메뉴 건너뛰기




Volumn 3, Issue 8, 2011, Pages 1-17

Phosphoinositides in cell architecture

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84863874680     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a004796     Document Type: Review
Times cited : (147)

References (130)
  • 1
    • 77952158913 scopus 로고    scopus 로고
    • PAR-3 mediates the initial clustering and apical localization of junction and polarity proteins during C. elegans intestinal epithelial cell polarization
    • Achilleos A, Wehman AM, Nance J. 2010. PAR-3 mediates the initial clustering and apical localization of junction and polarity proteins during C. elegans intestinal epithelial cell polarization. Development 137: 1833-1842.
    • (2010) Development , vol.137 , pp. 1833-1842
    • Achilleos, A.1    Wehman, A.M.2    Nance, J.3
  • 2
    • 4944259722 scopus 로고    scopus 로고
    • Reversal of glandular polarity in the lymphovascular compartment of breast cancer
    • Adams SA, Smith ME, Cowley GP, Carr LA. 2004. Reversal of glandular polarity in the lymphovascular compartment of breast cancer. J Clin Pathol 57: 1114-1117.
    • (2004) J Clin Pathol , vol.57 , pp. 1114-1117
    • Adams, S.A.1    Smith, M.E.2    Cowley, G.P.3    Carr, L.A.4
  • 3
    • 34547573606 scopus 로고    scopus 로고
    • Replacement of nonmuscle myosin II-B with II-A rescues brain but not cardiac defects in mice
    • Bao J, MaX, Liu C, Adelstein RS. 2007. Replacement of nonmuscle myosin II-B with II-A rescues brain but not cardiac defects in mice. J Biol Chem 282: 22102-22111.
    • (2007) J Biol Chem , vol.282 , pp. 22102-22111
    • Bao, J.1    Ma, X.2    Liu, C.3    Adelstein, R.S.4
  • 4
    • 72549104085 scopus 로고    scopus 로고
    • Nuclear phosphoinositides: A signaling enigma wrapped in a compartmental conundrum
    • Barlow CA, Laishram RS, Anderson RA. 2009. Nuclear phosphoinositides: A signaling enigma wrapped in a compartmental conundrum. Trends Cell Biol 20: 25-35.
    • (2009) Trends Cell Biol , vol.20 , pp. 25-35
    • Barlow, C.A.1    Laishram, R.S.2    Anderson, R.A.3
  • 5
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia R, Munro S. 2005. Organelle identity and the signposts for membrane traffic. Nature 438: 597-604.
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 6
    • 33748309166 scopus 로고    scopus 로고
    • Adhesionmediated mechanosensitivity: A time to experiment, and a time to theorize
    • Bershadsky A, Kozlov M, Geiger B. 2006. Adhesionmediated mechanosensitivity: a time to experiment, and a time to theorize. Curr Opin Cell Biol 18: 472-481.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 472-481
    • Bershadsky, A.1    Kozlov, M.2    Geiger, B.3
  • 7
    • 33748920035 scopus 로고    scopus 로고
    • Multicellular rosette formation links planar cell polarity to tissue morphogenesis
    • Blankenship JT, Backovic ST, Sanny JS, Weitz O, Zallen JA. 2006. Multicellular rosette formation links planar cell polarity to tissue morphogenesis. Dev Cell 11: 459-470.
    • (2006) Dev Cell , vol.11 , pp. 459-470
    • Blankenship, J.T.1    Backovic, S.T.2    Sanny, J.S.3    Weitz, O.4    Zallen, J.A.5
  • 8
    • 77951568703 scopus 로고    scopus 로고
    • Phosphoinositide signalling in cancer: Beyond PI3K and PTEN
    • Bunney TD, Katan M. 2010. Phosphoinositide signalling in cancer: Beyond PI3K and PTEN. Nat Rev Cancer 10: 342-352.
    • (2010) Nat Rev Cancer , vol.10 , pp. 342-352
    • Bunney, T.D.1    Katan, M.2
  • 9
    • 58149395054 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases in cell migration
    • Cain RJ, Ridley AJ. 2009. Phosphoinositide 3-kinases in cell migration. Biol Cell 101: 13-29.
    • (2009) Biol Cell , vol.101 , pp. 13-29
    • Cain, R.J.1    Ridley, A.J.2
  • 10
    • 77952929975 scopus 로고    scopus 로고
    • Molecular bases of cell-cell junctions stability and dynamics
    • Cavey M, Lecuit T. 2009. Molecular bases of cell-cell junctions stability and dynamics. Cold Spring Harb Perspect Biol 1: a002998.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Cavey, M.1    Lecuit, T.2
  • 11
    • 14744289370 scopus 로고    scopus 로고
    • Par-3 controls tight junction assembly through the Rac exchange factor Tiam1
    • Chen X, Macara IG. 2005. Par-3 controls tight junction assembly through the Rac exchange factor Tiam1. Nat Cell Biol 7: 262-269.
    • (2005) Nat Cell Biol , vol.7 , pp. 262-269
    • Chen, X.1    Macara, I.G.2
  • 12
    • 70350617938 scopus 로고    scopus 로고
    • The involvement of lethal giant larvae and Wnt signaling in bottle cell formation in Xenopus embryos
    • Choi SC, Sokol SY. 2009. The involvement of lethal giant larvae and Wnt signaling in bottle cell formation in Xenopus embryos. Dev Biol 336: 68-75.
    • (2009) Dev Biol , vol.336 , pp. 68-75
    • Choi, S.C.1    Sokol, S.Y.2
  • 13
    • 33646184680 scopus 로고    scopus 로고
    • ARF proteins: Roles in membrane traffic and beyond
    • D'Souza-Schorey C, Chavrier P. 2006. ARF proteins: Roles in membrane traffic and beyond. Nat Rev Mol Cell Biol 7: 347-358.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 347-358
    • D'Souza-Schorey, C.1    Chavrier, P.2
  • 14
    • 77952132991 scopus 로고    scopus 로고
    • The PAR complex regulates pulsed actomyosin contractions during amnioserosa apical constriction in Drosophila
    • David DJ, Tishkina A, Harris TJ. 2010. The PAR complex regulates pulsed actomyosin contractions during amnioserosa apical constriction in Drosophila. Development 137: 1645-1655.
    • (2010) Development , vol.137 , pp. 1645-1655
    • David, D.J.1    Tishkina, A.2    Harris, T.J.3
  • 15
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G, De Camilli P. 2006. Phosphoinositides in cell regulation and membrane dynamics. Nature 443: 651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    de Camilli, P.2
  • 16
    • 53149149836 scopus 로고    scopus 로고
    • Par-3-mediated junctional localization of the lipid phosphatase PTEN is required for cell polarity establishment
    • Feng W, Wu H, Chan LN, Zhang M. 2008. Par-3-mediated junctional localization of the lipid phosphatase PTEN is required for cell polarity establishment. J Biol Chem 283: 23440-23449.
    • (2008) J Biol Chem , vol.283 , pp. 23440-23449
    • Feng, W.1    Wu, H.2    Chan, L.N.3    Zhang, M.4
  • 17
    • 77649219554 scopus 로고    scopus 로고
    • Cell mechanics and feedback regulation of actomyosin networks
    • Fernandez-Gonzalez R, Zallen JA. 2009. Cell mechanics and feedback regulation of actomyosin networks. Sci Signal 2: e78.
    • (2009) Sci Signal , vol.2
    • Fernandez-Gonzalez, R.1    Zallen, J.A.2
  • 19
    • 66249146420 scopus 로고    scopus 로고
    • Interaction of E-cadherin and PTEN regulates morphogenesis and growth arrest in human mammary epithelial cells
    • Fournier MV, Fata JE, Martin KJ, Yaswen P, Bissell MJ. 2009. Interaction of E-cadherin and PTEN regulates morphogenesis and growth arrest in human mammary epithelial cells. Cancer Res 69: 4545-4552.
    • (2009) Cancer Res , vol.69 , pp. 4545-4552
    • Fournier, M.V.1    Fata, J.E.2    Martin, K.J.3    Yaswen, P.4    Bissell, M.J.5
  • 20
    • 33748199154 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells
    • Gassama-Diagne A, YuW, ter Beest M, Martin-Belmonte F, Kierbel A, Engel J, Mostov K. 2006. Phosphatidylinositol-3,4,5-trisphosphate regulates the formation of the basolateral plasma membrane in epithelial cells. Nat Cell Biol 8: 963-970.
    • (2006) Nat Cell Biol , vol.8 , pp. 963-970
    • Gassama-Diagne, A.1    Yu, W.2    ter Beest, M.3    Martin-Belmonte, F.4    Kierbel, A.5    Engel, J.6    Mostov, K.7
  • 21
    • 77951189656 scopus 로고    scopus 로고
    • Polarity proteins and Rho GTPases cooperate to spatially organise epithelial actinbased protrusions
    • Georgiou M, Baum B. 2010. Polarity proteins and Rho GTPases cooperate to spatially organise epithelial actinbased protrusions. J Cell Sci 123: 1089-1098.
    • (2010) J Cell Sci , vol.123 , pp. 1089-1098
    • Georgiou, M.1    Baum, B.2
  • 22
    • 55249111248 scopus 로고    scopus 로고
    • Cdc42, Par6, and aPKC regulate Arp2/3-mediated endocytosis to control local adherens junction stability
    • Georgiou M, Marinari E, Burden J, Baum B. 2008. Cdc42, Par6, and aPKC regulate Arp2/3-mediated endocytosis to control local adherens junction stability. Curr Biol 18: 1631-1638.
    • (2008) Curr Biol , vol.18 , pp. 1631-1638
    • Georgiou, M.1    Marinari, E.2    Burden, J.3    Baum, B.4
  • 23
    • 41049085170 scopus 로고    scopus 로고
    • Choose your own path: Specificity in Ras GTPase signaling
    • Goldfinger LE. 2008. Choose your own path: Specificity in Ras GTPase signaling. Mol Biosyst 4: 293-299.
    • (2008) Mol Biosyst , vol.4 , pp. 293-299
    • Goldfinger, L.E.1
  • 24
    • 35549001736 scopus 로고    scopus 로고
    • The PAR proteins: Fundamental players in animal cell polarization
    • Goldstein B, Macara IG. 2007. The PAR proteins: Fundamental players in animal cell polarization. Dev Cell 13: 609-622.
    • (2007) Dev Cell , vol.13 , pp. 609-622
    • Goldstein, B.1    Macara, I.G.2
  • 25
    • 33947305087 scopus 로고    scopus 로고
    • aPKC-PAR complex dysfunction and tight junction disassembly in renal epithelial cells during ATP depletion
    • Gopalakrishnan S, Hallett MA, Atkinson SJ, Marrs JA. 2007. aPKC-PAR complex dysfunction and tight junction disassembly in renal epithelial cells during ATP depletion. Am J Physiol Cell Physiol 292: C1094-1102.
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. 1094-1102
    • Gopalakrishnan, S.1    Hallett, M.A.2    Atkinson, S.J.3    Marrs, J.A.4
  • 26
    • 33744956177 scopus 로고    scopus 로고
    • Phosphatidylinositol 5-kinase stimulates apical biosynthetic delivery via an Arp2/3-dependent mechanism
    • Guerriero CJ, Weixel KM, Bruns JR, Weisz OA. 2006. Phosphatidylinositol 5-kinase stimulates apical biosynthetic delivery via an Arp2/3-dependent mechanism. J Biol Chem 281: 15376-15384.
    • (2006) J Biol Chem , vol.281 , pp. 15376-15384
    • Guerriero, C.J.1    Weixel, K.M.2    Bruns, J.R.3    Weisz, O.A.4
  • 27
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. 1994. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 371: 168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 28
    • 24144443830 scopus 로고    scopus 로고
    • The positioning and segregation of apical cues during epithelial polarity establishment in Drosophila
    • Harris TJ, Peifer M. 2005. The positioning and segregation of apical cues during epithelial polarity establishment in Drosophila. J Cell Biol 170: 813-823.
    • (2005) J Cell Biol , vol.170 , pp. 813-823
    • Harris, T.J.1    Peifer, M.2
  • 29
    • 58249094157 scopus 로고    scopus 로고
    • Cdc42 and Par proteins stabilize dynamic adherens junctions in the Drosophila neuroectoderm through regulation of apical endocytosis
    • Harris KP, Tepass U. 2008. Cdc42 and Par proteins stabilize dynamic adherens junctions in the Drosophila neuroectoderm through regulation of apical endocytosis. J Cell Biol 183: 1129-1143.
    • (2008) J Cell Biol , vol.183 , pp. 1129-1143
    • Harris, K.P.1    Tepass, U.2
  • 30
    • 77953878405 scopus 로고    scopus 로고
    • Adherens junctions: From molecules to morphogenesis
    • Harris TJ, Tepass U. 2010. Adherens junctions: From molecules to morphogenesis. Nat Rev Mol Cell Biol 11: 502-514.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 502-514
    • Harris, T.J.1    Tepass, U.2
  • 32
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: New insights into their functions from in vivo studies
    • Heasman SJ, Ridley AJ. 2008. Mammalian Rho GTPases: New insights into their functions from in vivo studies. Nat Rev Mol Cell Biol 9: 690-701.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 33
    • 39849103291 scopus 로고    scopus 로고
    • A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions
    • Ivanov AI, Bachar M, Babbin BA, Adelstein RS, Nusrat A, Parkos CA. 2007. A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions. PLoS One 2: e658.
    • (2007) PLoS One , vol.2
    • Ivanov, A.I.1    Bachar, M.2    Babbin, B.A.3    Adelstein, R.S.4    Nusrat, A.5    Parkos, C.A.6
  • 34
    • 58149191544 scopus 로고    scopus 로고
    • Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis
    • Jaffe AB, Kaji N, Durgan J, Hall A. 2008. Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis. J Cell Biol 183: 625-633.
    • (2008) J Cell Biol , vol.183 , pp. 625-633
    • Jaffe, A.B.1    Kaji, N.2    Durgan, J.3    Hall, A.4
  • 35
    • 77449083401 scopus 로고    scopus 로고
    • 0-kinase signalling supports cell height in established epithelial monolayers
    • 0-kinase signalling supports cell height in established epithelial monolayers. J Mol Histol 40: 395-405.
    • (2009) J Mol Histol , vol.40 , pp. 395-405
    • Jeanes, A.1    Smutny, M.2    Leerberg, J.M.3    Yap, A.S.4
  • 36
    • 0024284814 scopus 로고
    • Identification of genes required for cytoplasmic localization in early C. elegans embryos
    • Kemphues KJ, Priess JR, Morton DG, Cheng NS. 1988. Identification of genes required for cytoplasmic localization in early C. elegans embryos. Cell 52: 311-320.
    • (1988) Cell , vol.52 , pp. 311-320
    • Kemphues, K.J.1    Priess, J.R.2    Morton, D.G.3    Cheng, N.S.4
  • 37
    • 0032563207 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase induces scattering and tubulogenesis in epithelial cells through a novel pathway
    • Khwaja A, Lehmann K, Marte BM, Downward J. 1998. Phosphoinositide 3-kinase induces scattering and tubulogenesis in epithelial cells through a novel pathway. J Biol Chem 273: 18793-18801.
    • (1998) J Biol Chem , vol.273 , pp. 18793-18801
    • Khwaja, A.1    Lehmann, K.2    Marte, B.M.3    Downward, J.4
  • 38
    • 11244250646 scopus 로고    scopus 로고
    • Implication of the MAGI-1b/PTEN signalosome in stabilization of adherens junctions and suppression of invasiveness
    • Kotelevets L, van Hengel J, Bruyneel E, Mareel M, van Roy F, Chastre E. 2005. Implication of the MAGI-1b/PTEN signalosome in stabilization of adherens junctions and suppression of invasiveness. FASEB J 19: 115-117.
    • (2005) FASEB J , vol.19 , pp. 115-117
    • Kotelevets, L.1    van Hengel, J.2    Bruyneel, E.3    Mareel, M.4    van Roy, F.5    Chastre, E.6
  • 39
    • 0037155159 scopus 로고    scopus 로고
    • E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts
    • Kovacs EM, Ali RG, McCormack AJ, Yap AS. 2002. E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts. J Biol Chem 277: 6708-6718.
    • (2002) J Biol Chem , vol.277 , pp. 6708-6718
    • Kovacs, E.M.1    Ali, R.G.2    McCormack, A.J.3    Yap, A.S.4
  • 40
    • 1642448472 scopus 로고    scopus 로고
    • Functional divergence of human cytoplasmic myosin II: Kinetic characterization of the non-muscle IIA isoform
    • Kovacs M, Wang F, Hu A, Zhang Y, Sellers JR. 2003. Functional divergence of human cytoplasmic myosin II: Kinetic characterization of the non-muscle IIA isoform. J Biol Chem 278: 38132-38140.
    • (2003) J Biol Chem , vol.278 , pp. 38132-38140
    • Kovacs, M.1    Wang, F.2    Hu, A.3    Zhang, Y.4    Sellers, J.R.5
  • 41
    • 77950462697 scopus 로고    scopus 로고
    • Membrane targeting of Bazooka/PAR-3 is mediated by direct binding to phosphoinositide lipids
    • Krahn MP, Klopfenstein DR, Fischer N, Wodarz A. 2010. Membrane targeting of Bazooka/PAR-3 is mediated by direct binding to phosphoinositide lipids. Curr Biol 20: 636-642.
    • (2010) Curr Biol , vol.20 , pp. 636-642
    • Krahn, M.P.1    Klopfenstein, D.R.2    Fischer, N.3    Wodarz, A.4
  • 42
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski R, Hall A, Mellman I. 1999. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat Cell Biol 1: 8-13.
    • (1999) Nat Cell Biol , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 43
    • 70349566487 scopus 로고    scopus 로고
    • The WASP and WAVE family proteins
    • Kurisu S, Takenawa T. 2009. The WASP and WAVE family proteins. Genome Biol 10: 226.
    • (2009) Genome Biol , vol.10 , pp. 226
    • Kurisu, S.1    Takenawa, T.2
  • 44
    • 77953762012 scopus 로고    scopus 로고
    • Translation of the phosphoinositide code by PI effectors
    • Kutateladze TG. 2010. Translation of the phosphoinositide code by PI effectors. Nat Chem Biol 6: 507-513.
    • (2010) Nat Chem Biol , vol.6 , pp. 507-513
    • Kutateladze, T.G.1
  • 45
    • 77954410997 scopus 로고    scopus 로고
    • Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner
    • Le Duc Q, Shi Q, Blonk I, Sonnenberg A, Wang N, Leckband D, de Rooij J. 2010. Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J Cell Biol 189: 1107-1115.
    • (2010) J Cell Biol , vol.189 , pp. 1107-1115
    • Le Duc, Q.1    Shi, Q.2    Blonk, I.3    Sonnenberg, A.4    Wang, N.5    Leckband, D.6    de Rooij, J.7
  • 46
    • 33748195976 scopus 로고    scopus 로고
    • Mechanism and dynamics of cadherin adhesion
    • Leckband D, Prakasam A. 2006. Mechanism and dynamics of cadherin adhesion. Annu Rev Biomed Eng 8: 259-287.
    • (2006) Annu Rev Biomed Eng , vol.8 , pp. 259-287
    • Leckband, D.1    Prakasam, A.2
  • 47
    • 44449135987 scopus 로고    scopus 로고
    • Cell polarity and cancer-Cell and tissue polarity as a non-canonical tumor suppressor
    • Lee M, Vasioukhin V. 2008. Cell polarity and cancer-Cell and tissue polarity as a non-canonical tumor suppressor. J Cell Sci 121: 1141-1150.
    • (2008) J Cell Sci , vol.121 , pp. 1141-1150
    • Lee, M.1    Vasioukhin, V.2
  • 48
    • 55249104474 scopus 로고    scopus 로고
    • Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-cadherin endocytosis
    • Leibfried A, Fricke R, Morgan MJ, Bogdan S, Bellaiche Y. 2008. Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-cadherin endocytosis. Curr Biol 18: 1639-1648.
    • (2008) Curr Biol , vol.18 , pp. 1639-1648
    • Leibfried, A.1    Fricke, R.2    Morgan, M.J.3    Bogdan, S.4    Bellaiche, Y.5
  • 49
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon MA. 2008. Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9: 99-111.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 50
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon MA, Ferguson KM. 2000. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem J 350: 1-18.
    • (2000) Biochem J , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 51
    • 51849167782 scopus 로고    scopus 로고
    • Understanding PTEN regulation: PIP2, polarity and protein stability
    • Leslie NR, Batty IH, Maccario H, Davidson L, Downes CP. 2008. Understanding PTEN regulation: PIP2, polarity and protein stability. Oncogene 27: 5464-5476.
    • (2008) Oncogene , vol.27 , pp. 5464-5476
    • Leslie, N.R.1    Batty, I.H.2    Maccario, H.3    Davidson, L.4    Downes, C.P.5
  • 53
    • 34548851138 scopus 로고    scopus 로고
    • Restoring E-cadherin-mediated cell-cell adhesion increases PTEN protein level and stability in human breast carcinoma cells
    • Li Z, Wang L, ZhangW, Fu Y, Zhao H, Hu Y, Prins BP, Zha X. 2007. Restoring E-cadherin-mediated cell-cell adhesion increases PTEN protein level and stability in human breast carcinoma cells. Biochem Biophys Res Commun 363: 165-170.
    • (2007) Biochem Biophys Res Commun , vol.363 , pp. 165-170
    • Li, Z.1    Wang, L.2    Zhang, W.3    Fu, Y.4    Zhao, H.5    Hu, Y.6    Prins, B.P.7    Zha, X.8
  • 55
    • 1242285135 scopus 로고    scopus 로고
    • Polarity and proliferation are controlled by distinct signaling pathways downstream of PI3-kinase in breast epithelial tumorcells
    • Liu H, Radisky DC, Wang F, Bissell MJ. 2004. Polarity and proliferation are controlled by distinct signaling pathways downstream of PI3-kinase in breast epithelial tumorcells. J Cell Biol 164: 603-612.
    • (2004) J Cell Biol , vol.164 , pp. 603-612
    • Liu, H.1    Radisky, D.C.2    Wang, F.3    Bissell, M.J.4
  • 57
    • 56749164104 scopus 로고    scopus 로고
    • Biomechanical regulation of cell orientation and fate
    • Lopez JI, Mouw JK, Weaver VM. 2008. Biomechanical regulation of cell orientation and fate. Oncogene 27: 6981-6993.
    • (2008) Oncogene , vol.27 , pp. 6981-6993
    • Lopez, J.I.1    Mouw, J.K.2    Weaver, V.M.3
  • 59
    • 77951234490 scopus 로고    scopus 로고
    • Pulsation and stabilization: Contractile forces that underlie morphogenesis
    • Martin AC. 2010. Pulsation and stabilization: contractile forces that underlie morphogenesis. Dev Biol 341: 114-125.
    • (2010) Dev Biol , vol.341 , pp. 114-125
    • Martin, A.C.1
  • 60
    • 58749084302 scopus 로고    scopus 로고
    • Pulsed contractions of an actin-myosin network drive apical constriction
    • Martin AC, Kaschube M, Wieschaus EF. 2009. Pulsed contractions of an actin-myosin network drive apical constriction. Nature 457: 495-499.
    • (2009) Nature , vol.457 , pp. 495-499
    • Martin, A.C.1    Kaschube, M.2    Wieschaus, E.F.3
  • 62
    • 34548284082 scopus 로고    scopus 로고
    • Phosphoinositides control epithelial development
    • Martin-Belmonte F, Mostov K. 2007. Phosphoinositides control epithelial development. Cell Cycle 6: 1957-1961.
    • (2007) Cell Cycle , vol.6 , pp. 1957-1961
    • Martin-Belmonte, F.1    Mostov, K.2
  • 63
    • 63449134463 scopus 로고    scopus 로고
    • Chapter 3: Acquisition of membrane polarity in epithelial tube formation patterns, signaling pathways, molecular mechanisms, and disease
    • Martin-Belmonte F, Rodriguez-Fraticelli AE. 2009. Chapter 3: Acquisition of membrane polarity in epithelial tube formation patterns, signaling pathways, molecular mechanisms, and disease. Int Rev Cell Mol Biol 274: 129-182.
    • (2009) Int Rev Cell Mol Biol , vol.274 , pp. 129-182
    • Martin-Belmonte, F.1    Rodriguez-Fraticelli, A.E.2
  • 64
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42
    • Martin-Belmonte F, Gassama A, Datta A, Yu W, Rescher U, Gerke V, Mostov K. 2007. PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128: 383-397.
    • (2007) Cell , vol.128 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5    Gerke, V.6    Mostov, K.7
  • 65
    • 59849125052 scopus 로고    scopus 로고
    • Mutations in phosphoinositide metabolizing enzymes and human disease
    • McCrea HJ, De Camilli P. 2009. Mutations in phosphoinositide metabolizing enzymes and human disease. Physiology (Bethesda) 24: 8-16.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 8-16
    • McCrea, H.J.1    de Camilli, P.2
  • 66
    • 25444486668 scopus 로고    scopus 로고
    • The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex
    • Mertens AE, Rygiel TP, Olivo C, van der Kammen R, Collard JG. 2005. The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex. J Cell Biol 170: 1029-1037.
    • (2005) J Cell Biol , vol.170 , pp. 1029-1037
    • Mertens, A.E.1    Rygiel, T.P.2    Olivo, C.3    van der Kammen, R.4    Collard, J.G.5
  • 67
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki H, Sasaki T, Takai Y, Takenawa T. 1998. Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391: 93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 68
    • 33746038584 scopus 로고    scopus 로고
    • Actomyosin tension is required for correct recruitment of adherens junction components and zonula occludens formation
    • Miyake Y, Inoue N, Nishimura K, Kinoshita N, Hosoya H, Yonemura S. 2006. Actomyosin tension is required for correct recruitment of adherens junction components and zonula occludens formation. Exp Cell Res 312: 1637-1650.
    • (2006) Exp Cell Res , vol.312 , pp. 1637-1650
    • Miyake, Y.1    Inoue, N.2    Nishimura, K.3    Kinoshita, N.4    Hosoya, H.5    Yonemura, S.6
  • 69
    • 77951911203 scopus 로고    scopus 로고
    • aPKC phosphorylation of Bazooka defines the apical/lateral border in Drosophila epithelial cells
    • Morais-de-Sa E, Mirouse V, St Johnston D. 2010. aPKC phosphorylation of Bazooka defines the apical/lateral border in Drosophila epithelial cells. Cell 141: 509-523.
    • (2010) Cell , vol.141 , pp. 509-523
    • Morais-de-Sa, E.1    Mirouse, V.2    St Johnston, D.3
  • 70
    • 30844456421 scopus 로고    scopus 로고
    • PAR proteins and the cytoskeleton: A marriage of equals
    • Munro EM. 2006. PAR proteins and the cytoskeleton: A marriage of equals. Curr Opin Cell Biol 18: 86-94.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 86-94
    • Munro, E.M.1
  • 71
    • 0035341316 scopus 로고    scopus 로고
    • cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network
    • Musch A, Cohen D, Kreitzer G, Rodriguez-Boulan E. 2001. cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J 20: 2171-2179.
    • (2001) EMBO J , vol.20 , pp. 2171-2179
    • Musch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 73
    • 77951238830 scopus 로고    scopus 로고
    • Remodeling epithelial cell organization: Transitions between front-rear and apical-basal polarity
    • Nelson WJ. 2009. Remodeling epithelial cell organization: Transitions between front-rear and apical-basal polarity. Cold Spring Harb Perspect Biol 1: a000513.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Nelson, W.J.1
  • 75
    • 0036636095 scopus 로고    scopus 로고
    • Opinion: Building epithelial architecture: Insights from threedimensional culture models
    • O'Brien LE, Zegers MM, Mostov KE. 2002. Opinion: Building epithelial architecture: Insights from threedimensional culture models. Nat Rev Mol Cell Biol 3: 531-537.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 531-537
    • O'Brien, L.E.1    Zegers, M.M.2    Mostov, K.E.3
  • 76
    • 32144464080 scopus 로고    scopus 로고
    • Morphological and biochemical analysis of Rac1 in three-dimensional epithelial cell cultures
    • O'Brien LE, YuW, Tang K, Jou TS, Zegers MM, Mostov KE. 2006. Morphological and biochemical analysis of Rac1 in three-dimensional epithelial cell cultures. Methods Enzymol 406: 676-691.
    • (2006) Methods Enzymol , vol.406 , pp. 676-691
    • O'Brien, L.E.1    Yu, W.2    Tang, K.3    Jou, T.S.4    Zegers, M.M.5    Mostov, K.E.6
  • 77
    • 77953637330 scopus 로고    scopus 로고
    • Physical mechanisms of signal integration by WASP family proteins
    • Padrick SB, Rosen MK. 2010. Physical mechanisms of signal integration by WASP family proteins. Annu Rev Biochem 79: 707-735.
    • (2010) Annu Rev Biochem , vol.79 , pp. 707-735
    • Padrick, S.B.1    Rosen, M.K.2
  • 79
    • 65449131260 scopus 로고    scopus 로고
    • Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini
    • Palmer SM, Playford MP, Craig SW, Schaller MD, Campbell SL. 2009. Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini. J Biol Chem 284: 7223-7231.
    • (2009) J Biol Chem , vol.284 , pp. 7223-7231
    • Palmer, S.M.1    Playford, M.P.2    Craig, S.W.3    Schaller, M.D.4    Campbell, S.L.5
  • 80
    • 0034472867 scopus 로고    scopus 로고
    • New aspects of integrin signaling in cancer
    • Parise LV, Lee J, Juliano RL. 2000. New aspects of integrin signaling in cancer. Semin Cancer Biol 10: 407-414.
    • (2000) Semin Cancer Biol , vol.10 , pp. 407-414
    • Parise, L.V.1    Lee, J.2    Juliano, R.L.3
  • 81
  • 82
    • 33746706949 scopus 로고    scopus 로고
    • Spatial control of actin organization at adherens junctions by a synaptotagmin-like protein Btsz
    • Pilot F, Philippe JM, Lemmers C, Lecuit T. 2006. Spatial control of actin organization at adherens junctions by a synaptotagmin-like protein Btsz. Nature 442: 580-584.
    • (2006) Nature , vol.442 , pp. 580-584
    • Pilot, F.1    Philippe, J.M.2    Lemmers, C.3    Lecuit, T.4
  • 83
    • 30944433152 scopus 로고    scopus 로고
    • Regulated and polarized PtdIns(3,4,5)P3 accumulation is essential for apical membrane morphogenesis in photoreceptor epithelial cells
    • Pinal N, Goberdhan DC, Collinson L, Fujita Y, Cox IM, Wilson C, Pichaud F. 2006. Regulated and polarized PtdIns(3,4,5)P3 accumulation is essential for apical membrane morphogenesis in photoreceptor epithelial cells. Curr Biol 16: 140-149.
    • (2006) Curr Biol , vol.16 , pp. 140-149
    • Pinal, N.1    Goberdhan, D.C.2    Collinson, L.3    Fujita, Y.4    Cox, I.M.5    Wilson, C.6    Pichaud, F.7
  • 84
    • 70349245220 scopus 로고    scopus 로고
    • Mechanical signals trigger Myosin II redistribution and mesoderm invagination in Drosophila embryos
    • Pouille PA, Ahmadi P, Brunet AC, Farge E. 2009. Mechanical signals trigger Myosin II redistribution and mesoderm invagination in Drosophila embryos. Sci Signal 2: ra16.
    • (2009) Sci Signal , vol.2
    • Pouille, P.A.1    Ahmadi, P.2    Brunet, A.C.3    Farge, E.4
  • 85
    • 67649464358 scopus 로고    scopus 로고
    • PTEN is a mechanosensing signal transducer for myosin II localization in Dictyostelium cells
    • Pramanik MK, Iijima M, Iwadate Y, Yumura S. 2009. PTEN is a mechanosensing signal transducer for myosin II localization in Dictyostelium cells. Genes Cells 14: 821-834.
    • (2009) Genes Cells , vol.14 , pp. 821-834
    • Pramanik, M.K.1    Iijima, M.2    Iwadate, Y.3    Yumura, S.4
  • 86
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda KE, Scott JA, Mullins RD, Lim WA. 2000. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290: 801-806.
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 87
    • 77952396762 scopus 로고    scopus 로고
    • Tuba, a Cdc42 GEF, is required for polarized spindle orientation during epithelial cyst formation
    • Qin Y, Meisen WH, Hao Y, Macara IG. 2010. Tuba, a Cdc42 GEF, is required for polarized spindle orientation during epithelial cyst formation. J Cell Biol 189: 661-669.
    • (2010) J Cell Biol , vol.189 , pp. 661-669
    • Qin, Y.1    Meisen, W.H.2    Hao, Y.3    Macara, I.G.4
  • 88
    • 42649123661 scopus 로고    scopus 로고
    • Epithelial morphogenesis in embryos: Asymmetries, motors and brakes
    • Quintin S, Gally C, Labouesse M. 2008. Epithelial morphogenesis in embryos: asymmetries, motors and brakes. Trends Genet 24: 221-230.
    • (2008) Trends Genet , vol.24 , pp. 221-230
    • Quintin, S.1    Gally, C.2    Labouesse, M.3
  • 89
    • 33845498084 scopus 로고    scopus 로고
    • Vesicle transport, cilium formation, and membrane specialization: The origins of a sensory organelle
    • Reiter JF, Mostov K. 2006. Vesicle transport, cilium formation, and membrane specialization: The origins of a sensory organelle. Proc Natl Acad Sci 103: 18383-18384.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 18383-18384
    • Reiter, J.F.1    Mostov, K.2
  • 90
    • 3242887228 scopus 로고    scopus 로고
    • Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes
    • Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V. 2004. Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J Cell Sci 117: 3473-3480.
    • (2004) J Cell Sci , vol.117 , pp. 3473-3480
    • Rescher, U.1    Ruhe, D.2    Ludwig, C.3    Zobiack, N.4    Gerke, V.5
  • 92
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi R, Ho HY, Kirschner MW. 2000. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J Cell Biol 150: 1299-1310.
    • (2000) J Cell Biol , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 93
    • 0035159369 scopus 로고    scopus 로고
    • Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cells
    • Rojas R, Ruiz WG, Leung SM, Jou TS, Apodaca G. 2001. Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cells. Mol Biol Cell 12: 2257-2274.
    • (2001) Mol Biol Cell , vol.12 , pp. 2257-2274
    • Rojas, R.1    Ruiz, W.G.2    Leung, S.M.3    Jou, T.S.4    Apodaca, G.5
  • 94
    • 4344591544 scopus 로고    scopus 로고
    • Making tubes: Step by step
    • Rosario M, BirchmeierW. 2004. Making tubes: Step by step. Dev Cell 7: 3-5.
    • (2004) Dev Cell , vol.7 , pp. 3-5
    • Rosario, M.1    Birchmeier, W.2
  • 95
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas J, Zhao H, Lappalainen P. 2010. Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol Rev 90: 259-289.
    • (2010) Physiol Rev , vol.90 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.2    Lappalainen, P.3
  • 98
    • 50849083158 scopus 로고    scopus 로고
    • Cell adhesion receptors in mechanotransduction
    • Schwartz MA, DeSimoneDW. 2008. Cell adhesion receptors in mechanotransduction. Curr Opin Cell Biol 20: 551-556.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 551-556
    • Schwartz, M.A.1    DeSimone, D.W.2
  • 99
    • 55249124828 scopus 로고    scopus 로고
    • Intercellular junctions: Actin the PARt
    • Shen L, Turner JR. 2008. Intercellular junctions: Actin the PARt. Curr Biol 18: R1014-1017.
    • (2008) Curr Biol , vol.18 , pp. 1014-1017
    • Shen, L.1    Turner, J.R.2
  • 100
    • 78649290482 scopus 로고    scopus 로고
    • Sequential activation of apical and basolateral contractility drives ascidian endoderm invagination
    • Sherrard K, Robin F, Lemaire P, Munro E. 2010. Sequential activation of apical and basolateral contractility drives ascidian endoderm invagination. Curr Biol 20: 1499-1510.
    • (2010) Curr Biol , vol.20 , pp. 1499-1510
    • Sherrard, K.1    Robin, F.2    Lemaire, P.3    Munro, E.4
  • 101
    • 26244455734 scopus 로고    scopus 로고
    • Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts
    • Shewan AM, Maddugoda M, Kraemer A, Stehbens SJ, Verma S, Kovacs EM, Yap AS. 2005. Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts. Mol Biol Cell 16: 4531-4542.
    • (2005) Mol Biol Cell , vol.16 , pp. 4531-4542
    • Shewan, A.M.1    Maddugoda, M.2    Kraemer, A.3    Stehbens, S.J.4    Verma, S.5    Kovacs, E.M.6    Yap, A.S.7
  • 102
    • 0037428076 scopus 로고    scopus 로고
    • Hippocampal neuronal polarity specified by spatially localized mPar3/mPar6 and PI 3-kinase activity
    • Shi SH, Jan LY, Jan YN. 2003. Hippocampal neuronal polarity specified by spatially localized mPar3/mPar6 and PI 3-kinase activity. Cell 112: 63-75.
    • (2003) Cell , vol.112 , pp. 63-75
    • Shi, S.H.1    Jan, L.Y.2    Jan, Y.N.3
  • 104
    • 0031770943 scopus 로고    scopus 로고
    • RhoA-binding kinase α translocation is facilitated by the collapse of the vimentin intermediate filament network
    • Sin WC, Chen XQ, Leung T, Lim L. 1998. RhoA-binding kinase α translocation is facilitated by the collapse of the vimentin intermediate filament network. Mol Cell Biol 18: 6325-6339.
    • (1998) Mol Cell Biol , vol.18 , pp. 6325-6339
    • Sin, W.C.1    Chen, X.Q.2    Leung, T.3    Lim, L.4
  • 106
    • 67549147020 scopus 로고    scopus 로고
    • Pulsed forces timed by a ratchet-like mechanism drive directed tissue movement during dorsal closure
    • Solon J, Kaya-Copur A, Colombelli J, Brunner D. 2009. Pulsed forces timed by a ratchet-like mechanism drive directed tissue movement during dorsal closure. Cell 137: 1331-1342.
    • (2009) Cell , vol.137 , pp. 1331-1342
    • Solon, J.1    Kaya-Copur, A.2    Colombelli, J.3    Brunner, D.4
  • 107
    • 77953283628 scopus 로고    scopus 로고
    • Cell polarity in eggs and epithelia: Parallels and diversity
    • St Johnston D, Ahringer J. 2010. Cell polarity in eggs and epithelia: Parallels and diversity. Cell 141: 757-774.
    • (2010) Cell , vol.141 , pp. 757-774
    • St Johnston, D.1    Ahringer, J.2
  • 108
    • 14044261474 scopus 로고    scopus 로고
    • Vinculin controls PTEN protein level by maintaining the interaction of the adherens junction protein β-catenin with the scaffolding protein MAGI-2
    • Subauste MC, Nalbant P, Adamson ED, Hahn KM. 2005. Vinculin controls PTEN protein level by maintaining the interaction of the adherens junction protein β-catenin with the scaffolding protein MAGI-2. J Biol Chem 280: 5676-5681.
    • (2005) J Biol Chem , vol.280 , pp. 5676-5681
    • Subauste, M.C.1    Nalbant, P.2    Adamson, E.D.3    Hahn, K.M.4
  • 109
    • 33646763140 scopus 로고    scopus 로고
    • Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac
    • Suetsugu S, Kurisu S, Oikawa T, Yamazaki D, Oda A, Takenawa T. 2006. Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac. J Cell Biol 173: 571-585.
    • (2006) J Cell Biol , vol.173 , pp. 571-585
    • Suetsugu, S.1    Kurisu, S.2    Oikawa, T.3    Yamazaki, D.4    Oda, A.5    Takenawa, T.6
  • 110
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: Lessons in polarity
    • Suzuki A, Ohno S. 2006. The PAR-aPKC system: Lessons in polarity. J Cell Sci 119: 979-987.
    • (2006) J Cell Sci , vol.119 , pp. 979-987
    • Suzuki, A.1    Ohno, S.2
  • 112
    • 39549108299 scopus 로고    scopus 로고
    • aPKC restricts the basolateral determinant PtdIns(3,4,5)P3 to the basal region
    • Takahama S, Hirose T, Ohno S. 2008. aPKC restricts the basolateral determinant PtdIns(3,4,5)P3 to the basal region. Biochem Biophys Res Commun 368: 249-255.
    • (2008) Biochem Biophys Res Commun , vol.368 , pp. 249-255
    • Takahama, S.1    Hirose, T.2    Ohno, S.3
  • 113
    • 33846260506 scopus 로고    scopus 로고
    • Targeting and localized signalling by small GTPases
    • ten Klooster JP, Hordijk PL. 2007. Targeting and localized signalling by small GTPases. Biol Cell 99: 1-12.
    • (2007) Biol Cell , vol.99 , pp. 1-12
    • ten Klooster, J.P.1    Hordijk, P.L.2
  • 115
    • 77950365395 scopus 로고    scopus 로고
    • ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability
    • Vemula S, Shi J, Hanneman P, Wei L, Kapur R. 2010. ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability. Blood 115: 1785-1796.
    • (2010) Blood , vol.115 , pp. 1785-1796
    • Vemula, S.1    Shi, J.2    Hanneman, P.3    Wei, L.4    Kapur, R.5
  • 117
    • 17744386543 scopus 로고    scopus 로고
    • Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling
    • von SteinW, Ramrath A, Grimm A, Muller-Borg M, Wodarz A. 2005. Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling. Development 132: 1675-1686.
    • (2005) Development , vol.132 , pp. 1675-1686
    • von Stein, W.1    Ramrath, A.2    Grimm, A.3    Muller-Borg, M.4    Wodarz, A.5
  • 118
    • 36649014876 scopus 로고    scopus 로고
    • Apical junctional complexes and cell polarity
    • Wang Q, Margolis B. 2007. Apical junctional complexes and cell polarity. Kidney Int 72: 1448-1458.
    • (2007) Kidney Int , vol.72 , pp. 1448-1458
    • Wang, Q.1    Margolis, B.2
  • 119
    • 0042347443 scopus 로고    scopus 로고
    • Kinetic mechanism of non-muscle myosin IIB: Functional adaptations for tension generation and maintenance
    • Wang F, Kovacs M, Hu A, Limouze J, Harvey EV, Sellers JR. 2003. Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance. J Biol Chem 278: 27439-27448.
    • (2003) J Biol Chem , vol.278 , pp. 27439-27448
    • Wang, F.1    Kovacs, M.2    Hu, A.3    Limouze, J.4    Harvey, E.V.5    Sellers, J.R.6
  • 120
    • 77957086665 scopus 로고    scopus 로고
    • Nonmuscle myosin II isoform and domain specificity during early mouse development
    • Wang A, MaX, Conti MA, Liu C, Kawamoto S, Adelstein RS. 2010. Nonmuscle myosin II isoform and domain specificity during early mouse development. Proc Natl Acad Sci 107: 14645-14650.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 14645-14650
    • Wang, A.1    Ma, X.2    Conti, M.A.3    Liu, C.4    Kawamoto, S.5    Adelstein, R.S.6
  • 121
    • 49849098669 scopus 로고    scopus 로고
    • The ghost in the machine: Small GTPases as spatial regulators of exocytosis
    • Wu H, Rossi G, Brennwald P. 2008. The ghost in the machine: Small GTPases as spatial regulators of exocytosis. Trends Cell Biol 18: 397-404.
    • (2008) Trends Cell Biol , vol.18 , pp. 397-404
    • Wu, H.1    Rossi, G.2    Brennwald, P.3
  • 122
    • 36749070993 scopus 로고    scopus 로고
    • PDZ domains of Par-3 as potential phosphoinositide signaling integrators
    • Wu H, FengW, Chen J, Chan LN, Huang S, Zhang M. 2007. PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Mol Cell 28: 886-898.
    • (2007) Mol Cell , vol.28 , pp. 886-898
    • Wu, H.1    Feng, W.2    Chen, J.3    Chan, L.N.4    Huang, S.5    Zhang, M.6
  • 123
    • 34547571737 scopus 로고    scopus 로고
    • Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion
    • Yamada S, Nelson WJ. 2007. Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. J Cell Biol 178: 517-527.
    • (2007) J Cell Biol , vol.178 , pp. 517-527
    • Yamada, S.1    Nelson, W.J.2
  • 124
    • 33846847697 scopus 로고    scopus 로고
    • Rac-WAVE-mediated actin reorganization is required for organization and maintenance of cell-cell adhesion
    • Yamazaki D, Oikawa T, Takenawa T. 2007. Rac-WAVE-mediated actin reorganization is required for organization and maintenance of cell-cell adhesion. JCell Sci 120: 86-100.
    • (2007) JCell Sci , vol.120 , pp. 86-100
    • Yamazaki, D.1    Oikawa, T.2    Takenawa, T.3
  • 125
    • 23744480002 scopus 로고    scopus 로고
    • The Rho kinases I and II regulate different aspects of myosin II activity
    • Yoneda A, Multhaupt HA, Couchman JR. 2005. The Rho kinases I and II regulate different aspects of myosin II activity. J Cell Biol 170: 443-453.
    • (2005) J Cell Biol , vol.170 , pp. 443-453
    • Yoneda, A.1    Multhaupt, H.A.2    Couchman, J.R.3
  • 126
    • 33846099490 scopus 로고    scopus 로고
    • Fibronectin matrix assembly requires distinct contributions from Rho kinases I and-II
    • Yoneda A, Ushakov D, Multhaupt HA, Couchman JR. 2007. Fibronectin matrix assembly requires distinct contributions from Rho kinases I and-II. Mol Biol Cell 18: 66-75.
    • (2007) Mol Biol Cell , vol.18 , pp. 66-75
    • Yoneda, A.1    Ushakov, D.2    Multhaupt, H.A.3    Couchman, J.R.4
  • 127
    • 77953123743 scopus 로고    scopus 로고
    • α-Catenin as a tension transducer that induces adherens junction development
    • Yonemura S, Wada Y, Watanabe T, Nagafuchi A, Shibata M. 2010. α-Catenin as a tension transducer that induces adherens junction development. Nat Cell Biol 12: 533-542.
    • (2010) Nat Cell Biol , vol.12 , pp. 533-542
    • Yonemura, S.1    Wada, Y.2    Watanabe, T.3    Nagafuchi, A.4    Shibata, M.5
  • 129
    • 33644747349 scopus 로고    scopus 로고
    • The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis
    • Zhang H, Macara IG. 2006. The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis. Nat Cell Biol 8: 227-237.
    • (2006) Nat Cell Biol , vol.8 , pp. 227-237
    • Zhang, H.1    Macara, I.G.2
  • 130
    • 38849119148 scopus 로고    scopus 로고
    • The PAR-6 polarity protein regulates dendritic spine morphogenesis through p190 RhoGAP and the Rho GTPase
    • Zhang H, Macara IG. 2008. The PAR-6 polarity protein regulates dendritic spine morphogenesis through p190 RhoGAP and the Rho GTPase. Dev Cell 14: 216-226.
    • (2008) Dev Cell , vol.14 , pp. 216-226
    • Zhang, H.1    Macara, I.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.