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Volumn 6, Issue 1, 2015, Pages 42-54

Proteomic identification and functional characterization of MYH9, Hsc70, and DNAJA1 as novel substrates of HDAC6 deacetylase activity

Author keywords

HDAC6; interaction; lysine acetylation; quantitative proteomics; substrate

Indexed keywords

HEAT SHOCK COGNATE PROTEIN 70; HISTONE DEACETYLASE 11; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE 4; HISTONE DEACETYLASE 5; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE 7; HISTONE DEACETYLASE 9; MYOSIN HEAVY CHAIN 9; PEPTIDES AND PROTEINS; PLASMID VECTOR; PROTEIN DNAJ 1; SIRTUIN 2; UNCLASSIFIED DRUG; ACTIN; DNAJA1 PROTEIN, MOUSE; HDAC6 PROTEIN, MOUSE; HEAT SHOCK PROTEIN 40; HISTONE DEACETYLASE; LYSINE; MYH9 PROTEIN, MOUSE; MYOSIN IIA; PROTEIN BINDING;

EID: 84922080063     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-014-0102-8     Document Type: Article
Times cited : (52)

References (44)
  • 1
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • COI: 1:CAS:528:DyaF2cXktlekurg%3D, PID: 14172992
    • Allfrey VG, Faulkner R, Mirsky AE (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA 51:786–794
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 2
    • 0035870122 scopus 로고    scopus 로고
    • dSIR2 and dHDAC6: two novel, inhibitor-resistant deacetylases in Drosophila melanogaster
    • COI: 1:CAS:528:DC%2BD3MXitlaht74%3D, PID: 11281647
    • Barlow AL, van Drunen CM, Johnson CA, Tweedie S, Bird A, Turner BM (2001) dSIR2 and dHDAC6: two novel, inhibitor-resistant deacetylases in Drosophila melanogaster. Exp Cell Res 265:90–103
    • (2001) Exp Cell Res , vol.265 , pp. 90-103
    • Barlow, A.L.1    van Drunen, C.M.2    Johnson, C.A.3    Tweedie, S.4    Bird, A.5    Turner, B.M.6
  • 3
    • 55849093586 scopus 로고    scopus 로고
    • Triplex protein quantification based on stable isotope labeling by peptide dimethylation applied to cell and tissue lysates
    • COI: 1:CAS:528:DC%2BD1cXhsV2js73O, PID: 18850632
    • Boersema PJ, Aye TT, van Veen TA, Heck AJ, Mohammed S (2008) Triplex protein quantification based on stable isotope labeling by peptide dimethylation applied to cell and tissue lysates. Proteomics 8:4624–4632
    • (2008) Proteomics , vol.8 , pp. 4624-4632
    • Boersema, P.J.1    Aye, T.T.2    van Veen, T.A.3    Heck, A.J.4    Mohammed, S.5
  • 4
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • COI: 1:CAS:528:DC%2BD1MXjvFyjs7g%3D, PID: 19300442
    • Boersema PJ, Raijmakers R, Lemeer S, Mohammed S, Heck AJ (2009) Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat Protoc 4:484–494
    • (2009) Nat Protoc , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 5
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • COI: 1:CAS:528:DyaK1cXhtFGisLk%3D, PID: 9476895
    • Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351–366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 6
    • 84867186480 scopus 로고    scopus 로고
    • Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways
    • COI: 1:CAS:528:DC%2BC38XhsFSmtrzN, PID: 22826441
    • Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y (2012) Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Mol Cell Proteomics 11:1048–1062
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1048-1062
    • Chen, Y.1    Zhao, W.2    Yang, J.S.3    Cheng, Z.4    Luo, H.5    Lu, Z.6    Tan, M.7    Gu, W.8    Zhao, Y.9
  • 7
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • COI: 1:CAS:528:DC%2BD1MXps1Ogt70%3D, PID: 19608861
    • Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325:834–840
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8
  • 9
    • 37549010715 scopus 로고    scopus 로고
    • Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis
    • COI: 1:CAS:528:DC%2BD1cXmt1Cjug%3D%3D, PID: 17938201
    • Gao YS, Hubbert CC, Lu J, Lee YS, Lee JY, Yao TP (2007) Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis. Mol Cell Biol 27:8637–8647
    • (2007) Mol Cell Biol , vol.27 , pp. 8637-8647
    • Gao, Y.S.1    Hubbert, C.C.2    Lu, J.3    Lee, Y.S.4    Lee, J.Y.5    Yao, T.P.6
  • 10
    • 0014409959 scopus 로고
    • Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone
    • COI: 1:CAS:528:DyaF1cXkslChsrY%3D, PID: 5679978
    • Gershey EL, Vidali G, Allfrey VG (1968) Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. J Biol Chem 243:5018–5022
    • (1968) J Biol Chem , vol.243 , pp. 5018-5022
    • Gershey, E.L.1    Vidali, G.2    Allfrey, V.G.3
  • 11
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • COI: 1:CAS:528:DyaK1MXjtVKms7s%3D, PID: 10220385
    • Grozinger CM, Hassig CA, Schreiber SL (1999) Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc Natl Acad Sci USA 96:4868–4873
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 12
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • COI: 1:CAS:528:DyaK2sXlvFKmtLc%3D, PID: 9288740
    • Gu W, Roeder RG (1997) Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595–606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 13
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • COI: 1:CAS:528:DC%2BD3sXjt12gtL0%3D, PID: 12677000
    • Haggarty SJ, Koeller KM, Wong JC, Grozinger CM, Schreiber SL (2003) Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc Natl Acad Sci USA 100:4389–4394
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 16
    • 79953203531 scopus 로고    scopus 로고
    • Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6
    • COI: 1:CAS:528:DC%2BC3MXjtFOisb8%3D, PID: 21220424
    • Huo L, Li D, Sun X, Shi X, Karna P, Yang W, Liu M, Qiao W, Aneja R, Zhou J (2011) Regulation of Tat acetylation and transactivation activity by the microtubule-associated deacetylase HDAC6. J Biol Chem 286:9280–9286
    • (2011) J Biol Chem , vol.286 , pp. 9280-9286
    • Huo, L.1    Li, D.2    Sun, X.3    Shi, X.4    Karna, P.5    Yang, W.6    Liu, M.7    Qiao, W.8    Aneja, R.9    Zhou, J.10
  • 17
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • COI: 1:CAS:528:DC%2BD28Xpt1Snurk%3D, PID: 16916647
    • Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L et al (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 23:607–618
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6    Cheng, T.7    Kho, Y.8    Xiao, H.9    Xiao, L.10
  • 19
    • 45149089913 scopus 로고    scopus 로고
    • HDAC6 is required for epidermal growth factor-induced beta-catenin nuclear localization
    • COI: 1:CAS:528:DC%2BD1cXltlGkur8%3D, PID: 18356165
    • Li Y, Zhang X, Polakiewicz RD, Yao TP, Comb MJ (2008) HDAC6 is required for epidermal growth factor-induced beta-catenin nuclear localization. J Biol Chem 283:12686–12690
    • (2008) J Biol Chem , vol.283 , pp. 12686-12690
    • Li, Y.1    Zhang, X.2    Polakiewicz, R.D.3    Yao, T.P.4    Comb, M.J.5
  • 20
    • 79953219078 scopus 로고    scopus 로고
    • Microtubule-associated deacetylase HDAC6 promotes angiogenesis by regulating cell migration in an EB1-dependent manner
    • COI: 1:CAS:528:DC%2BC3MXjtFSku7k%3D, PID: 21359602
    • Li D, Xie S, Ren Y, Huo L, Gao J, Cui D, Liu M, Zhou J (2011) Microtubule-associated deacetylase HDAC6 promotes angiogenesis by regulating cell migration in an EB1-dependent manner. Protein Cell 2:150–160
    • (2011) Protein Cell , vol.2 , pp. 150-160
    • Li, D.1    Xie, S.2    Ren, Y.3    Huo, L.4    Gao, J.5    Cui, D.6    Liu, M.7    Zhou, J.8
  • 21
    • 84898599000 scopus 로고    scopus 로고
    • Histone deacetylase 6 and cytoplasmic linker protein 170 function together to regulate the motility of pancreatic cancer cells
    • COI: 1:CAS:528:DC%2BC2cXhsl2mt7o%3D, PID: 24474193
    • Li D, Sun X, Zhang L, Yan B, Xie S, Liu R, Liu M, Zhou J (2014) Histone deacetylase 6 and cytoplasmic linker protein 170 function together to regulate the motility of pancreatic cancer cells. Protein Cell 5:214–223
    • (2014) Protein Cell , vol.5 , pp. 214-223
    • Li, D.1    Sun, X.2    Zhang, L.3    Yan, B.4    Xie, S.5    Liu, R.6    Liu, M.7    Zhou, J.8
  • 22
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • COI: 1:CAS:528:DyaK1MXisVWnsbo%3D, PID: 10075921
    • Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM (1999) The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J 18:1492–1505
    • (1999) EMBO J , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 25
    • 79251566746 scopus 로고    scopus 로고
    • Physical and functional HAT/HDAC interplay regulates protein acetylation balance
    • PID: 21151613
    • Peserico A, Simone C (2011) Physical and functional HAT/HDAC interplay regulates protein acetylation balance. J Biomed Biotechnol 2011:371832
    • (2011) J Biomed Biotechnol , vol.2011 , pp. 371832
    • Peserico, A.1    Simone, C.2
  • 28
    • 79251540554 scopus 로고    scopus 로고
    • The tale of protein lysine acetylation in the cytoplasm
    • PID: 21151618
    • Sadoul K, Wang J, Diagouraga B, Khochbin S (2011) The tale of protein lysine acetylation in the cytoplasm. J Biomed Biotechnol 2011:970382
    • (2011) J Biomed Biotechnol , vol.2011 , pp. 970382
    • Sadoul, K.1    Wang, J.2    Diagouraga, B.3    Khochbin, S.4
  • 30
    • 0020356742 scopus 로고
    • The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation
    • COI: 1:CAS:528:DyaL38XmtFSrtL0%3D, PID: 6128340
    • Sellers JR, Eisenberg E, Adelstein RS (1982) The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation. J Biol Chem 257:13880–13883
    • (1982) J Biol Chem , vol.257 , pp. 13880-13883
    • Sellers, J.R.1    Eisenberg, E.2    Adelstein, R.S.3
  • 31
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • COI: 1:CAS:528:DC%2BD2sXhtFGjt7nM, PID: 17406544
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 1:2856–2860
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 32
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • COI: 1:CAS:528:DC%2BD2sXhtVGqsr3N, PID: 17533153
    • Shilov IV, Seymour SL, Patel AA, Loboda A, Tang WH, Keating SP, Hunter CL, Nuwaysir LM, Schaeffer DA (2007) The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol Cell Proteomics 6:1638–1655
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 33
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase
    • COI: 1:CAS:528:DC%2BD3sXoslyjtr8%3D, PID: 14506307
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol Rev 83:1325–1358
    • (2003) Physiol Rev , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 34
    • 80051496447 scopus 로고    scopus 로고
    • HDAC6 deacetylates Ku70 and regulates Ku70-Bax binding in neuroblastoma
    • COI: 1:CAS:528:DC%2BC3MXhtFCkurfF, PID: 21847364
    • Subramanian C, Jarzembowski JA, Opipari AW Jr, Castle VP, Kwok RP (2011) HDAC6 deacetylates Ku70 and regulates Ku70-Bax binding in neuroblastoma. Neoplasia 13:726–734
    • (2011) Neoplasia , vol.13 , pp. 726-734
    • Subramanian, C.1    Jarzembowski, J.A.2    Opipari, A.W.3    Castle, V.P.4    Kwok, R.P.5
  • 35
    • 0020395203 scopus 로고
    • An actin-binding site on the 20K fragment of myosin subfragment 1
    • COI: 1:CAS:528:DyaL38XltVGktrY%3D, PID: 7138830
    • Sutoh K (1982) An actin-binding site on the 20K fragment of myosin subfragment 1. Biochemistry 21:4800–4804
    • (1982) Biochemistry , vol.21 , pp. 4800-4804
    • Sutoh, K.1
  • 38
    • 70350454867 scopus 로고    scopus 로고
    • Non-muscle myosin II takes centre stage in cell adhesion and migration
    • COI: 1:CAS:528:DC%2BD1MXhtlSjur7I, PID: 19851336
    • Vicente-Manzanares M, Ma X, Adelstein RS, Horwitz AR (2009) Non-muscle myosin II takes centre stage in cell adhesion and migration. Nat Rev Mol Cell Biol 10:778–790
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 778-790
    • Vicente-Manzanares, M.1    Ma, X.2    Adelstein, R.S.3    Horwitz, A.R.4
  • 39
    • 0029294663 scopus 로고
    • Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function
    • COI: 1:CAS:528:DyaK2MXmvVertrk%3D, PID: 7786288
    • Yoshida M, Horinouchi S, Beppu T (1995) Trichostatin A and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structure and function. Bioessays 17:423–430
    • (1995) Bioessays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 40
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • COI: 1:CAS:528:DC%2BD3sXit1yls7c%3D, PID: 12606581
    • Zhang Y, Li N, Caron C, Matthias G, Hess D, Khochbin S, Matthias P (2003) HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J 22:1168–1179
    • (2003) EMBO J , vol.22 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6    Matthias, P.7
  • 43
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • COI: 1:CAS:528:DC%2BC3cXitVSjtbo%3D, PID: 20167786
    • Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H et al (2010) Regulation of cellular metabolism by protein lysine acetylation. Science 327:1000–1004
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4    Lin, Y.5    Zhang, T.6    Yao, J.7    Zhou, L.8    Zeng, Y.9    Li, H.10
  • 44
    • 65649130809 scopus 로고    scopus 로고
    • The protein farnesyltransferase regulates HDAC6 activity in a microtubule-dependent manner
    • COI: 1:CAS:528:DC%2BD1MXjvFKkt70%3D, PID: 19228685
    • Zhou J, Vos CC, Gjyrezi A, Yoshida M, Khuri FR, Tamanoi F, Giannakakou P (2009) The protein farnesyltransferase regulates HDAC6 activity in a microtubule-dependent manner. J Biol Chem 284:9648–9655
    • (2009) J Biol Chem , vol.284 , pp. 9648-9655
    • Zhou, J.1    Vos, C.C.2    Gjyrezi, A.3    Yoshida, M.4    Khuri, F.R.5    Tamanoi, F.6    Giannakakou, P.7


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