메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Spatiotemporal analysis of RhoA/B/C activation in primary human endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CADHERIN; GREEN FLUORESCENT PROTEIN; LEUKOCYTE ANTIGEN; NOCODAZOLE; PHOTOPROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA PROTEIN, HUMAN; RHOB GUANINE NUCLEOTIDE BINDING PROTEIN; RHOC GUANINE NUCLEOTIDE BINDING PROTEIN; RHOC PROTEIN, HUMAN; THROMBIN; TUMOR NECROSIS FACTOR; VASCULAR ENDOTHELIAL CADHERIN; YELLOW FLUORESCENT PROTEIN, BACTERIA;

EID: 84966348740     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep25502     Document Type: Article
Times cited : (46)

References (61)
  • 1
    • 33846798106 scopus 로고    scopus 로고
    • Phenotypic heterogeneity of the endothelium: I. Structure, function, and mechanisms
    • Aird, W. C. Phenotypic heterogeneity of the endothelium: I. Structure, function, and mechanisms. Circ. Res. 100, 158-173 (2007).
    • (2007) Circ. Res. , vol.100 , pp. 158-173
    • Aird, W.C.1
  • 2
    • 33846849237 scopus 로고    scopus 로고
    • Phenotypic heterogeneity of the endothelium: II. Representative vascular beds
    • Aird, W. C. Phenotypic heterogeneity of the endothelium: II. Representative vascular beds. Circ. Res. 100, 174-190 (2007).
    • (2007) Circ. Res. , vol.100 , pp. 174-190
    • Aird, W.C.1
  • 3
    • 84867241703 scopus 로고    scopus 로고
    • Atheroprotective mechanisms of shear stress-regulated microRNAs
    • Boon, R. A., Hergenreider, E. & Dimmeler, S. Atheroprotective mechanisms of shear stress-regulated microRNAs. Thromb. Haemost. 108, 616-620 (2012).
    • (2012) Thromb. Haemost. , vol.108 , pp. 616-620
    • Boon, R.A.1    Hergenreider, E.2    Dimmeler, S.3
  • 4
    • 84930924311 scopus 로고    scopus 로고
    • Extracellular vesicle microRNA transfer in cardiovascular disease
    • Das, S. & Halushka, M. K. Extracellular vesicle microRNA transfer in cardiovascular disease. Cardiovasc. Pathol. 24, 199-206 (2015).
    • (2015) Cardiovasc. Pathol. , vol.24 , pp. 199-206
    • Das, S.1    Halushka, M.K.2
  • 5
    • 77951597881 scopus 로고    scopus 로고
    • Breaching multiple barriers: Leukocyte motility through venular walls and the interstitium
    • Nourshargh, S., Hordijk, P. L. & Sixt, M. Breaching multiple barriers: leukocyte motility through venular walls and the interstitium. Nat. Rev. Mol. Cell Biol. 11, 366-378 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 366-378
    • Nourshargh, S.1    Hordijk, P.L.2    Sixt, M.3
  • 6
    • 79751485813 scopus 로고    scopus 로고
    • Mechanisms of Leukocyte Transendothelial Migration
    • Muller, W. A. Mechanisms of Leukocyte Transendothelial Migration. Annu. Rev. Pathol. Mech. Dis. 6, 323-344 (2011).
    • (2011) Annu. Rev. Pathol. Mech. Dis. , vol.6 , pp. 323-344
    • Muller, W.A.1
  • 7
    • 84945471772 scopus 로고    scopus 로고
    • How leukocytes cross the vascular endothelium
    • Vestweber, D. How leukocytes cross the vascular endothelium. Nat. Publ. Gr. 15, 692-704 (2015).
    • (2015) Nat. Publ. Gr. , vol.15 , pp. 692-704
    • Vestweber, D.1
  • 8
    • 77951495204 scopus 로고    scopus 로고
    • Control of endothelial barrier function by regulating vascular endothelial-cadherin
    • Vestweber, D., Broermann, A. & Schulte, D. Control of endothelial barrier function by regulating vascular endothelial-cadherin. Curr. Opin. Hematol. 17, 230-236 (2010).
    • (2010) Curr. Opin. Hematol. , vol.17 , pp. 230-236
    • Vestweber, D.1    Broermann, A.2    Schulte, D.3
  • 9
    • 84935414352 scopus 로고    scopus 로고
    • Cell-stiffness-induced mechanosignaling - A key driver of leukocyte transendothelial migration
    • Schaefer, A. & Hordijk, P. L. Cell-stiffness-induced mechanosignaling - a key driver of leukocyte transendothelial migration. J. Cell Sci. 128, 2221-2230 (2015).
    • (2015) J. Cell Sci. , vol.128 , pp. 2221-2230
    • Schaefer, A.1    Hordijk, P.L.2
  • 10
    • 84942414356 scopus 로고    scopus 로고
    • Mechanisms of Vessel Pruning and Regression
    • Korn, C. & Augustin, H. G. Mechanisms of Vessel Pruning and Regression. Dev. Cell 34, 5-17 (2015).
    • (2015) Dev. Cell , vol.34 , pp. 5-17
    • Korn, C.1    Augustin, H.G.2
  • 11
    • 84973513794 scopus 로고    scopus 로고
    • Neovascularization of the atherosclerotic plaque: Interplay between atherosclerotic lesion, adventitia-derived microvessels and perivascular fat
    • van Hinsbergh, V. W. M., Eringa, E. C. & Daemen, M. J. A. P. Neovascularization of the atherosclerotic plaque: interplay between atherosclerotic lesion, adventitia-derived microvessels and perivascular fat. Curr. Opin. Lipidol. 26, 405-411 (2015).
    • (2015) Curr. Opin. Lipidol. , vol.26 , pp. 405-411
    • Van Hinsbergh, V.W.M.1    Eringa, E.C.2    Daemen, M.J.A.P.3
  • 12
    • 84875241774 scopus 로고    scopus 로고
    • The role of VE-cadherin in vascular morphogenesis and permeability control
    • Dejana, E. & Vestweber, D. The role of VE-cadherin in vascular morphogenesis and permeability control. Prog. Mol. Biol. Transl. Sci. 116, 119-144 (2013).
    • (2013) Prog. Mol. Biol. Transl. Sci. , vol.116 , pp. 119-144
    • Dejana, E.1    Vestweber, D.2
  • 13
    • 33644839612 scopus 로고    scopus 로고
    • Signaling mechanisms regulating endothelial permeability
    • Mehta, D. & Malik, A. B. Signaling mechanisms regulating endothelial permeability. Physiol. Rev. 86, 279-367 (2006).
    • (2006) Physiol. Rev. , vol.86 , pp. 279-367
    • Mehta, D.1    Malik, A.B.2
  • 14
    • 48049094159 scopus 로고    scopus 로고
    • The role of adherens junctions and VE-cadherin in the control of vascular permeability
    • Dejana, E., Orsenigo, F. & Lampugnani, M. G. The role of adherens junctions and VE-cadherin in the control of vascular permeability. J. Cell Sci. 121, 2115-2122 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2115-2122
    • Dejana, E.1    Orsenigo, F.2    Lampugnani, M.G.3
  • 15
    • 0028900299 scopus 로고
    • The molecular organization of endothelial cell to cell junctions: Differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular endothelial cadherin (VE-cadherin)
    • Lampugnani, M. G. et al. The molecular organization of endothelial cell to cell junctions: differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular endothelial cadherin (VE-cadherin). J. Cell Biol. 129, 203-217 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 203-217
    • Lampugnani, M.G.1
  • 16
    • 0029858026 scopus 로고    scopus 로고
    • Endothelial adherens junctions: Implications in the control of vascular permeability and angiogenesis
    • Dejana, E. Endothelial adherens junctions: implications in the control of vascular permeability and angiogenesis. J. Clin. Invest. 98, 1949-1953 (1996).
    • (1996) J. Clin. Invest. , vol.98 , pp. 1949-1953
    • Dejana, E.1
  • 17
    • 84884149475 scopus 로고    scopus 로고
    • VE-cadherin and endothelial adherens junctions: Active guardians of vascular integrity
    • Giannotta, M., Trani, M. & Dejana, E. VE-cadherin and endothelial adherens junctions: active guardians of vascular integrity. Dev. Cell 26, 441-454 (2013).
    • (2013) Dev. Cell , vol.26 , pp. 441-454
    • Giannotta, M.1    Trani, M.2    Dejana, E.3
  • 18
    • 84899450606 scopus 로고    scopus 로고
    • Dynamics between actin and the VE-cadherin/catenin complex: Novel aspects of the ARP2/3 complex in regulation of endothelial junctions
    • Abu Taha, A. & Schnittler, H.-J. Dynamics between actin and the VE-cadherin/catenin complex: novel aspects of the ARP2/3 complex in regulation of endothelial junctions. Cell Adh. Migr. 8, 125-135 (2014).
    • (2014) Cell Adh. Migr. , vol.8 , pp. 125-135
    • Abu Taha, A.1    Schnittler, H.-J.2
  • 20
    • 84914115812 scopus 로고    scopus 로고
    • TNF-induced endothelial barrier disruption: Beyond actin and Rho
    • Marcos-Ramiro, B., García-Weber, D. & Millán, J. TNF-induced endothelial barrier disruption: beyond actin and Rho. Thromb. Haemost. 112, 1088-1102 (2014).
    • (2014) Thromb. Haemost. , vol.112 , pp. 1088-1102
    • Marcos-Ramiro, B.1    García-Weber, D.2    Millán, J.3
  • 21
    • 84925352315 scopus 로고    scopus 로고
    • Cadherins in tissue architecture and disease
    • Vestweber, D. Cadherins in tissue architecture and disease. J. Mol. Med. (Berl). 93, 5-11 (2015).
    • (2015) J. Mol. Med. (Berl) , vol.93 , pp. 5-11
    • Vestweber, D.1
  • 22
    • 84946882340 scopus 로고    scopus 로고
    • Localized signals that regulate transendothelial migration
    • Muller, W. A. Localized signals that regulate transendothelial migration. Curr. Opin. Immunol. 38, 24-29 (2016).
    • (2016) Curr. Opin. Immunol. , vol.38 , pp. 24-29
    • Muller, W.A.1
  • 23
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe, A. B. & Hall, A. Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21, 247-269 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 24
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley, A. J. Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 16, 522-529 (2006).
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 25
    • 84922251368 scopus 로고    scopus 로고
    • Toward understanding RhoGTPase specificity: Structure, function and local activation
    • Schaefer, A., Reinhard, N. R. & Hordijk, P. L. Toward understanding RhoGTPase specificity: structure, function and local activation. Small GTPases 5, 1-11 (2014).
    • (2014) Small GTPases , vol.5 , pp. 1-11
    • Schaefer, A.1    Reinhard, N.R.2    Hordijk, P.L.3
  • 26
    • 84874433733 scopus 로고    scopus 로고
    • Regulation of small GTPases by GEFs, GAPs, and GDIs
    • Cherfils, J. & Zeghouf, M. Regulation of small GTPases by GEFs, GAPs, and GDIs. Physiol. Rev. 93, 269-309 (2013).
    • (2013) Physiol. Rev. , vol.93 , pp. 269-309
    • Cherfils, J.1    Zeghouf, M.2
  • 27
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • Bos, J. L., Rehmann, H. & Wittinghofer, A. GEFs and GAPs: critical elements in the control of small G proteins. Cell 129, 865-877 (2007).
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 29
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • Wittinghofer, A. & Vetter, I. R. Structure-function relationships of the G domain, a canonical switch motif. Annu. Rev. Biochem. 80, 943-971 (2011).
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 30
  • 31
    • 0344305784 scopus 로고    scopus 로고
    • Cell migration: Integrating signals from front to back
    • Ridley, A. J. et al. Cell migration: integrating signals from front to back. Science 302, 1704-1709 (2003).
    • (2003) Science , vol.302 , pp. 1704-1709
    • Ridley, A.J.1
  • 32
    • 84941283246 scopus 로고    scopus 로고
    • Rho GTPase signalling in cell migration
    • Ridley, A. J. Rho GTPase signalling in cell migration. Curr. Opin. Cell Biol. 36, 103-112 (2015).
    • (2015) Curr. Opin. Cell Biol. , vol.36 , pp. 103-112
    • Ridley, A.J.1
  • 34
    • 84924359656 scopus 로고    scopus 로고
    • Between Rho(k) and a hard place: The relation between vessel wall stiffness, endothelial contractility, and cardiovascular disease
    • Huveneers, S., Daemen, M. J. A. P. & Hordijk, P. L. Between Rho(k) and a hard place: the relation between vessel wall stiffness, endothelial contractility, and cardiovascular disease. Circ. Res. 116, 895-908 (2015).
    • (2015) Circ. Res. , vol.116 , pp. 895-908
    • Huveneers, S.1    Daemen, M.J.A.P.2    Hordijk, P.L.3
  • 36
    • 0029889591 scopus 로고    scopus 로고
    • Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain
    • Reid, T. et al. Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. J. Biol. Chem. 271, 13556-13560 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 13556-13560
    • Reid, T.1
  • 37
    • 0034682993 scopus 로고    scopus 로고
    • Activation of RhoA by Thrombin in Endothelial Hyperpermeability : Role of Rho Kinase and Protein Tyrosine Kinases
    • Amerongen, G. P. v. N., Delft, S. v., Vermeer, M. A., Collard, J. G. & van Hinsbergh, V. W. M. Activation of RhoA by Thrombin in Endothelial Hyperpermeability : Role of Rho Kinase and Protein Tyrosine Kinases. Circ. Res. 87, 335-340 (2000).
    • (2000) Circ. Res. , vol.87 , pp. 335-340
    • Amerongen, G.P.V.N.1    Delft, S.V.2    Vermeer, M.A.3    Collard, J.G.4    Van Hinsbergh, V.W.M.5
  • 38
    • 0036357937 scopus 로고    scopus 로고
    • Molecular mechanisms of thrombin-induced endothelial cell permeability
    • Bogatcheva, N. V., Garcia, J. G. N. & Verin, A. D. Molecular mechanisms of thrombin-induced endothelial cell permeability. Biochem. (Mosc). 67, 75-84 (2002).
    • (2002) Biochem. (Mosc) , vol.67 , pp. 75-84
    • Bogatcheva, N.V.1    Garcia, J.G.N.2    Verin, A.D.3
  • 39
    • 84926642278 scopus 로고    scopus 로고
    • Interplay between chemotaxis and contact inhibition of locomotion determines exploratory cell migration
    • Lin, B., Yin, T., Wu, Y. I., Inoue, T. & Levchenko, A. Interplay between chemotaxis and contact inhibition of locomotion determines exploratory cell migration. Nat. Commun. 6, 7619 (2015).
    • (2015) Nat. Commun. , vol.6 , pp. 7619
    • Lin, B.1    Yin, T.2    Wu, Y.I.3    Inoue, T.4    Levchenko, A.5
  • 40
    • 84942893087 scopus 로고    scopus 로고
    • Plasma membrane restricted RhoGEF activity is sufficient for RhoA-mediated actin polymerization
    • van Unen, J. et al. Plasma membrane restricted RhoGEF activity is sufficient for RhoA-mediated actin polymerization. Sci. Rep. 5, 14693 (2015).
    • (2015) Sci. Rep. , vol.5 , pp. 14693
    • Van Unen, J.1
  • 41
    • 84893202278 scopus 로고    scopus 로고
    • The Rac1 hypervariable region in targeting and signaling: A tail of many stories
    • Lam, B. D. & Hordijk, P. L. The Rac1 hypervariable region in targeting and signaling: a tail of many stories. Small GTPases 4, 78-89 (2013).
    • (2013) Small GTPases , vol.4 , pp. 78-89
    • Lam, B.D.1    Hordijk, P.L.2
  • 42
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • Michaelson, D. et al. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152, 111-126 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1
  • 43
    • 21644478501 scopus 로고    scopus 로고
    • RhoB regulates endosome transport by promoting actin assembly on endosomal membranes through Dia1
    • Fernandez-Borja, M., Janssen, L., Verwoerd, D., Hordijk, P. & Neefjes, J. RhoB regulates endosome transport by promoting actin assembly on endosomal membranes through Dia1. J. Cell Sci. 118, 2661-2670 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 2661-2670
    • Fernandez-Borja, M.1    Janssen, L.2    Verwoerd, D.3    Hordijk, P.4    Neefjes, J.5
  • 44
    • 48249098842 scopus 로고    scopus 로고
    • GEF-H1 couples nocodazole-induced microtubule disassembly to cell contractility via RhoA
    • Chang, Y.-C., Nalbant, P., Birkenfeld, J., Chang, Z.-F. & Bokoch, G. M. GEF-H1 couples nocodazole-induced microtubule disassembly to cell contractility via RhoA. Mol. Biol. Cell 19, 2147-2153 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2147-2153
    • Chang, Y.-C.1    Nalbant, P.2    Birkenfeld, J.3    Chang, Z.-F.4    Bokoch, G.M.5
  • 45
    • 0032567341 scopus 로고    scopus 로고
    • Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases
    • Ren, Y., Li, R., Zheng, Y. & Busch, H. Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J. Biol. Chem. 273, 34954-34960 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 34954-34960
    • Ren, Y.1    Li, R.2    Zheng, Y.3    Busch, H.4
  • 47
    • 10044270843 scopus 로고    scopus 로고
    • Novel role of microtubules in thrombin-induced endothelial barrier dysfunction
    • Birukova, A. A. et al. Novel role of microtubules in thrombin-induced endothelial barrier dysfunction. FASEB J. 18, 1879-90 (2004).
    • (2004) FASEB J. , vol.18 , pp. 1879-1890
    • Birukova, A.A.1
  • 48
    • 0037044785 scopus 로고    scopus 로고
    • XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC
    • Arthur, W. T., Ellerbroek, S. M., Der, C. J., Burridge, K. & Wennerberg, K. XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC. J. Biol. Chem. 277, 42964-72 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 42964-42972
    • Arthur, W.T.1    Ellerbroek, S.M.2    Der, C.J.3    Burridge, K.4    Wennerberg, K.5
  • 49
    • 84879993509 scopus 로고    scopus 로고
    • Rasip1 mediates Rap1 regulation of Rho in endothelial barrier function through ArhGAP29
    • Post, A. et al. Rasip1 mediates Rap1 regulation of Rho in endothelial barrier function through ArhGAP29. Proc. Natl. Acad. Sci. USA 110, 11427-32 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 11427-11432
    • Post, A.1
  • 50
    • 80053262749 scopus 로고    scopus 로고
    • Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction control
    • Pannekoek, W. J. et al. Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction control. Cell. Signal. 23, 2056-2064 (2011).
    • (2011) Cell. Signal , vol.23 , pp. 2056-2064
    • Pannekoek, W.J.1
  • 51
    • 84884168966 scopus 로고    scopus 로고
    • RhoA, RhoB and RhoC have different roles in cancer cell migration
    • Ridley, A. J. RhoA, RhoB and RhoC have different roles in cancer cell migration. J. Microsc. 251, 242-249 (2013).
    • (2013) J. Microsc. , vol.251 , pp. 242-249
    • Ridley, A.J.1
  • 52
    • 84946082846 scopus 로고    scopus 로고
    • RhoC maintains vascular homeostasis by regulating VEGF-induced signaling in endothelial cells
    • Hoeppner, L. H. et al. RhoC maintains vascular homeostasis by regulating VEGF-induced signaling in endothelial cells. J. Cell Sci. 128, 3556-3568 (2015).
    • (2015) J. Cell Sci. , vol.128 , pp. 3556-3568
    • Hoeppner, L.H.1
  • 53
    • 84876927634 scopus 로고    scopus 로고
    • PDZ-RhoGEF and LARG are essential for embryonic development and provide a link between thrombin and LPA receptors and Rho activation
    • Mikelis, C. M. et al. PDZ-RhoGEF and LARG are essential for embryonic development and provide a link between thrombin and LPA receptors and Rho activation. J. Biol. Chem. 288, 12232-12243 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 12232-12243
    • Mikelis, C.M.1
  • 54
    • 84919874130 scopus 로고    scopus 로고
    • Mechanistic insight into GPCR-mediated activation of the microtubule-associated RhoA exchange factor GEF-H1
    • Meiri, D. et al. Mechanistic insight into GPCR-mediated activation of the microtubule-associated RhoA exchange factor GEF-H1. Nat. Commun. 5, 4857 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4857
    • Meiri, D.1
  • 55
    • 79955425392 scopus 로고    scopus 로고
    • A novel spatiotemporal RhoC activation pathway locally regulates cofilin activity at invadopodia
    • Bravo-Cordero, J. J. et al. A novel spatiotemporal RhoC activation pathway locally regulates cofilin activity at invadopodia. Curr. Biol. 21, 635-644 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 635-644
    • Bravo-Cordero, J.J.1
  • 56
    • 84892419336 scopus 로고    scopus 로고
    • A RhoC biosensor reveals differences in the activation kinetics of RhoA and RhoC in migrating cells
    • Zawistowski, J. S., Sabouri-Ghomi, M., Danuser, G., Hahn, K. M. & Hodgson, L. A RhoC biosensor reveals differences in the activation kinetics of RhoA and RhoC in migrating cells. PLos One 8, e79877 (2013).
    • (2013) PLos One , vol.8
    • Zawistowski, J.S.1    Sabouri-Ghomi, M.2    Danuser, G.3    Hahn, K.M.4    Hodgson, L.5
  • 57
    • 84887572710 scopus 로고    scopus 로고
    • Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB
    • Hutchinson, C. L., Lowe, P. N., McLaughlin, S. H., Mott, H. R. & Owen, D. Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB. Biochemistry 52, 7999-8011 (2013).
    • (2013) Biochemistry , vol.52 , pp. 7999-8011
    • Hutchinson, C.L.1    Lowe, P.N.2    McLaughlin, S.H.3    Mott, H.R.4    Owen, D.5
  • 58
    • 84940173841 scopus 로고    scopus 로고
    • G Protein-Coupled Receptor and RhoA-Stimulated Transcriptional Responses: Links to Inflammation, Differentiation, and Cell Proliferation
    • Yu, O. M. & Brown, J. H. G Protein-Coupled Receptor and RhoA-Stimulated Transcriptional Responses: Links to Inflammation, Differentiation, and Cell Proliferation. Mol. Pharmacol. 88, 171-180 (2015).
    • (2015) Mol. Pharmacol. , vol.88 , pp. 171-180
    • Yu, O.M.1    Brown, J.H.2
  • 59
    • 85006314494 scopus 로고    scopus 로고
    • A novel Epac-specific cAMP analogue demonstrates independent regulation of Rap1 and ERK
    • Enserink, J. M. et al. A novel Epac-specific cAMP analogue demonstrates independent regulation of Rap1 and ERK. Nat. Cell Biol. 4, 901-906 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 901-906
    • Enserink, J.M.1
  • 60
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates Rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander, E. E., Ten Klooster, J. P., Van Delft, S., Van Der Kammen, R. A. & Collard, J. G. Rac downregulates Rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147, 1009-1021 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1009-1021
    • Sander, E.E.1    Ten Klooster, J.P.2    Van Delft, S.3    Van Der Kammen, R.A.4    Collard, J.G.5
  • 61
    • 84939474806 scopus 로고    scopus 로고
    • A local VE-cadherin and Trio-based signaling complex stabilizes endothelial junctions through Rac1
    • Timmerman, I. et al. A local VE-cadherin and Trio-based signaling complex stabilizes endothelial junctions through Rac1. J. Cell Sci. 128, 3041-3054 (2015).
    • (2015) J. Cell Sci. , vol.128 , pp. 3041-3054
    • Timmerman, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.