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Volumn 40, Issue 3, 2008, Pages 231-240

HBP21: A novel member of TPR motif family, as a potential chaperone of heat shock protein 70 in proliferative vitreoretinopathy (PVR) and breast cancer

Author keywords

HBP21; Heat shock protein70; Protein interaction; Tetratricopeptide repeats

Indexed keywords

AMINES; AMINO ACIDS; ELECTRIC GROUNDING; HYBRID COMPUTERS; ORGANIC ACIDS; YEAST;

EID: 62349132785     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12033-008-9080-5     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 0035887167 scopus 로고    scopus 로고
    • Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins
    • 10.1042/0264-6021:3590419
    • W Shinjen L Fuhwa H Suming 2001 Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins Biochemical Journal 359 419 426 10.1042/0264-6021:3590419
    • (2001) Biochemical Journal , vol.359 , pp. 419-426
    • Shinjen, W.1    Fuhwa, L.2    Suming, H.3
  • 2
    • 0033607515 scopus 로고    scopus 로고
    • Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats
    • 10.1074/jbc.274.48.34425
    • FH Liu SJ Wu SM Hu CD Hsiao C Wang 1999 Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats Journal of Biological Chemistry 274 34425 34432 10.1074/jbc.274.48.34425
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 34425-34432
    • Liu, F.H.1    Wu, S.J.2    Hu, S.M.3    Hsiao, C.D.4    Wang, C.5
  • 3
    • 33644500163 scopus 로고    scopus 로고
    • Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure
    • 10.1110/ps.051810106
    • PE Carrigan LA Sikkink F David 2006 Domain:domain interactions within Hop, the Hsp70/Hsp90 organizing protein, are required for protein stability and structure Protein Science 15 522 532 10.1110/ps.051810106
    • (2006) Protein Science , vol.15 , pp. 522-532
    • Carrigan, P.E.1    Sikkink, L.A.2    David, F.3
  • 4
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
    • 10.1210/me.10.6.682
    • S Chen V Prapapanich 1996 Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 Molecular Endocrinology (Baltimore, MD) 10 682 693 10.1210/me.10.6.682
    • (1996) Molecular Endocrinology (Baltimore, MD) , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2
  • 5
    • 0033575232 scopus 로고    scopus 로고
    • Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90
    • 10.1074/jbc.274.29.20060
    • LC Russell SR Whitt MS Chen M Chinkers 1999 Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90 Journal of Biological Chemistry 274 20060 20063 10.1074/jbc.274.29.20060
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 20060-20063
    • Russell, L.C.1    Whitt, S.R.2    Chen, M.S.3    Chinkers, M.4
  • 6
    • 0034625327 scopus 로고    scopus 로고
    • Overlapping sites of tetratricopeptide repeat protein binding and chaperone activity in heat shock protein 90
    • 10.1074/jbc.M001625200
    • AJ Ramsey LC Russell SR Whitt 2000 Overlapping sites of tetratricopeptide repeat protein binding and chaperone activity in heat shock protein 90 Journal of Biological Chemistry 275 17857 17862 10.1074/jbc.M001625200
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 17857-17862
    • Ramsey, A.J.1    Russell, L.C.2    Whitt, S.R.3
  • 7
    • 0037470073 scopus 로고    scopus 로고
    • Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction
    • 10.1074/jbc.M206867200
    • OO Odunuga JA Hornby C Bies 2003 Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction Journal of Biological Chemistry 9 6896 6904 10.1074/jbc.M206867200
    • (2003) Journal of Biological Chemistry , vol.9 , pp. 6896-6904
    • Odunuga, O.O.1    Hornby, J.A.2    Bies, C.3
  • 8
    • 34447281117 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of FKB-6, the sole large TPR-containing immunophilin from C. elegans
    • 10.1016/j.bbrc.2007.06.080
    • JM Richardson J Dornan M Opamawutthikul 2007 Cloning, expression and characterisation of FKB-6, the sole large TPR-containing immunophilin from C. elegans Biochemical and Biophysical Research Communications 360 566 572 10.1016/j.bbrc.2007.06.080
    • (2007) Biochemical and Biophysical Research Communications , vol.360 , pp. 566-572
    • Richardson, J.M.1    Dornan, J.2    Opamawutthikul, M.3
  • 9
    • 33646474760 scopus 로고    scopus 로고
    • A Hsp90beta binding partner, is accumulated in the nucleus during cell apoptosis
    • 10.1016/j.bbrc.2006.03.090
    • H Yin H Wang H Zong 2006 A Hsp90beta binding partner, is accumulated in the nucleus during cell apoptosis Biochemical and Biophysical Research Communications 343 1153 1158 10.1016/j.bbrc.2006.03.090
    • (2006) Biochemical and Biophysical Research Communications , vol.343 , pp. 1153-1158
    • Yin, H.1    Wang, H.2    Zong, H.3
  • 10
    • 0028133445 scopus 로고
    • A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus
    • MX Chen AE McPartlin L Brown YH Chen HM Barker 1994 A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus EMBO Journal 13 4278 4290
    • (1994) EMBO Journal , vol.13 , pp. 4278-4290
    • Chen, M.X.1    McPartlin, A.E.2    Brown, L.3    Chen, Y.H.4    Barker, H.M.5
  • 11
    • 30544453079 scopus 로고    scopus 로고
    • Crystal structure of PilF: Functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa
    • 10.1016/j.bbrc.2005.12.108
    • K Kim J Oh D Han 2006 Crystal structure of PilF: Functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa Biochemical and Biophysical Research Communications 340 1028 1038 10.1016/j.bbrc.2005.12.108
    • (2006) Biochemical and Biophysical Research Communications , vol.340 , pp. 1028-1038
    • Kim, K.1    Oh, J.2    Han, D.3
  • 12
    • 34447540060 scopus 로고    scopus 로고
    • Crystal structure of YrrB: A TPR protein with an unusual peptide-binding site
    • 10.1016/j.bbrc.2007.06.129
    • D Han J Oh K Kim H Lim Y Kim 2007 Crystal structure of YrrB: A TPR protein with an unusual peptide-binding site Biochemical and Biophysical Research Communications 360 784 790 10.1016/j.bbrc.2007.06.129
    • (2007) Biochemical and Biophysical Research Communications , vol.360 , pp. 784-790
    • Han, D.1    Oh, J.2    Kim, K.3    Lim, H.4    Kim, Y.5
  • 13
    • 0027438228 scopus 로고
    • The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59)
    • T Ratajczak A Carrello PJ Mark 1993 The cyclophilin component of the unactivated estrogen receptor contains a tetratricopeptide repeat domain and shares identity with p59 (FKBP59) Journal of Biological Chemistry 268 13187 13192
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 13187-13192
    • Ratajczak, T.1    Carrello, A.2    Mark, P.J.3
  • 14
    • 0027962531 scopus 로고
    • The ability of the immunophilin FKBP59-HBI to interact with the 90 kDa heat shock protein is encoded by its tetratricopeptide repeat domain
    • doi: 10.1073/pnas.91.23.11197
    • Radanyi, C., Chambraud, B., & Baulieu, E. E. (1994). The ability of the immunophilin FKBP59-HBI to interact with the 90 kDa heat shock protein is encoded by its tetratricopeptide repeat domain. Proceedings of the National Academy of Sciences of the United States of America, 91, 11197-11201. doi: 10.1073/pnas.91.23.11197
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , pp. 11197-11201
    • Radanyi, C.1    Chambraud, B.2    Baulieu, E.E.3
  • 15
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • 10.1016/S0092-8674(00)80830-2
    • C Scheufler A Brinker G Bourenkov 2000 Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell 101 199 210 10.1016/S0092-8674(00)80830-2
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3
  • 16
    • 0034141290 scopus 로고    scopus 로고
    • Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs
    • 10.1042/0264-6021:3450645
    • J Van Der Spuy BD Kana HW Dirr GL Blatch 2000 Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs Biochemical Journal 345 645 651 10.1042/0264-6021:3450645
    • (2000) Biochemical Journal , vol.345 , pp. 645-651
    • Van Der Spuy, J.1    Kana, B.D.2    Dirr, H.W.3    Blatch, G.L.4
  • 17
    • 0030050335 scopus 로고    scopus 로고
    • Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding
    • 10.1074/jbc.271.6.2961
    • T Ratajczak Carrello 1996 Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding Journal of Biological Chemistry 271 2961 2965 10.1074/jbc.271.6.2961
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 2961-2965
    • Ratajczak, T.1    Carrello2
  • 19
    • 33646124489 scopus 로고    scopus 로고
    • A testis-specific and testis developmentally regulated tumor protein D52 (TPD52)-like protein TPD52L3/hD55 interacts with TPD52 family proteins
    • 10.1016/j.bbrc.2006.03.208
    • QH Cao J Chen L Zhu Y Liu 2006 A testis-specific and testis developmentally regulated tumor protein D52 (TPD52)-like protein TPD52L3/hD55 interacts with TPD52 family proteins Biochemical and Biophysical Research Communications 344 798 806 10.1016/j.bbrc.2006.03.208
    • (2006) Biochemical and Biophysical Research Communications , vol.344 , pp. 798-806
    • Cao, Q.H.1    Chen, J.2    Zhu, L.3    Liu, Y.4
  • 20
    • 12744273395 scopus 로고    scopus 로고
    • Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole
    • 10.1042/BJ20040690
    • T Zeke N Morrice C Vázquez-Martin PT Cohen 2005 Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole Biochemical Journal 385 45 56 10.1042/BJ20040690
    • (2005) Biochemical Journal , vol.385 , pp. 45-56
    • Zeke, T.1    Morrice, N.2    Vázquez-Martin, C.3    Cohen, P.T.4
  • 22
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • 10.1038/sj.onc.1207529
    • DD Mosser RI Morimoto 2004 Molecular chaperones and the stress of oncogenesis Oncogene 23 2907 2918 10.1038/sj.onc.1207529
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 23
    • 17944366977 scopus 로고    scopus 로고
    • Heat-shock protein 70 antagonizes apoptosis-inducing factor
    • 10.1038/ncb0901-839
    • LS Ravagnan SA Gurbuxani 2001 Heat-shock protein 70 antagonizes apoptosis-inducing factor Nature Cell Biology 3 839 843 10.1038/ncb0901-839
    • (2001) Nature Cell Biology , vol.3 , pp. 839-843
    • Ravagnan, L.S.1    Gurbuxani, S.A.2
  • 24
    • 0034713335 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits caspase-dependent and -independent apoptosis in Jurkat T cells
    • 10.1006/excr.2000.4856
    • EM Creagh RJ Carmody TG Cotter 2000 Heat shock protein 70 inhibits caspase-dependent and -independent apoptosis in Jurkat T cells Experimental Cell Research 257 58 66 10.1006/excr.2000.4856
    • (2000) Experimental Cell Research , vol.257 , pp. 58-66
    • Creagh, E.M.1    Carmody, R.J.2    Cotter, T.G.3
  • 26
    • 33644834999 scopus 로고    scopus 로고
    • Inducible heat shock protein 70 expression as a potential predictive marker of metastasis in breast tumors
    • 10.1379/CSC-159R.1
    • C Torronteguy A Frasson F Zerwes E Winnikov 2006 Inducible heat shock protein 70 expression as a potential predictive marker of metastasis in breast tumors Cell Stress and Chaperones 11 34 43 10.1379/CSC-159R.1
    • (2006) Cell Stress and Chaperones , vol.11 , pp. 34-43
    • Torronteguy, C.1    Frasson, A.2    Zerwes, F.3    Winnikov, E.4
  • 27
    • 0034733644 scopus 로고    scopus 로고
    • Natural resistance of human beta cells toward nitric oxide is mediated by heat shock protein 70
    • 10.1074/jbc.M002265200
    • V Burkart H Liu K Bellmann D Wissing 2000 Natural resistance of human beta cells toward nitric oxide is mediated by heat shock protein 70 Journal of Biological Chemistry 275 19521 19528 10.1074/jbc.M002265200
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 19521-19528
    • Burkart, V.1    Liu, H.2    Bellmann, K.3    Wissing, D.4
  • 28
    • 0035182221 scopus 로고    scopus 로고
    • Stress management-heat shock protein-70 and the regulation of apoptosis
    • 10.1016/S0962-8924(00)01874-2
    • HM Beere DR Green 2000 Stress management-heat shock protein-70 and the regulation of apoptosis Trends in Cell Biology 11 6 10 10.1016/S0962-8924(00) 01874-2
    • (2000) Trends in Cell Biology , vol.11 , pp. 6-10
    • Beere, H.M.1    Green, D.R.2
  • 29
    • 0033546721 scopus 로고    scopus 로고
    • Effects of exposure to repetitive pulsed magnetic stimulation on cell proliferation and expression of heat shock protein 70 in normal and malignant cells
    • 10.1006/bbrc.1999.1110
    • G Tsurita S Ueno NH Tsuno H Nagawa T Muto 1999 Effects of exposure to repetitive pulsed magnetic stimulation on cell proliferation and expression of heat shock protein 70 in normal and malignant cells Biochemical and Biophysical Research Communications 261 689 694 10.1006/bbrc.1999.1110
    • (1999) Biochemical and Biophysical Research Communications , vol.261 , pp. 689-694
    • Tsurita, G.1    Ueno, S.2    Tsuno, N.H.3    Nagawa, H.4    Muto, T.5
  • 31
    • 0034532599 scopus 로고    scopus 로고
    • Suppression of stress kinase JNK is involved in HSP72-mediated protection of myogenic cells from transient energy deprivation:HSP72 alleviates the stress-induced inhibition of JNK dephosphorylation
    • 10.1074/jbc.M006632200
    • VL Gabai AB Meriin JA Yaglom JY Wei DD Mosser MY Sherman 2000 Suppression of stress kinase JNK is involved in HSP72-mediated protection of myogenic cells from transient energy deprivation:HSP72 alleviates the stress-induced inhibition of JNK dephosphorylation Journal of Biological Chemistry 275 38088 38094 10.1074/jbc.M006632200
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 38088-38094
    • Gabai, V.L.1    Meriin, A.B.2    Yaglom, J.A.3    Wei, J.Y.4    Mosser, D.D.5    Sherman, M.Y.6
  • 32
    • 33646384157 scopus 로고    scopus 로고
    • Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation
    • 10.1074/jbc.M513728200
    • K Ruchalski H Mao 2006 Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation Journal of Biological Chemistry 281 7873 7880 10.1074/jbc.M513728200
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 7873-7880
    • Ruchalski, K.1    Mao, H.2
  • 33
    • 4344651318 scopus 로고    scopus 로고
    • Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization
    • 10.1084/jem.20040531
    • J Nylandsted M Gyrd-Hansen AD Anielewicz N Fehrenbacher 2004 Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization Journal of Experimental Medicine 200 425 435 10.1084/jem.20040531
    • (2004) Journal of Experimental Medicine , vol.200 , pp. 425-435
    • Nylandsted, J.1    Gyrd-Hansen, M.2    Anielewicz, A.D.3    Fehrenbacher, N.4
  • 34
    • 21744438271 scopus 로고    scopus 로고
    • C-terminus of heat shock protein 70-interacting protein facilitates degradation of apoptosis signalregulating kinase 1 and inhibits apoptosis signal-regulating kinase 1-dependent apoptosis
    • 10.1379/CSC-90R.1
    • JR Hwang C Zhang 2005 C-terminus of heat shock protein 70-interacting protein facilitates degradation of apoptosis signalregulating kinase 1 and inhibits apoptosis signal-regulating kinase 1-dependent apoptosis Cell Stress and Chaperones 10 147 156 10.1379/CSC-90R.1
    • (2005) Cell Stress and Chaperones , vol.10 , pp. 147-156
    • Hwang, J.R.1    Zhang, C.2
  • 37
    • 0038389383 scopus 로고    scopus 로고
    • Differential, stage-dependent expression of Hsp70, Hsp110 and Bcl-2 in colorectal cancer
    • T. S. Hwang H. S. Han 2003 Differential, stage-dependent expression of Hsp70, Hsp110 and Bcl-2 in colorectal cancer Journal of Gastroenterology and Hepatology 18 690 700
    • (2003) Journal of Gastroenterology and Hepatology , vol.18 , pp. 690-700
    • Hwang, T.S.1    Han, H.S.2
  • 38
    • 0031444439 scopus 로고    scopus 로고
    • Ascorbate affects proliferation of guinea-pig vascular smooth muscle cells by direct and extracellular matrix-mediated effects
    • 10.1006/jmcc.1997.0555
    • VO Ivanov SV Ivanova A Niedzwiecki 1997 Ascorbate affects proliferation of guinea-pig vascular smooth muscle cells by direct and extracellular matrix-mediated effects Journal of Molecular and Cellular Cardiology 29 3293 3303 10.1006/jmcc.1997.0555
    • (1997) Journal of Molecular and Cellular Cardiology , vol.29 , pp. 3293-3303
    • Ivanov, V.O.1    Ivanova, S.V.2    Niedzwiecki, A.3
  • 39
    • 0036784791 scopus 로고    scopus 로고
    • Ribozyme to proliferating cell nuclear antigen to treat proliferative vitreoretinopathy
    • N Mandava P Blackburn 2002 Ribozyme to proliferating cell nuclear antigen to treat proliferative vitreoretinopathy Investigative Ophthalmology and Visual Science 43 3338 3349
    • (2002) Investigative Ophthalmology and Visual Science , vol.43 , pp. 3338-3349
    • Mandava, N.1    Blackburn, P.2
  • 40
    • 0033828125 scopus 로고    scopus 로고
    • Attenuation of experimental proliferative vitreoretinopathy by inhibiting the platelet-derived growth factor receptor
    • Y. Ikuno F.-I. Leong A. Kazlauskas 2000 Attenuation of experimental proliferative vitreoretinopathy by inhibiting the platelet-derived growth factor receptor Investigative Ophthalmology and Visual Science 41 3107 3118
    • (2000) Investigative Ophthalmology and Visual Science , vol.41 , pp. 3107-3118
    • Ikuno, Y.1    Leong, F.-I.2    Kazlauskas, A.3


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