메뉴 건너뛰기




Volumn 34, Issue 1, 2014, Pages 16-29

Microtubule dynamic instability controls podosome patterning in osteoclasts through EB1, cortactin, and src

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CORTACTIN; EB1 PROTEIN; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 84891424014     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00578-13     Document Type: Article
Times cited : (48)

References (95)
  • 1
    • 0023686835 scopus 로고
    • Polarized secretion of lysosomal enzymes: co-distribution of cationindependent mannose-6-phosphate receptors and lysosomal enzymes along the osteoclast exocytic pathway
    • Baron R, NeffL, Brown W, Courtoy PJ, Louvard D, Farquhar MG. 1988. Polarized secretion of lysosomal enzymes: co-distribution of cationindependent mannose-6-phosphate receptors and lysosomal enzymes along the osteoclast exocytic pathway. J. Cell Biol. 106:1863-1872. http://dx.doi.org/10.1083/jcb.106.6.1863
    • (1988) J. Cell Biol. , vol.106 , pp. 1863-1872
    • Baron, R.1    Neff, L.2    Brown, W.3    Courtoy, P.J.4    Louvard, D.5    Farquhar, M.G.6
  • 2
    • 0043267732 scopus 로고    scopus 로고
    • Genetic regulation of osteoclast development and function
    • Teitelbaum SL, Ross FP. 2003. Genetic regulation of osteoclast development and function. Nat. Rev. Genet. 4:638-649. http://dx.doi.org/10.1038/nrg1122.
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 638-649
    • Teitelbaum, S.L.1    Ross, F.P.2
  • 4
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: adhesion hot-spots of invasive cells
    • Linder S, Aepfelbacher M. 2003. Podosomes: adhesion hot-spots of invasive cells. Trends Cell Biol. 13:376-385. http://dx.doi.org/10.1016/S0962-8924(03)00128-4.
    • (2003) Trends Cell Biol , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 5
    • 21044433334 scopus 로고    scopus 로고
    • Podosomes at a glance
    • Linder S, Kopp P. 2005. Podosomes at a glance. J. Cell Sci. 118:2079-2082. http://dx.doi.org/10.1242/jcs.02390.
    • (2005) J. Cell Sci. , vol.118 , pp. 2079-2082
    • Linder, S.1    Kopp, P.2
  • 6
    • 70350418724 scopus 로고    scopus 로고
    • Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions
    • Albiges-Rizo C, Destaing O, Fourcade B, Planus E, Block MR. 2009. Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions. J. Cell Sci. 122:3037-3049. http://dx.doi.org/10.1242/jcs.052704.
    • (2009) J. Cell Sci. , vol.122 , pp. 3037-3049
    • Albiges-Rizo, C.1    Destaing, O.2    Fourcade, B.3    Planus, E.4    Block, M.R.5
  • 7
    • 79959541003 scopus 로고    scopus 로고
    • The "ins" and "outs" of podosomes and invadopodia: characteristics, formation and function
    • Murphy DA, Courtneidge SA. 2011. The "ins" and "outs" of podosomes and invadopodia: characteristics, formation and function. Nat. Rev. Mol. Cell Biol. 12:413-426. http://dx.doi.org/10.1038/nrm3141.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 413-426
    • Murphy, D.A.1    Courtneidge, S.A.2
  • 8
    • 0037329229 scopus 로고    scopus 로고
    • Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein
    • Destaing O, Saltel F, Geminard JC, Jurdic P, Bard F. 2003. Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein. Mol. Biol. Cell 14:407-416. http://dx.doi.org/10.1091/mbc. E02-07-0389.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 407-416
    • Destaing, O.1    Saltel, F.2    Geminard, J.C.3    Jurdic, P.4    Bard, F.5
  • 10
    • 33845897882 scopus 로고    scopus 로고
    • Involvement of the Src-cortactin pathway in podosome formation and turnover during polarization of cultured osteoclasts
    • Luxenburg C, Parsons JT, Addadi L, Geiger B. 2006. Involvement of the Src-cortactin pathway in podosome formation and turnover during polarization of cultured osteoclasts. J. Cell Sci. 119:4878-4888. http://dx.doi.org/10.1242/jcs.03271.
    • (2006) J. Cell Sci. , vol.119 , pp. 4878-4888
    • Luxenburg, C.1    Parsons, J.T.2    Addadi, L.3    Geiger, B.4
  • 11
    • 55249119822 scopus 로고    scopus 로고
    • The architecture of the adhesive apparatus of cultured osteoclasts: from podosome formation to sealing zone assembly
    • Luxenburg C, Geblinger D, Klein E, Anderson K, Hanein D, Geiger B, Addadi L. 2007. The architecture of the adhesive apparatus of cultured osteoclasts: from podosome formation to sealing zone assembly. PLoS One 2:e179. http://dx.doi.org/10.1371/journal.pone.0000179.
    • (2007) PLoS One , vol.2
    • Luxenburg, C.1    Geblinger, D.2    Klein, E.3    Anderson, K.4    Hanein, D.5    Geiger, B.6    Addadi, L.7
  • 12
    • 33644950260 scopus 로고    scopus 로고
    • Podosome and sealing zone: specificity of the osteoclast model
    • Jurdic P, Saltel F, Chabadel A, Destaing O. 2006. Podosome and sealing zone: specificity of the osteoclast model. Eur. J. Cell Biol. 85:195-202. http://dx.doi.org/10.1016/j.ejcb.2005.09.008.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 195-202
    • Jurdic, P.1    Saltel, F.2    Chabadel, A.3    Destaing, O.4
  • 13
    • 0035931748 scopus 로고    scopus 로고
    • Convergence of _v_3 integrin- and macrophage colony stimulating factor-mediated signals on phospholipase C in prefusion osteoclasts
    • Nakamura I, Lipfert L, Rodan GA, Le TD. 2001. Convergence of _v_3 integrin- and macrophage colony stimulating factor-mediated signals on phospholipase C in prefusion osteoclasts. J. Cell Biol. 152:361-373. http://dx.doi.org/10.1083/jcb.152.2.361.
    • (2001) J. Cell Biol. , vol.152 , pp. 361-373
    • Nakamura, I.1    Lipfert, L.2    Rodan, G.A.3    Le, T.D.4
  • 15
    • 0035825121 scopus 로고    scopus 로고
    • Cbl associates with Pyk2 and Src to regulate Src kinase activity, _v_3 integrin-mediated signaling, cell adhesion, and osteoclast motility
    • Sanjay A, Houghton A, NeffL, DiDomenico E, Bardelay C, Antoine E, Levy J, Gailit J, Bowtell D, Horne WC, Baron R. 2001. Cbl associates with Pyk2 and Src to regulate Src kinase activity, _v_3 integrin-mediated signaling, cell adhesion, and osteoclast motility. J. Cell Biol. 152:181-195. http://dx.doi.org/10.1083/jcb.152.1.181.
    • (2001) J. Cell Biol. , vol.152 , pp. 181-195
    • Sanjay, A.1    Houghton, A.2    Neff, L.3    DiDomenico, E.4    Bardelay, C.5    Antoine, E.6    Levy, J.7    Gailit, J.8    Bowtell, D.9    Horne, W.C.10    Baron, R.11
  • 16
    • 0041731907 scopus 로고    scopus 로고
    • Dynamic changes in the osteoclast cytoskeleton in response to growth factors and cell attachment are controlled by _3 integrin
    • Faccio R, Novack DV, Zallone A, Ross FP, Teitelbaum SL. 2003. Dynamic changes in the osteoclast cytoskeleton in response to growth factors and cell attachment are controlled by _3 integrin. J. Cell Biol. 162:499-509. http://dx.doi.org/10.1083/jcb.200212082.
    • (2003) J. Cell Biol. , vol.162 , pp. 499-509
    • Faccio, R.1    Novack, D.V.2    Zallone, A.3    Ross, F.P.4    Teitelbaum, S.L.5
  • 17
    • 2342442847 scopus 로고    scopus 로고
    • Src kinase activity is essential for osteoclast function
    • Miyazaki T, Sanjay A, NeffL, Tanaka S, Horne WC, Baron R. 2004. Src kinase activity is essential for osteoclast function. J. Biol. Chem. 279: 17660-17666. http://dx.doi.org/10.1074/jbc. M311032200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17660-17666
    • Miyazaki, T.1    Sanjay, A.2    Neff, L.3    Tanaka, S.4    Horne, W.C.5    Baron, R.6
  • 18
    • 0026023289 scopus 로고
    • Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
    • Soriano P, Montgomery C, Geske R, Bradley A. 1991. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64: 693-702. http://dx.doi.org/10.1016/0092-8674(91)90499-O.
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 19
    • 0030856131 scopus 로고    scopus 로고
    • Rescue of osteoclast function by transgenic expression of kinase-deficient Src in src_/_ mutant mice
    • Schwartzberg PL, Xing L, Hoffmann O, Lowell CA, Garrett L, Boyce BF, Varmus HE. 1997. Rescue of osteoclast function by transgenic expression of kinase-deficient Src in src_/_ mutant mice. Genes Dev. 11:2835-2844. http://dx.doi.org/10.1101/gad.11.21.2835.
    • (1997) Genes Dev , vol.11 , pp. 2835-2844
    • Schwartzberg, P.L.1    Xing, L.2    Hoffmann, O.3    Lowell, C.A.4    Garrett, L.5    Boyce, B.F.6    Varmus, H.E.7
  • 20
    • 38749128376 scopus 로고    scopus 로고
    • The tyrosine kinase activity of c-Src regulates actin dynamics and organization of podosomes in osteoclasts
    • Destaing O, Sanjay A, Itzstein C, Horne WC, Toomre D, De Camilli P, Baron R. 2008. The tyrosine kinase activity of c-Src regulates actin dynamics and organization of podosomes in osteoclasts. Mol. Biol. Cell 19: 394-404. http://dx.doi.org/10.1091/mbc. E07-03-0227.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 394-404
    • Destaing, O.1    Sanjay, A.2    Itzstein, C.3    Horne, W.C.4    Toomre, D.5    De Camilli, P.6    Baron, R.7
  • 22
    • 0035831497 scopus 로고    scopus 로고
    • Inhibition of osteoclast function by adenovirus expressing antisense protein-tyrosine kinase 2
    • Duong LT, Nakamura I, Lakkakorpi PT, Lipfert L, Bett AJ, Rodan GA. 2001. Inhibition of osteoclast function by adenovirus expressing antisense protein-tyrosine kinase 2. J. Biol. Chem. 276:7484-7492. http://dx.doi.org/10.1074/jbc. M008368200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7484-7492
    • Duong, L.T.1    Nakamura, I.2    Lakkakorpi, P.T.3    Lipfert, L.4    Bett, A.J.5    Rodan, G.A.6
  • 23
    • 70350230150 scopus 로고    scopus 로고
    • c- Cbl and Cbl-b act redundantly to protect osteoclasts from apoptosis and to displace HDAC6 from beta-tubulin, stabilizing microtubules and podosomes
    • Purev E, NeffL, Horne WC, Baron R. 2009. c-Cbl and Cbl-b act redundantly to protect osteoclasts from apoptosis and to displace HDAC6 from beta-tubulin, stabilizing microtubules and podosomes. Mol. Biol. Cell 20: 4021-4030. http://dx.doi.org/10.1091/mbc. E09-03-0248.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4021-4030
    • Purev, E.1    Neff, L.2    Horne, W.C.3    Baron, R.4
  • 24
    • 23744515800 scopus 로고    scopus 로고
    • A novel Rho-mDia2-HDAC6 pathway controls podosome patterning through microtubule acetylation in osteoclasts
    • Destaing O, Saltel F, Gilquin B, Chabadel A, Khochbin S, Ory S, Jurdic P. 2005. A novel Rho-mDia2-HDAC6 pathway controls podosome patterning through microtubule acetylation in osteoclasts. J. Cell Sci. 118: 2901-2911. http://dx.doi.org/10.1242/jcs.02425.
    • (2005) J. Cell Sci. , vol.118 , pp. 2901-2911
    • Destaing, O.1    Saltel, F.2    Gilquin, B.3    Chabadel, A.4    Khochbin, S.5    Ory, S.6    Jurdic, P.7
  • 25
    • 0034536206 scopus 로고    scopus 로고
    • Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages
    • Linder S, Hufner K, Wintergerst U, Aepfelbacher M. 2000. Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages. J. Cell Sci. 113:4165-4176.
    • (2000) J. Cell Sci. , vol.113 , pp. 4165-4176
    • Linder, S.1    Hufner, K.2    Wintergerst, U.3    Aepfelbacher, M.4
  • 26
    • 0037512351 scopus 로고    scopus 로고
    • Macrophage podosomes assemble at the leading lamella by growth and fragmentation
    • Evans JG, Correia I, Krasavina O, Watson N, Matsudaira P. 2003. Macrophage podosomes assemble at the leading lamella by growth and fragmentation. J. Cell Biol. 161:697-705. http://dx.doi.org/10.1083/jcb.200212037.
    • (2003) J. Cell Biol. , vol.161 , pp. 697-705
    • Evans, J.G.1    Correia, I.2    Krasavina, O.3    Watson, N.4    Matsudaira, P.5
  • 27
    • 39149112463 scopus 로고    scopus 로고
    • Adhesion structures and their cytoskeleton-membrane interactions at podosomes of osteoclasts in culture
    • Akisaka T, Yoshida H, Suzuki R, Takama K. 2008. Adhesion structures and their cytoskeleton-membrane interactions at podosomes of osteoclasts in culture. Cell Tissue Res. 331:625-641. http://dx.doi.org/10.1007/s00441-007-0552-x.
    • (2008) Cell Tissue Res , vol.331 , pp. 625-641
    • Akisaka, T.1    Yoshida, H.2    Suzuki, R.3    Takama, K.4
  • 28
    • 79960903518 scopus 로고    scopus 로고
    • Differential distribution of posttranslationally modified microtubules in osteoclasts
    • Akisaka T, Yoshida H, Takigawa T. 2011. Differential distribution of posttranslationally modified microtubules in osteoclasts. J. Histochem. Cytochem. 59:630-638. http://dx.doi.org/10.1369/0022155411405334.
    • (2011) J. Histochem. Cytochem. , vol.59 , pp. 630-638
    • Akisaka, T.1    Yoshida, H.2    Takigawa, T.3
  • 30
    • 77955670180 scopus 로고    scopus 로고
    • Plus-end-tracking proteins and their interactions at microtubule ends
    • Galjart N. 2010. Plus-end-tracking proteins and their interactions at microtubule ends. Curr. Biol. 20:R528-R537. http://dx.doi.org/10.1016/j.cub.2010.05.022.
    • (2010) Curr. Biol. , vol.20
    • Galjart, N.1
  • 31
    • 33846286901 scopus 로고    scopus 로고
    • Shaping the actin cytoskeleton using microtubule tips
    • Basu R, Chang F. 2007. Shaping the actin cytoskeleton using microtubule tips. Curr. Opin. Cell Biol. 19:88-94. http://dx.doi.org/10.1016/j.ceb.2006.12.012.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 88-94
    • Basu, R.1    Chang, F.2
  • 32
    • 41149156427 scopus 로고    scopus 로고
    • Tracking the ends: a dynamic protein network controls the fate of microtubule tips
    • Akhmanova A, Steinmetz MO. 2008. Tracking the ends: a dynamic protein network controls the fate of microtubule tips. Nat. Rev. Mol. Cell Biol. 9:309-322. http://dx.doi.org/10.1038/nrm2369.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 309-322
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 33
    • 84872831129 scopus 로고    scopus 로고
    • End- binding proteins and Ase1/PRC1 define local functionality of structurally distinct parts of the microtubule cytoskeleton
    • Duellberg C, Fourniol FJ, Maurer SP, Roostalu J, Surrey T. 2013. End-binding proteins and Ase1/PRC1 define local functionality of structurally distinct parts of the microtubule cytoskeleton. Trends Cell Biol. 23:54-63. http://dx.doi.org/10.1016/j.tcb.2012.10.003.
    • (2013) Trends Cell Biol , vol.23 , pp. 54-63
    • Duellberg, C.1    Fourniol, F.J.2    Maurer, S.P.3    Roostalu, J.4    Surrey, T.5
  • 34
    • 33745848829 scopus 로고    scopus 로고
    • Microtubule plus end: a hub of cellular activities
    • Lansbergen G, Akhmanova A. 2006. Microtubule plus end: a hub of cellular activities. Traffic 7:499-507. http://dx.doi.org/10.1111/j.1600-0854.2006.00400.x.
    • (2006) Traffic , vol.7 , pp. 499-507
    • Lansbergen, G.1    Akhmanova, A.2
  • 38
    • 84859736946 scopus 로고    scopus 로고
    • EBs recognize a nucleotide-dependent structural cap at growing microtubule ends
    • Maurer SP, Fourniol FJ, Bohner G, Moores CA, Surrey T. 2012. EBs recognize a nucleotide-dependent structural cap at growing microtubule ends. Cell 149:371-382. http://dx.doi.org/10.1016/j.cell.2012.02.049.
    • (2012) Cell , vol.149 , pp. 371-382
    • Maurer, S.P.1    Fourniol, F.J.2    Bohner, G.3    Moores, C.A.4    Surrey, T.5
  • 39
    • 33644992707 scopus 로고    scopus 로고
    • In situ fluorescence analysis demonstrates active siRNA exclusion from the nucleus by Exportin 5
    • Ohrt T, Merkle D, Birkenfeld K, Echeverri CJ, Schwille P. 2006. In situ fluorescence analysis demonstrates active siRNA exclusion from the nucleus by Exportin 5. Nucleic Acids Res. 34:1369-1380. http://dx.doi.org/10.1093/nar/gkl001.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1369-1380
    • Ohrt, T.1    Merkle, D.2    Birkenfeld, K.3    Echeverri, C.J.4    Schwille, P.5
  • 41
    • 0034614936 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC) protein moves along microtubules and concentrates at their growing ends in epithelial cells
    • Mimori-Kiyosue Y, Shiina N, Tsukita S. 2000. Adenomatous polyposis coli (APC) protein moves along microtubules and concentrates at their growing ends in epithelial cells. J. Cell Biol. 148:505-518. http://dx.doi.org/10.1083/jcb.148.3.505.
    • (2000) J. Cell Biol. , vol.148 , pp. 505-518
    • Mimori-Kiyosue, Y.1    Shiina, N.2    Tsukita, S.3
  • 42
    • 0030920202 scopus 로고    scopus 로고
    • Nanomolar concentrations of nocodazole alter microtubule dynamic instability in vivo and in vitro
    • Vasquez RJ, Howell B, Yvon AM, Wadsworth P, Cassimeris L. 1997. Nanomolar concentrations of nocodazole alter microtubule dynamic instability in vivo and in vitro. Mol. Biol. Cell 8:973-985. http://dx.doi.org/10.1091/mbc.8.6.973.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 973-985
    • Vasquez, R.J.1    Howell, B.2    Yvon, A.M.3    Wadsworth, P.4    Cassimeris, L.5
  • 44
    • 77956340867 scopus 로고    scopus 로고
    • Analysis of microtubule dynamic instability using a plus-end growth marker
    • Matov A, Applegate K, Kumar P, Thoma C, Krek W, Danuser G, Wittmann T. 2010. Analysis of microtubule dynamic instability using a plus-end growth marker. Nat. Methods 7:761-768. http://dx.doi.org/10.1038/nmeth.1493.
    • (2010) Nat. Methods , vol.7 , pp. 761-768
    • Matov, A.1    Applegate, K.2    Kumar, P.3    Thoma, C.4    Krek, W.5    Danuser, G.6    Wittmann, T.7
  • 45
  • 47
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • 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. U. S. A. 100:4389-4394. http://dx.doi.org/10.1073/pnas.0430973100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 48
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • 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. http://dx.doi.org/10.1093/emboj/cdg115.
    • (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
  • 49
    • 0034642479 scopus 로고    scopus 로고
    • EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue
    • Nakagawa H, Koyama K, Murata Y, Morito M, Akiyama T, Nakamura Y. 2000. EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue. Oncogene 19:210-216. http://dx.doi.org/10.1038/sj.onc.1203308.
    • (2000) Oncogene , vol.19 , pp. 210-216
    • Nakagawa, H.1    Koyama, K.2    Murata, Y.3    Morito, M.4    Akiyama, T.5    Nakamura, Y.6
  • 50
    • 33644882476 scopus 로고    scopus 로고
    • Cortactin regulates podosome formation: roles of the protein interaction domains
    • Webb BA, Eves R, Mak AS. 2006. Cortactin regulates podosome formation: roles of the protein interaction domains. Exp. Cell Res. 312:760-769. http://dx.doi.org/10.1016/j.yexcr.2005.11.032.
    • (2006) Exp. Cell Res. , vol.312 , pp. 760-769
    • Webb, B.A.1    Eves, R.2    Mak, A.S.3
  • 52
    • 33745626457 scopus 로고    scopus 로고
    • Cortactin has an essential and specific role in osteoclast actin assembly
    • Tehrani S, Faccio R, Chandrasekar I, Ross FP, Cooper JA. 2006. Cortactin has an essential and specific role in osteoclast actin assembly. Mol. Biol. Cell 17:2882-2895. http://dx.doi.org/10.1091/mbc. E06-03-0187.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2882-2895
    • Tehrani, S.1    Faccio, R.2    Chandrasekar, I.3    Ross, F.P.4    Cooper, J.A.5
  • 53
    • 77956920121 scopus 로고    scopus 로고
    • Regulation of sealing ring formation by L-plastin and cortactin in osteoclasts
    • Ma T, Sadashivaiah K, Madayiputhiya N, Chellaiah MA. 2010. Regulation of sealing ring formation by L-plastin and cortactin in osteoclasts. J. Biol. Chem. 285:29911-29924. http://dx.doi.org/10.1074/jbc. M109.099697.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29911-29924
    • Ma, T.1    Sadashivaiah, K.2    Madayiputhiya, N.3    Chellaiah, M.A.4
  • 55
    • 67650065066 scopus 로고    scopus 로고
    • Dynamin reduces Pyk2 Y402 phosphorylation and SRC binding in osteoclasts
    • Bruzzaniti A, NeffL, Sandoval A, Du L, Horne WC, Baron R. 2009. Dynamin reduces Pyk2 Y402 phosphorylation and SRC binding in osteoclasts. Mol. Cell Biol. 29:3644-3656. http://dx.doi.org/10.1128/MCB.00851-08.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 3644-3656
    • Bruzzaniti, A.1    Neff, L.2    Sandoval, A.3    Du, L.4    Horne, W.C.5    Baron, R.6
  • 57
    • 0041468477 scopus 로고    scopus 로고
    • Cortactin tyrosine phosphorylation requires Rac1 activity and association with the cortical actin cytoskeleton
    • Head JA, Jiang D, Li M, Zorn LJ, Schaefer EM, Parsons JT, Weed SA. 2003. Cortactin tyrosine phosphorylation requires Rac1 activity and association with the cortical actin cytoskeleton. Mol. Biol. Cell 14:3216-3229. http://dx.doi.org/10.1091/mbc. E02-11-0753.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3216-3229
    • Head, J.A.1    Jiang, D.2    Li, M.3    Zorn, L.J.4    Schaefer, E.M.5    Parsons, J.T.6    Weed, S.A.7
  • 61
    • 79151472958 scopus 로고    scopus 로고
    • HDAC6 is required for invadopodia activity and invasion by breast tumor cells
    • Rey M, Irondelle M, Waharte F, Lizarraga F, Chavrier P. 2011. HDAC6 is required for invadopodia activity and invasion by breast tumor cells. Eur. J. Cell Biol. 90:128-135. http://dx.doi.org/10.1016/j.ejcb.2010.09.004.
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 128-135
    • Rey, M.1    Irondelle, M.2    Waharte, F.3    Lizarraga, F.4    Chavrier, P.5
  • 63
    • 84859136035 scopus 로고    scopus 로고
    • Cortactin tyrosine phosphorylation promotes its deacetylation and inhibits cell spreading
    • Meiler E, Nieto-Pelegrin E, Martinez-Quiles N. 2012. Cortactin tyrosine phosphorylation promotes its deacetylation and inhibits cell spreading. PLoS One 7:e33662. http://dx.doi.org/10.1371/journal.pone.0033662.
    • (2012) PLoS One , vol.7
    • Meiler, E.1    Nieto-Pelegrin, E.2    Martinez-Quiles, N.3
  • 64
    • 0032697492 scopus 로고    scopus 로고
    • Signaling pathways and structural domains required for phosphorylation of EMS1/cortactin
    • Campbell DH, Sutherland RL, Daly RJ. 1999. Signaling pathways and structural domains required for phosphorylation of EMS1/cortactin. Cancer Res. 59:5376-5385.
    • (1999) Cancer Res , vol.59 , pp. 5376-5385
    • Campbell, D.H.1    Sutherland, R.L.2    Daly, R.J.3
  • 65
    • 0038498066 scopus 로고    scopus 로고
    • A cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton
    • Lynch DK, Winata SC, Lyons RJ, Hughes WE, Lehrbach GM, Wasinger V, Corthals G, Cordwell S, Daly RJ. 2003. A cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton. J. Biol. Chem. 278:21805-21813. http://dx.doi.org/10.1074/jbc. M211407200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21805-21813
    • Lynch, D.K.1    Winata, S.C.2    Lyons, R.J.3    Hughes, W.E.4    Lehrbach, G.M.5    Wasinger, V.6    Corthals, G.7    Cordwell, S.8    Daly, R.J.9
  • 66
    • 0030947860 scopus 로고    scopus 로고
    • Substrate recognition by osteoclast precursors induces C-src/microtubule association
    • Abu-Amer Y, Ross FP, Schlesinger P, Tondravi MM, Teitelbaum SL. 1997. Substrate recognition by osteoclast precursors induces C-src/microtubule association. J. Cell Biol. 137:247-258. http://dx.doi.org/10.1083/jcb.137.1.247.
    • (1997) J. Cell Biol. , vol.137 , pp. 247-258
    • Abu-Amer, Y.1    Ross, F.P.2    Schlesinger, P.3    Tondravi, M.M.4    Teitelbaum, S.L.5
  • 67
    • 84872699940 scopus 로고    scopus 로고
    • Disruption of the dynein-dynactin complex unveils motor-specific functions in osteoclast formation and bone resorption
    • Ng PY, Cheng TS, Zhao H, Ye S, Sm Ang E, Khor EC, Feng HT, Xu J, Zheng MH, Pavlos NJ. 2013. Disruption of the dynein-dynactin complex unveils motor-specific functions in osteoclast formation and bone resorption. J. Bone Miner. Res. 28:119-134. http://dx.doi.org/10.1002/jbmr.1725.
    • (2013) J. Bone Miner. Res. , vol.28 , pp. 119-134
    • Ng, P.Y.1    Cheng, T.S.2    Zhao, H.3    Ye, S.4    Sm Ang, E.5    Khor, E.C.6    Feng, H.T.7    Xu, J.8    Zheng, M.H.9    Pavlos, N.J.10
  • 68
  • 70
    • 67649460727 scopus 로고    scopus 로고
    • ATP- induced osteoclast function: the formation of sealing-zone like structure and the secretion of lytic granules via microtubule-deacetylation under the control of Syk
    • Hazama R, Qu X, Yokoyama K, Tanaka C, Kinoshita E, He J, Takahashi S, Tohyama K, Yamamura H, Tohyama Y. 2009. ATP-induced osteoclast function: the formation of sealing-zone like structure and the secretion of lytic granules via microtubule-deacetylation under the control of Syk. Genes Cells14:871-884. http://dx.doi.org/10.1111/j.1365-2443.2009.01317.x.
    • (2009) Genes Cells , vol.14 , pp. 871-884
    • Hazama, R.1    Qu, X.2    Yokoyama, K.3    Tanaka, C.4    Kinoshita, E.5    He, J.6    Takahashi, S.7    Tohyama, K.8    Yamamura, H.9    Tohyama, Y.10
  • 71
    • 1642290655 scopus 로고    scopus 로고
    • Endocytic trafficking in actively resorbing osteoclasts
    • Stenbeck G, Horton MA. 2004. Endocytic trafficking in actively resorbing osteoclasts. J. Cell Sci. 117:827-836. http://dx.doi.org/10.1242/jcs.00935.
    • (2004) J. Cell Sci. , vol.117 , pp. 827-836
    • Stenbeck, G.1    Horton, M.A.2
  • 72
    • 0037936890 scopus 로고    scopus 로고
    • From lysosomes to the plasma membrane: localization of vacuolar-type H_-ATPase with the a3 isoform during osteoclast differentiation
    • Toyomura T, Murata Y, Yamamoto A, Oka T, Sun-Wada GH, Wada Y, Futai M. 2003. From lysosomes to the plasma membrane: localization of vacuolar-type H_-ATPase with the a3 isoform during osteoclast differentiation. J. Biol. Chem. 278:22023-22030. http://dx.doi.org/10.1074/jbc. M302436200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22023-22030
    • Toyomura, T.1    Murata, Y.2    Yamamoto, A.3    Oka, T.4    Sun-Wada, G.H.5    Wada, Y.6    Futai, M.7
  • 73
    • 79951822972 scopus 로고    scopus 로고
    • Calpain-6, a target molecule of glucocorticoids, regulates osteoclastic bone resorption via cytoskeletal organization and microtubule acetylation
    • Hong JM, Teitelbaum SL, Kim TH, Ross FP, Kim SY, Kim HJ. 2011. Calpain-6, a target molecule of glucocorticoids, regulates osteoclastic bone resorption via cytoskeletal organization and microtubule acetylation. J. Bone Miner. Res. 26:657-665. http://dx.doi.org/10.1002/jbmr.241.
    • (2011) J. Bone Miner. Res. , vol.26 , pp. 657-665
    • Hong, J.M.1    Teitelbaum, S.L.2    Kim, T.H.3    Ross, F.P.4    Kim, S.Y.5    Kim, H.J.6
  • 74
    • 77951211165 scopus 로고    scopus 로고
    • Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules
    • McMichael BK, Cheney RE, Lee BS. 2010. Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules. J. Biol. Chem. 285:9506-9515. http://dx.doi.org/10.1074/jbc. M109.017269.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9506-9515
    • McMichael, B.K.1    Cheney, R.E.2    Lee, B.S.3
  • 76
  • 77
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
    • Schoumacher M, Goldman RD, Louvard D, Vignjevic DM. 2010. Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J. Cell Biol. 189:541-556. http://dx.doi.org/10.1083/jcb.200909113.
    • (2010) J. Cell Biol. , vol.189 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 80
    • 0028934290 scopus 로고
    • Differentiation dependent expression of tensin and cortactin in chicken osteoclasts
    • Hiura K, Lim SS, Little SP, Lin S, Sato M. 1995. Differentiation dependent expression of tensin and cortactin in chicken osteoclasts. Cell Motil. Cytoskeleton 30:272-284.
    • (1995) Cell Motil. Cytoskeleton , vol.30 , pp. 272-284
    • Hiura, K.1    Lim, S.S.2    Little, S.P.3    Lin, S.4    Sato, M.5
  • 81
    • 2942702354 scopus 로고    scopus 로고
    • Actin-related protein 2/3 complex is required for actin ring formation
    • Hurst IR, Zuo J, Jiang J, Holliday LS. 2004. Actin-related protein 2/3 complex is required for actin ring formation. J. Bone Miner. Res. 19:499-506. http://dx.doi.org/10.1359/JBMR.0301238.
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 499-506
    • Hurst, I.R.1    Zuo, J.2    Jiang, J.3    Holliday, L.S.4
  • 83
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases
    • Kanner SB, Reynolds AB, Vines RR, Parsons JT. 1990. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc. Natl. Acad. Sci. U. S. A. 87: 3328-3332. http://dx.doi.org/10.1073/pnas.87.9.3328.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3328-3332
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 84
    • 50649090270 scopus 로고    scopus 로고
    • Cortactin branches out: roles in regulating protrusive actin dynamics
    • Ammer AG, Weed SA. 2008. Cortactin branches out: roles in regulating protrusive actin dynamics. Cell Motil. Cytoskeleton 65:687-707. http://dx.doi.org/10.1359/JBMR.0301238.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 687-707
    • Ammer, A.G.1    Weed, S.A.2
  • 85
    • 33947140891 scopus 로고    scopus 로고
    • Dissecting the functional domain requirements of cortactin in invadopodia formation
    • Webb BA, Jia L, Eves R, Mak AS. 2007. Dissecting the functional domain requirements of cortactin in invadopodia formation. Eur. J. Cell Biol. 86:189-206. http://dx.doi.org/10.1016/j.ejcb.2007.01.003.
    • (2007) Eur. J. Cell Biol. , vol.86 , pp. 189-206
    • Webb, B.A.1    Jia, L.2    Eves, R.3    Mak, A.S.4
  • 86
    • 33644860573 scopus 로고    scopus 로고
    • Effects of tyrosine phosphorylation of cortactin on podosome formation in A7r5 vascular smooth muscle cells
    • Zhou S, Webb BA, Eves R, Mak AS. 2006. Effects of tyrosine phosphorylation of cortactin on podosome formation in A7r5 vascular smooth muscle cells. Am. J. Physiol. Cell Physiol. 290:C463-C471. http://dx.doi.org/10.1152/ajpcell.00350.2005.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Zhou, S.1    Webb, B.A.2    Eves, R.3    Mak, A.S.4
  • 87
    • 33645507413 scopus 로고    scopus 로고
    • Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function
    • Artym VV, Zhang Y, Seillier-Moiseiwitsch F, Yamada KM, Mueller SC. 2006. Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function. Cancer Res. 66:3034-3043. http://dx.doi.org/10.1158/0008-5472.CAN-05-2177.
    • (2006) Cancer Res , vol.66 , pp. 3034-3043
    • Artym, V.V.1    Zhang, Y.2    Seillier-Moiseiwitsch, F.3    Yamada, K.M.4    Mueller, S.C.5
  • 88
    • 40549089536 scopus 로고    scopus 로고
    • Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation
    • Ayala I, Baldassarre M, Giacchetti G, Caldieri G, Tete S, Luini A, Buccione R. 2008. Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation. J. Cell Sci. 121:369-378. http://dx.doi.org/10.1242/jcs.008037.
    • (2008) J. Cell Sci. , vol.121 , pp. 369-378
    • Ayala, I.1    Baldassarre, M.2    Giacchetti, G.3    Caldieri, G.4    Tete, S.5    Luini, A.6    Buccione, R.7
  • 89
    • 34249320529 scopus 로고    scopus 로고
    • Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia
    • Clark ES, Whigham AS, Yarbrough WG, Weaver AM. 2007. Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia. Cancer Res. 67:4227-4235. http://dx.doi.org/10.1158/0008-5472.CAN-06-3928.
    • (2007) Cancer Res , vol.67 , pp. 4227-4235
    • Clark, E.S.1    Whigham, A.S.2    Yarbrough, W.G.3    Weaver, A.M.4
  • 91
    • 33646071808 scopus 로고    scopus 로고
    • Co- localization of cortactin and phosphotyrosine identifies active invadopodia in human breast cancer cells
    • Bowden ET, Onikoyi E, Slack R, Myoui A, Yoneda T, Yamada KM, Mueller SC. 2006. Co-localization of cortactin and phosphotyrosine identifies active invadopodia in human breast cancer cells. Exp. Cell Res. 312: 1240-1253. http://dx.doi.org/10.1016/j.yexcr.2005.12.012.
    • (2006) Exp. Cell Res. , vol.312 , pp. 1240-1253
    • Bowden, E.T.1    Onikoyi, E.2    Slack, R.3    Myoui, A.4    Yoneda, T.5    Yamada, K.M.6    Mueller, S.C.7
  • 93
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • 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. http://dx.doi.org/10.1126/science.1175371.
    • (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
  • 94
    • 84867398827 scopus 로고    scopus 로고
    • ATAT1/MEC-17 acetyltransferase and HDAC6 deacetylase control a balance of acetylation of alpha-tubulin and cortactin and regulate MT1-MMP trafficking and breast tumor cell invasion
    • Castro-Castro A, Janke C, Montagnac G, Paul-Gilloteaux P, Chavrier P. 2012. ATAT1/MEC-17 acetyltransferase and HDAC6 deacetylase control a balance of acetylation of alpha-tubulin and cortactin and regulate MT1-MMP trafficking and breast tumor cell invasion. Eur. J. Cell Biol. 91:950-960. http://dx.doi.org/10.1016/j.ejcb.2012.07.001.
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 950-960
    • Castro-Castro, A.1    Janke, C.2    Montagnac, G.3    Paul-Gilloteaux, P.4    Chavrier, P.5
  • 95
    • 0035860713 scopus 로고    scopus 로고
    • Src-catalyzed phosphorylation of c-Cbl leads to the interdependent ubiquitination of both proteins
    • Yokouchi M, Kondo T, Sanjay A, Houghton A, Yoshimura A, Komiya S, Zhang H, Baron R. 2001. Src-catalyzed phosphorylation of c-Cbl leads to the interdependent ubiquitination of both proteins. J. Biol. Chem. 276: 35185-35193. http://dx.doi.org/10.1074/jbc. M102219200.
    • (2001) J. Biol. Chem , vol.276 , pp. 35185-35193
    • Yokouchi, M.1    Kondo, T.2    Sanjay, A.3    Houghton, A.4    Yoshimura, A.5    Komiya, S.6    Zhang, H.7    Baron, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.