메뉴 건너뛰기




Volumn 15, Issue 2, 2013, Pages 179-188

SCF Fbxw5 mediates transient degradation of actin remodeller Eps8 to allow proper mitotic progression

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE 8; PROTEASOME; SCF PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; EPS8 PROTEIN, HUMAN; EPS8 PROTEIN, MOUSE; F BOX PROTEIN; FBXW5 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84873406469     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb2661     Document Type: Article
Times cited : (30)

References (62)
  • 1
    • 0027179703 scopus 로고
    • Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals
    • Fazioli, F. et al. Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals. EMBOJ. 12, 3799-3808 (1993).
    • (1993) EMBOJ , vol.12 , pp. 3799-3808
    • Fazioli, F.1
  • 3
    • 10344251483 scopus 로고    scopus 로고
    • Eps8 controls actin-based motility by capping the barbed ends of actin filaments
    • Disanza, A. et al. Eps8 controls actin-based motility by capping the barbed ends of actin filaments. Nat Cell Biol. 6, 1180-1188 (2004).
    • (2004) Nat Cell Biol. , vol.6 , pp. 1180-1188
    • Disanza, A.1
  • 4
    • 33751543109 scopus 로고    scopus 로고
    • Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex
    • Disanza, A. et al. Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex. Nat Cell Biol. 8, 1337-1347 (2006).
    • (2006) Nat Cell Biol. , vol.8 , pp. 1337-1347
    • Disanza, A.1
  • 5
    • 0033575885 scopus 로고    scopus 로고
    • EPS8 and E3B1 transduce signals from Ras to Rac
    • Scita, G. et al. EPS8 and E3B1 transduce signals from Ras to Rac. Nature 401, 290-293 (1999).
    • (1999) Nature , vol.401 , pp. 290-293
    • Scita, G.1
  • 6
    • 0035802118 scopus 로고    scopus 로고
    • An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine
    • Scita, G. et al. An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine. J. Cell Biol. 154, 1031-1044 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 1031-1044
    • Scita, G.1
  • 7
    • 77954732524 scopus 로고    scopus 로고
    • Molecular basis for the dual function of Eps8 on actin dynamics: Bundling and capping
    • Hertzog, M. et al. Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping. PLoS Biol. 8, e1000387 (2010).
    • (2010) PLoS Biol. , vol.8
    • Hertzog, M.1
  • 8
    • 67649935286 scopus 로고    scopus 로고
    • Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF)
    • Menna, E. et al. Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF). PLoS Biol. 7, e1000138 (2009).
    • (2009) PLoS Biol. , vol.7
    • Menna, E.1
  • 9
    • 67650423992 scopus 로고    scopus 로고
    • Upregulation of Eps8 in oral squamous cell carcinoma promotes cell migration and invasion through integrin-dependent Rac1 activation
    • Yap, L. F. et al. Upregulation of Eps8 in oral squamous cell carcinoma promotes cell migration and invasion through integrin-dependent Rac1 activation. Oncogene 28, 2524-2534 (2009).
    • (2009) Oncogene , vol.28 , pp. 2524-2534
    • Yap, L.F.1
  • 10
    • 80053133518 scopus 로고    scopus 로고
    • The signaling adaptor Eps8 is an essential actin capping protein for dendritic cell migration
    • Frittoli, E. et al. The signaling adaptor Eps8 is an essential actin capping protein for dendritic cell migration. Immunity 35, 388-399 (2011).
    • (2011) Immunity , vol.35 , pp. 388-399
    • Frittoli, E.1
  • 11
    • 79151470659 scopus 로고    scopus 로고
    • Regulation of stereocilia length by myosin XVa and whirlin depends on the actin-regulatory protein Eps8
    • Manor, U. et al. Regulation of stereocilia length by myosin XVa and whirlin depends on the actin-regulatory protein Eps8. Curr. Biol. 21, 167-172 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 167-172
    • Manor, U.1
  • 12
    • 0035804176 scopus 로고    scopus 로고
    • Overexpression of p97Eps8 leads to cellular transformation: Implication of pleckstrin homology domain in p97Eps8-mediated ERK activation
    • Maa, M. C., Hsieh, C. Y. & Leu, T. H. Overexpression of p97Eps8 leads to cellular transformation: implication of pleckstrin homology domain in p97Eps8-mediated ERK activation. Oncogene 20, 106-112 (2001).
    • (2001) Oncogene , vol.20 , pp. 106-112
    • Maa, M.C.1    Hsieh, C.Y.2    Leu, T.H.3
  • 13
    • 49849083350 scopus 로고    scopus 로고
    • Eps8 decreases chemosen-sitivity and affects survival of cervical cancer patients
    • Chen, Y. J., Shen, M. R., Maa, M. C. & Leu, T. H. Eps8 decreases chemosen-sitivity and affects survival of cervical cancer patients. Mol. Cancer Ther. 7, 1376-1385 (2008).
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1376-1385
    • Chen, Y.J.1    Shen, M.R.2    Maa, M.C.3    Leu, T.H.4
  • 15
    • 66449089619 scopus 로고    scopus 로고
    • Epidermal growth factor receptor pathway substrate 8 (Eps8) is overexpressed in human pituitary tumors: Role in proliferation and survival
    • Xu, M. et al. Epidermal growth factor receptor pathway substrate 8 (Eps8) is overexpressed in human pituitary tumors: role in proliferation and survival. Endocrinology 150, 2064-2071 (2009).
    • (2009) Endocrinology , vol.150 , pp. 2064-2071
    • Xu, M.1
  • 16
    • 34547937489 scopus 로고    scopus 로고
    • Eps8 is increased in pancreatic cancer and required for dynamic actin-based cell protrusions and intercellular cytoskeletal organization
    • Welsch, T., Endlich, K., Giese, T., Buchler, M. W. & Schmidt, J. Eps8 is increased in pancreatic cancer and required for dynamic actin-based cell protrusions and intercellular cytoskeletal organization. CancerLett. 255, 205-218 (2007).
    • (2007) CancerLett. , vol.255 , pp. 205-218
    • Welsch, T.1    Endlich, K.2    Giese, T.3    Buchler, M.W.4    Schmidt, J.5
  • 17
    • 77953362503 scopus 로고    scopus 로고
    • Eps8 is recruited to lysosomesand subjected tochaperone-mediated autophagy in cancer cells
    • Welsch,T. et al. Eps8 is recruited to lysosomesand subjected tochaperone-mediated autophagy in cancer cells. Exp. Cell Res. 316, 1914-1924 (2010).
    • (2010) Exp. Cell Res. , vol.316 , pp. 1914-1924
    • Welsch, T.1
  • 18
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: Same molecule, different degradation pathways
    • Clague, M. J. & Urbe, S. Ubiquitin: same molecule, different degradation pathways. Cell 143, 682-685 (2010).
    • (2010) Cell , vol.143 , pp. 682-685
    • Clague, M.J.1    Urbe, S.2
  • 19
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 20
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M. D. & Deshaies, R. J. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6, 9-20 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 21
    • 78649653568 scopus 로고    scopus 로고
    • Structural assembly of cullin-RING ubiquitin ligasecomplexes
    • Zimmerman, E. S., Schulman, B. A. & Zheng, N. Structural assembly of cullin-RING ubiquitin ligasecomplexes. Curr. Opin. Struct. Biol. 20, 714-721 (2010).
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 714-721
    • Zimmerman, E.S.1    Schulman, B.A.2    Zheng, N.3
  • 22
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng, N. et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002).
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 23
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights intoa molecularmachine
    • Cardozo,T. & Pagano, M.The SCF ubiquitin ligase: insights intoa molecularmachine. Nat. Rev. Mol. Cell Biol. 5, 739-751 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 24
    • 79960990834 scopus 로고    scopus 로고
    • The SCF-Fbxw5 E3-ubiquitin ligase is regulated by Plk4 and targets HsSAS-6 to control centrosome duplication
    • Puklowski, A. et al. The SCF-Fbxw5 E3-ubiquitin ligase is regulated by Plk4 and targets HsSAS-6 to control centrosome duplication. Nat. Cell Biol. 13, 1004-1009 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1004-1009
    • Puklowski, A.1
  • 25
    • 79961002246 scopus 로고    scopus 로고
    • FBXW5 controls centrosome number
    • Pagan, J. & Pagano, M. FBXW5 controls centrosome number. Nat. Cell Biol. 13, 888-890 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 888-890
    • Pagan, J.1    Pagano, M.2
  • 26
    • 0029737650 scopus 로고    scopus 로고
    • Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin e
    • Won, K.A. & Reed, S. I. Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J. 15, 4182-4193 (1996).
    • (1996) EMBO J. , vol.15 , pp. 4182-4193
    • Won, K.A.1    Reed, S.I.2
  • 27
    • 0033695002 scopus 로고    scopus 로고
    • Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C
    • Takizawa, C. G. & Morgan, D. O. Control of mitosis by changes in the subcellular location of cyclin-B1-Cdk1 and Cdc25C. Curr. Opin. Cell Biol. 12, 658-665 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 658-665
    • Takizawa, C.G.1    Morgan, D.O.2
  • 28
    • 1842457017 scopus 로고    scopus 로고
    • RanGAP1&z.ast;SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly
    • Swaminathan, S. et al. RanGAP1&z.ast;SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly. J. Cell Biol. 164, 965-971 (2004).
    • (2004) J. Cell Biol. , vol.164 , pp. 965-971
    • Swaminathan, S.1
  • 29
    • 41649117158 scopus 로고    scopus 로고
    • WD40 protein FBW5 promotes ubiquitination of tumorsuppressorTSC2 by DDB1-CUL4-ROC1 ligase
    • Hu,J.etal. WD40 protein FBW5 promotes ubiquitination of tumorsuppressorTSC2 by DDB1-CUL4-ROC1 ligase. Genes Dev. 22, 866-871 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 866-871
    • Hu, J.1
  • 30
    • 34250318465 scopus 로고    scopus 로고
    • The missing link of the CUL4-DDB1 ubiquitin ligase
    • Lee, J. & Zhou, P. DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase. Mol. Cell 26, 775-780 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 775-780
    • Lee, J.1    Dcafs, Z.P.2
  • 31
    • 27644598123 scopus 로고    scopus 로고
    • High-level expression and purification of recombinant SCF ubiquitin ligases
    • Li, T., Pavletich, N. P., Schulman, B.A. & Zheng, N. High-level expression and purification of recombinant SCF ubiquitin ligases. Methods Enzymol. 398, 125-142 (2005).
    • (2005) Methods Enzymol. , vol.398 , pp. 125-142
    • Li, T.1    Pavletich, N.P.2    Schulman, B.A.3    Zheng, N.4
  • 32
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D. M. et al. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134, 995-1006 (2008).
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1
  • 33
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha, A. & Deshaies, R.J. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol. Cell 32, 21-31 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 34
    • 77949548466 scopus 로고    scopus 로고
    • Priming and Extending: A UbcH5Cdc34 E2 Handoff Mechanism for Polyubiquitination on A SCF Substrate
    • Wu, K., Kovacev, J. & Pan, Z. Q. Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate. Mol. Cell 37, 784-796 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 784-796
    • Wu, K.1    Kovacev, J.2    Pan, Z.Q.3
  • 35
    • 0031846612 scopus 로고    scopus 로고
    • Eps8, a tyrosine kinase substrate, is recruited to the cell cortex and dynamic F-actin upon cytoskeleton remodeling
    • Provenzano, C. et al. Eps8, a tyrosine kinase substrate, is recruited to the cell cortex and dynamic F-actin upon cytoskeleton remodeling. Exp. Cell Res. 242, 186-200 (1998).
    • (1998) Exp. Cell Res. , vol.242 , pp. 186-200
    • Provenzano, C.1
  • 36
    • 59049101302 scopus 로고    scopus 로고
    • Aurora B-mediated abscission checkpoint protects against tetraploidization
    • Steigemann, P. et al. Aurora B-mediated abscission checkpoint protects against tetraploidization. Cell 136, 473-484 (2009).
    • (2009) Cell , vol.136 , pp. 473-484
    • Steigemann, P.1
  • 37
    • 84865102938 scopus 로고    scopus 로고
    • Changes in ect2 localization couple actomyosin-dependent cell shape changes to mitotic progression
    • Matthews, H. K. et al. Changes in ect2 localization couple actomyosin-dependent cell shape changes to mitotic progression. Dev. Cell 23, 371-383 (2012).
    • (2012) Dev. Cell , vol.23 , pp. 371-383
    • Matthews, H.K.1
  • 38
    • 13944278891 scopus 로고    scopus 로고
    • SAS-6 defines a protein family required for centrosome duplication in C. elegans and in human cells
    • Leidel, S., Delattre, M., Cerutti, L., Baumer, K. & Gonczy, P. SAS-6 defines a protein family required for centrosome duplication in C. elegans and in human cells. Nat. Cell Biol. 7, 115-125 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 115-125
    • Leidel, S.1    Delattre, M.2    Cerutti, L.3    Baumer, K.4    Gonczy, P.5
  • 39
    • 63449127363 scopus 로고    scopus 로고
    • The actin cytoskeleton in spindle assembly and positioning
    • Kunda, P. & Baum, B. The actin cytoskeleton in spindle assembly and positioning. Trends Cell Biol. 19, 174-179 (2009).
    • (2009) Trends Cell Biol. , vol.19 , pp. 174-179
    • Kunda, P.1    Baum, B.2
  • 40
    • 38349022141 scopus 로고    scopus 로고
    • Moesin controls cortical rigidity, cell rounding, and spindle morphogenesis during mitosis
    • Kunda, P., Pelling, A. E., Liu, T. & Baum, B. Moesin controls cortical rigidity, cell rounding, and spindle morphogenesis during mitosis. Curr. Biol. 18, 91-101 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 91-101
    • Kunda, P.1    Pelling, A.E.2    Liu, T.3    Baum, B.4
  • 41
    • 34249288541 scopus 로고    scopus 로고
    • Endosomal recycling controls plasma membrane area during mitosis
    • Boucrot, E. & Kirchhausen, T. Endosomal recycling controls plasma membrane area during mitosis. Proc. NatlAcad. Sci. USA 104, 7939-7944 (2007).
    • (2007) Proc. NatlAcad. Sci. USA , vol.104 , pp. 7939-7944
    • Boucrot, E.1    Kirchhausen, T.2
  • 42
    • 80052054346 scopus 로고    scopus 로고
    • Polar actomyosin contractility destabilizes the position of the cytokinetic furrow
    • Sedzinski, J. et al. Polar actomyosin contractility destabilizes the position of the cytokinetic furrow. Nature 476, 462-466 (2011).
    • (2011) Nature , vol.476 , pp. 462-466
    • Sedzinski, J.1
  • 43
    • 70549105793 scopus 로고    scopus 로고
    • Control of cell growth by the SCF and APC/C ubiquitin ligases
    • Skaar, J. R. & Pagano, M. Control of cell growth by the SCF and APC/C ubiquitin ligases. Curr. Opin. Cell Biol. 21, 816-824 (2009).
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 816-824
    • Skaar, J.R.1    Pagano, M.2
  • 44
    • 77954240714 scopus 로고    scopus 로고
    • SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelitythroughCP110degradation
    • D'Angiolella, V. et al. SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelitythroughCP110degradation. Nature 466, 138-142 (2010).
    • (2010) Nature , vol.466 , pp. 138-142
    • D'Angiolella, V.1
  • 45
    • 67549093540 scopus 로고    scopus 로고
    • SnapShot: F box proteins i
    • e1161
    • Skaar, J. R., Pagan, J. K. & Pagano, M. SnapShot: F box proteins I. Cell 137, 1160-1160 (2009)e1161.
    • (2009) Cell , vol.137 , pp. 1160-1160
    • Skaar, J.R.1    Pagan, J.K.2    Pagano, M.3
  • 46
    • 0037462424 scopus 로고    scopus 로고
    • Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase
    • Orlicky, S., Tang, X., Willems, A., Tyers, M. & Sicheri, F. Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell 112, 243-256 (2003).
    • (2003) Cell , vol.112 , pp. 243-256
    • Orlicky, S.1    Tang, X.2    Willems, A.3    Tyers, M.4    Sicheri, F.5
  • 47
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a ß-TrCP1-Skp1-ß-catenin complex: Destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase
    • Wu, G. et al. Structure of a ß-TrCP1-Skp1-ß-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. Mol. Cell 11, 1445-1456 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1445-1456
    • Wu, G.1
  • 48
    • 25844441096 scopus 로고    scopus 로고
    • Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase
    • Hao, B. et al. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol. Cell 20, 9-19 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 9-19
    • Hao, B.1
  • 49
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-cyclin e complex: Multisite-phosphorylated substrate recognition by SCF ubiquitin ligases
    • Hao, B., Oehlmann, S., Sowa, M. E., Harper, J. W. & Pavletich, N. P. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol. Cell 26, 131-143 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 50
    • 15444366629 scopus 로고    scopus 로고
    • FBW2 targets GCMa to the ubiquitin-proteasome degradation system
    • Yang, C. S. et al. FBW2 targets GCMa to the ubiquitin-proteasome degradation system. J. Biol. Chem. 280, 10083-10090 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 10083-10090
    • Yang, C.S.1
  • 51
    • 0035966288 scopus 로고    scopus 로고
    • Multisite phosphorylation and the countdown to S phase
    • Deshaies, R. J. & Ferrell, J. E. Jr Multisite phosphorylation and the countdown to S phase. Cell 107, 819-822 (2001).
    • (2001) Cell , vol.107 , pp. 819-822
    • Deshaies, R.J.1    Ferrell Jr., J.E.2
  • 52
    • 78650833597 scopus 로고    scopus 로고
    • Substrate-specific regulation of ubiquitination by the anaphase-promoting complex
    • Song, L. & Rape, M. Substrate-specific regulation of ubiquitination by the anaphase-promoting complex. Cell Cycle 10, 52-56 (2011).
    • (2011) Cell Cycle , vol.10 , pp. 52-56
    • Song, L.1    Rape, M.2
  • 53
    • 10344222932 scopus 로고    scopus 로고
    • A novel actin barbed-end-capping activity in EPS-8 regulates apical morphogenesis in intestinal cells of Caenorhabditis elegans
    • Croce, A. et al. A novel actin barbed-end-capping activity in EPS-8 regulates apical morphogenesis in intestinal cells of Caenorhabditis elegans. Nat. Cell Biol. 6, 1173-1179 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1173-1179
    • Croce, A.1
  • 54
    • 30444460120 scopus 로고    scopus 로고
    • Dynamic modes of the cortical actomyosin gel during cell locomotion and division
    • Paluch, E., Sykes, C., Prost, J. & Bornens, M. Dynamic modes of the cortical actomyosin gel during cell locomotion and division. Trends Cell Biol. 16, 5-10 (2006).
    • (2006) Trends Cell Biol. , vol.16 , pp. 5-10
    • Paluch, E.1    Sykes, C.2    Prost, J.3    Bornens, M.4
  • 55
    • 78651388574 scopus 로고    scopus 로고
    • Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding
    • Stewart, M. P. et al. Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding. Nature 469, 226-230 (2011).
    • (2011) Nature , vol.469 , pp. 226-230
    • Stewart, M.P.1
  • 56
    • 43949143882 scopus 로고    scopus 로고
    • Cappingprotein increases the rate ofactin-based motility by promoting filament nucleation by the Arp2/3 complex
    • Akin, O. & Mullins, R. D. Cappingprotein increases the rate ofactin-based motility by promoting filament nucleation by the Arp2/3 complex. Cell 133, 841-851 (2008).
    • (2008) Cell , vol.133 , pp. 841-851
    • Akin, O.1    Mullins, R.D.2
  • 57
    • 43949120138 scopus 로고    scopus 로고
    • Follow the monomer
    • Bear, J. E. Follow the monomer. Cell 133, 765-767 (2008).
    • (2008) Cell , vol.133 , pp. 765-767
    • Bear, J.E.1
  • 58
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25
    • Meulmeester, E., Kunze, M., Hsiao, H. H., Urlaub, H. & Melchior, F. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol. Cell 30, 610-619 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 59
    • 0025352187 scopus 로고
    • Advanced mammalian gene transfer: High titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line
    • Morgenstern, J. P. & Land, H. Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line. Nucl. Acids Res. 18, 3587-3596 (1990).
    • (1990) Nucl. Acids Res. , vol.18 , pp. 3587-3596
    • Morgenstern, J.P.1    Land, H.2
  • 60
    • 27644546219 scopus 로고    scopus 로고
    • In vitro reconstitution of SCF substrate ubiquitination with purified proteins
    • Petroski, M. D. & Deshaies, R. J. In vitro reconstitution of SCF substrate ubiquitination with purified proteins. Methods Enzymol. 398, 143-158 (2005).
    • (2005) Methods Enzymol. , vol.398 , pp. 143-158
    • Petroski, M.D.1    Deshaies, R.J.2
  • 61
    • 28844462033 scopus 로고    scopus 로고
    • Controlled synthesis of polyubiquitin chains
    • Pickart, C. M. & Raasi, S. Controlled synthesis of polyubiquitin chains. Methods Enzymol. 399, 21-36 (2005).
    • (2005) Methods Enzymol. , vol.399 , pp. 21-36
    • Pickart, C.M.1    Raasi, S.2
  • 62
    • 10544244161 scopus 로고    scopus 로고
    • Linking genome and proteome by mass spectrometry: Large-scale identification of yeast proteins from two dimensional gels
    • Shevchenko, A. et al. Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels. Proc. Natl Acad. Sci. USA93, 14440-14445 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14440-14445
    • Shevchenko, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.