 scopus 로고    scopus 로고
    • MIP-T3 associates with IL-13Ralpha1 and suppresses STAT6 activation in response to IL-13 stimulation
    • Niu, Y., Murata, T., Watanabe, K., Kawakami, K. et al., MIP-T3 associates with IL-13Ralpha1 and suppresses STAT6 activation in response to IL-13 stimulation. FEBS Lett. 2003, 550, 139-143.
    • (2003) FEBS Lett. , vol.550 , pp. 139-143
    • Niu, Y.1    Murata, T.2    Watanabe, K.3    Kawakami, K.4
  • 19
    • 35848955168 scopus 로고    scopus 로고
    • Mass spectrometry-based functional proteomics: From molecular machines to protein networks
    • Kocher, T., Superti-Furga, G., Mass spectrometry-based functional proteomics: from molecular machines to protein networks. Nat. Methods 2007, 4, 807-815.
    • (2007) Nat. Methods , vol.4 , pp. 807-815
    • Kocher, T.1    Superti-Furga, G.2
  • 20
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., Yamamura, K., Miyazaki, J., Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 1991, 108, 193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 22
    • 33846067524 scopus 로고    scopus 로고
    • PANTHER version 6: Protein sequence and function evolution data with expanded representation of biological pathways
    • Mi, H., Guo, N., Kejariwal, A., Thomas, P. D., PANTHER version 6: protein sequence and function evolution data with expanded representation of biological pathways. Nucleic Acids Res. 2007, 35, D247-D252.
    • (2007) Nucleic Acids Res. , vol.35
    • Mi, H.1    Guo, N.2    Kejariwal, A.3    Thomas, P.D.4
  • 23
    • 0242559054 scopus 로고    scopus 로고
    • Pathway studio - The analysis and navigation of molecular networks
    • DOI 10.1093/bioinformatics/btg290
    • Nikitin, A., Egorov, S., Daraselia, N., Mazo, I., Pathway studio - the analysis and navigation of molecular networks. Bioinformatics 2003, 19, 2155-2157. (Pubitemid 37408171)
    • (2003) Bioinformatics , vol.19 , Issue.16 , pp. 2155-2157
    • Nikitin, A.1    Egorov, S.2    Daraselia, N.3    Mazo, I.4
  • 24
    • 67049115481 scopus 로고    scopus 로고
    • Proteomic and functional analyses reveal a dual molecular mechanism underlying arsenic-induced apoptosis in human multiple myeloma cells
    • Ge, F., Lu, X. P., Zeng, H. L., He, Q. Y. et al., Proteomic and functional analyses reveal a dual molecular mechanism underlying arsenic-induced apoptosis in human multiple myeloma cells. J. Proteome Res. 2009, 8, 3006-3019.
    • (2009) J. Proteome Res. , vol.8 , pp. 3006-3019
    • Ge, F.1    Lu, X.P.2    Zeng, H.L.3    He, Q.Y.4
  • 25
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • DOI 10.1111/j.1365-2818.2006.01706.x
    • Bolte, S., Cordelieres, F. P., A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 2006, 224, 213-232. (Pubitemid 46010930)
    • (2006) Journal of Microscopy , vol.224 , Issue.3 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 26
    • 2942642590 scopus 로고    scopus 로고
    • Automatic and quantitative measurement of protein-protein colocalization in live cells
    • DOI 10.1529/biophysj.103.038422
    • Costes, S. V., Daelemans, D., Cho, E. H., Dobbin, Z. et al., Automatic and quantitative measurement of protein-protein colocalization in live cells. Biophys. J. 2004, 86, 3993-4003. (Pubitemid 38780275)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3993-4003
    • Costes, S.V.1    Daelemans, D.2    Cho, E.H.3    Dobbin, Z.4    Pavlakis, G.5    Lockett, S.6
  • 27
    • 70450208789 scopus 로고    scopus 로고
    • Actin and microtubule cytoskeleton interactions
    • Petrasek, J., Schwarzerova, K., Actin and microtubule cytoskeleton interactions. Curr. Opin. Plant Biol. 2009, 12, 728-734.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 728-734
    • Petrasek, J.1    Schwarzerova, K.2
  • 28
    • 0345627979 scopus 로고    scopus 로고
    • The interaction of Mip-90 with microtubules and actin filaments in human fibroblasts
    • Gonzalez, M., Cambiazo, V., Maccioni, R. B., The interaction of Mip-90 with microtubules and actin filaments in human fibroblasts. Exp. Cell Res. 1998, 239, 243-253.
    • (1998) Exp. Cell Res. , vol.239 , pp. 243-253
    • Gonzalez, M.1    Cambiazo, V.2    Maccioni, R.B.3
  • 29
    • 0027173094 scopus 로고
    • A tau-like protein interacts with stress fibers and microtubules in human and rodent cultured cell lines
    • Cross, D., Vial, C., Maccioni, R. B., A tau-like protein interacts with stress fibers and microtubules in human and rodent cultured cell lines. J. Cell Sci. 1993, 105, 51-60. (Pubitemid 23187545)
    • (1993) Journal of Cell Science , vol.105 , Issue.1 , pp. 51-60
    • Cross, D.1    Vial, C.2    Maccioni, R.B.3
  • 30
    • 0028942256 scopus 로고
    • Actin- And microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford, G. M., Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol. 1995, 7, 82-88.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 31
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • DOI 10.1016/S0955-0674(99)00058-7
    • Goode, B. L., Drubin, D. G., Barnes, G., Functional cooperation between the microtubule and actin cytoskeletons. Curr. Opin. Cell Biol. 2000, 12, 63-71. (Pubitemid 30095271)
    • (2000) Current Opinion in Cell Biology , vol.12 , Issue.1 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 32
    • 56149117515 scopus 로고    scopus 로고
    • Actin-targeting natural compounds as tools to study the role of actin cytoskeleton in signal transduction
    • Kustermans, G., Piette, J., Legrand-Poels, S., Actin-targeting natural compounds as tools to study the role of actin cytoskeleton in signal transduction. Biochem. Pharmacol. 2008, 76, 1310-1322.
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1310-1322
    • Kustermans, G.1    Piette, J.2    Legrand-Poels, S.3
  • 33
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas, J., Zhao, H., Lappalainen, P., Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol. Rev. 2010, 90, 259-289.
    • (2010) Physiol. Rev. , vol.90 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.2    Lappalainen, P.3
  • 35
    • 0032223791 scopus 로고    scopus 로고
    • Influence of phospholipids and sequential kinase activities on TAU in vitro
    • Shea, T. B., Ekinci, F. J., Influence of phospholipids and sequential kinase activities on tau in vitro. Adv. Exp. Med. Biol. 1998, 446, 181-201. (Pubitemid 128701737)
    • (1998) Advances in Experimental Medicine and Biology , vol.446 , pp. 181-201
    • Shea, T.B.1    Ekinci, F.J.2
  • 36
    • 0033005733 scopus 로고    scopus 로고
    • Accessory protein regulation of microtubule dynamics throughout the cell cycle
    • DOI 10.1016/S0955-0674(99)80017-9
    • Cassimeris, L., Accessory protein regulation of microtubule dynamics throughout the cell cycle. Curr. Opin. Cell Biol. 1999, 11, 134-141. (Pubitemid 29084142)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.1 , pp. 134-141
    • Cassimeris, L.1
  • 37
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • DOI 10.1021/bi800639z
    • Vos, M. J., Hageman, J., Carra, S., Kampinga, H. H., Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 2008, 47, 7001-7011. (Pubitemid 351956349)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 38
    • 34250871853 scopus 로고    scopus 로고
    • All in the family: Atypical Hsp70 chaperones are conserved modulators of Hsp70 activity
    • Shaner, L., Morano, K. A., All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity. Cell Stress Chaperones 2007, 12, 1-8.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 1-8
    • Shaner, L.1    Morano, K.A.2
  • 39
    • 76349117689 scopus 로고    scopus 로고
    • Structure of clathrin coat with bound Hsc70 and auxilin: Mechanism of Hsc70-facilitated disassembly
    • Xing, Y., Bocking, T., Wolf, M., Grigorieff, N. et al., Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly. EMBO J. 2010, 29, 655-665.
    • (2010) EMBO J. , vol.29 , pp. 655-665
    • Xing, Y.1    Bocking, T.2    Wolf, M.3    Grigorieff, N.4
  • 40
    • 73849088641 scopus 로고    scopus 로고
    • Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells
    • Nirde, P., Derocq, D., Maynadier, M., Chambon, M. et al., Heat shock cognate 70 protein secretion as a new growth arrest signal for cancer cells. Oncogene 2010, 29, 117-127.
    • (2010) Oncogene , vol.29 , pp. 117-127
    • Nirde, P.1    Derocq, D.2    Maynadier, M.3    Chambon, M.4
  • 41
    • 70449701828 scopus 로고    scopus 로고
    • Deletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperone
    • Scott-Ward, T. S., Amaral, M. D., Deletion of Phe508 in the first nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator increases its affinity for the heat shock cognate 70 chaperone. FEBS J. 2009, 276, 7097-7109.
    • (2009) FEBS J. , vol.276 , pp. 7097-7109
    • Scott-Ward, T.S.1    Amaral, M.D.2
  • 43
    • 0026779422 scopus 로고
    • Interaction of heat-shock protein 70 with p53 translated in vitro: Evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation
    • Hainaut, P., Milner, J., Interaction of heat-shock protein 70 with p53 translated in vitro: evidence for interaction with dimeric p53 and for a role in the regulation of p53 conformation. EMBO J. 1992, 11, 3513-3520.
    • (1992) EMBO J. , vol.11 , pp. 3513-3520
    • Hainaut, P.1    Milner, J.2
  • 44
    • 70350547754 scopus 로고    scopus 로고
    • Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth
    • Sharp, A., Cutress, R. I., Johnson, P. W., Packham, G., Townsend, P. A., Short peptides derived from the BAG-1 C-terminus inhibit the interaction between BAG-1 and HSC70 and decrease breast cancer cell growth. FEBS Lett. 2009, 583, 3405-3411.
    • (2009) FEBS Lett. , vol.583 , pp. 3405-3411
    • Sharp, A.1    Cutress, R.I.2    Johnson, P.W.3    Packham, G.4    Townsend, P.A.5
  • 45
    • 64249125928 scopus 로고    scopus 로고
    • Mitochondrial carrier protein biogenesis: Role of the chaperones Hsc70 and Hsp90
    • Zara, V., Ferramosca, A., Robitaille-Foucher, P., Palmieri, F., Young, J. C., Mitochondrial carrier protein biogenesis: role of the chaperones Hsc70 and Hsp90. Biochem. J. 2009, 419, 369-375.
    • (2009) Biochem. J. , vol.419 , pp. 369-375
    • Zara, V.1    Ferramosca, A.2    Robitaille-Foucher, P.3    Palmieri, F.4    Young, J.C.5
  • 46
    • 0028965273 scopus 로고
    • Partner proteins determine multiple functions of Hsp70
    • Rassow, J., Voos, W., Pfanner, N., Partner proteins determine multiple functions of Hsp70. Trends Cell Biol. 1995, 5, 207-212.
    • (1995) Trends Cell Biol. , vol.5 , pp. 207-212
    • Rassow, J.1    Voos, W.2    Pfanner, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.