메뉴 건너뛰기




Volumn 17, Issue 2, 2005, Pages 123-128

Linking Rap to cell adhesion

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AFADIN; ARAP 3 PROTEIN; CADHERIN; GUANINE NUCLEOTIDE; GUANOSINE TRIPHOSPHATASE; INTEGRIN; PDZ PROTEIN; RAC PROTEIN; RAP PROTEIN; RAPL PROTEIN; RIAM PROTEIN; UNCLASSIFIED DRUG; VAV PROTEIN;

EID: 15044359236     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2005.02.009     Document Type: Review
Times cited : (410)

References (40)
  • 3
    • 0037329747 scopus 로고    scopus 로고
    • Cellular functions of the Rap1 GTP-binding protein: A pattern emerges
    • E. Caron Cellular functions of the Rap1 GTP-binding protein: a pattern emerges J Cell Sci 116 2003 435 440
    • (2003) J Cell Sci , vol.116 , pp. 435-440
    • Caron, E.1
  • 5
    • 0034710567 scopus 로고    scopus 로고
    • The GTPase Rap1 controls functional activation of macrophage integrin αmβ2 by LPS and other inflammatory mediators
    • E. Caron, A.J. Self, and A. Hall The GTPase Rap1 controls functional activation of macrophage integrin αMβ2 by LPS and other inflammatory mediators Curr Biol 10 2000 974 978
    • (2000) Curr Biol , vol.10 , pp. 974-978
    • Caron, E.1    Self, A.J.2    Hall, A.3
  • 6
    • 0034004457 scopus 로고    scopus 로고
    • Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase
    • K. Katagiri, M. Hattori, N. Minato, S. Irie, K. Takatsu, and T. Kinashi Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase Mol Cell Biol 20 2000 1956 1969
    • (2000) Mol Cell Biol , vol.20 , pp. 1956-1969
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Irie, S.4    Takatsu, K.5    Kinashi, T.6
  • 7
    • 7244242394 scopus 로고    scopus 로고
    • The cAMP-Epac-Rap1 pathway regulates cell spreading and cell adhesion to laminin-5 through the α3β1 integrin but not the α6β4 integrin
    • J.M. Enserink, L.S. Price, T. Methi, M. Mahic, A. Sonnenberg, J.L. Bos, and K. Tasken The cAMP-Epac-Rap1 pathway regulates cell spreading and cell adhesion to laminin-5 through the α3β1 integrin but not the α6β4 integrin J Biol Chem 279 2004 44889 44896
    • (2004) J Biol Chem , vol.279 , pp. 44889-44896
    • Enserink, J.M.1    Price, L.S.2    Methi, T.3    Mahic, M.4    Sonnenberg, A.5    Bos, J.L.6    Tasken, K.7
  • 8
    • 4644221351 scopus 로고    scopus 로고
    • CalDAG-GEFI integrates signaling for platelet aggregation and thrombus formation
    • J.R. Crittenden, W. Bergmeier, Y. Zhang, C.L. Piffath, Y. Liang, D.D. Wagner, D.E. Housman, and A.M. Graybiel CalDAG-GEFI integrates signaling for platelet aggregation and thrombus formation Nat Med 10 2004 982 986 This paper describes a knockout mouse of RasGRP2 (also known as CalDAGGEF1), which exhibits impaired integrin-mediated adhesion of platelets, further establishing the role of Rap1 signalling in integrin-mediated cell adhesion.
    • (2004) Nat Med , vol.10 , pp. 982-986
    • Crittenden, J.R.1    Bergmeier, W.2    Zhang, Y.3    Piffath, C.L.4    Liang, Y.5    Wagner, D.D.6    Housman, D.E.7    Graybiel, A.M.8
  • 9
    • 0037083415 scopus 로고    scopus 로고
    • Rap1 GTPase regulation of adherens junction positioning and cell adhesion
    • A.L. Knox, and N.H. Brown Rap1 GTPase regulation of adherens junction positioning and cell adhesion Science 295 2002 1285 1288
    • (2002) Science , vol.295 , pp. 1285-1288
    • Knox, A.L.1    Brown, N.H.2
  • 10
    • 0037423929 scopus 로고    scopus 로고
    • DOCK4, a GTPase activator, is disrupted during tumorigenesis
    • V. Yajnik, C. Paulding, R. Sordella, A.I. McClatchey, M. Saito, D.C. Wahrer, P. Reynolds, D.W. Bell, R. Lake, and S. van den Heuvel DOCK4, a GTPase activator, is disrupted during tumorigenesis Cell 112 2003 673 684 This paper provided the first link of Rap1 to adherence junctions in mammalian cells by showing that Rap1 and the Rap1GEF Dock4 are involved in the formation of these junctions.
    • (2003) Cell , vol.112 , pp. 673-684
    • Yajnik, V.1    Paulding, C.2    Sordella, R.3    McClatchey, A.I.4    Saito, M.5    Wahrer, D.C.6    Reynolds, P.7    Bell, D.W.8    Lake, R.9    Van Den Heuvel, S.10
  • 14
    • 0034485413 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions
    • A. Mino, T. Ohtsuka, E. Inoue, and Y. Takai Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions Genes Cells 5 2000 1009 1016
    • (2000) Genes Cells , vol.5 , pp. 1009-1016
    • Mino, A.1    Ohtsuka, T.2    Inoue, E.3    Takai, Y.4
  • 15
    • 14944377651 scopus 로고    scopus 로고
    • Regulation of vascular endothelial barrier function by Epac, a cAMP activated exchange factor for Rap GTPase
    • 10.1182/blood-2004-05-1987.
    • •] show that the Rap1GEFs Epac and Rap1 control VE-cadherin-mediated endothelial cell junction formation. These papers are important as they demonstrate that Epac and Rap1 mediate cAMP-induced inhibition of endothelial cell permeability.
    • (2004) Blood
    • Cullere, X.1    Shaw, S.K.2    Andersson, L.3    Hirahashi, J.4    Luscinskas, F.W.5    Mayadas, T.N.6
  • 17
    • 0042490495 scopus 로고    scopus 로고
    • RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1
    • ••] show that RapL is an effector of Rap1, mediating integrin clustering in T-cells. It shows that RapL binds to active Rap1 and mediates integrin clustering by forming a complex with integrins.
    • (2003) Nat Immunol , vol.4 , pp. 741-748
    • Katagiri, K.1    Maeda, A.2    Shimonaka, M.3    Kinashi, T.4
  • 20
    • 0032753450 scopus 로고    scopus 로고
    • Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells
    • T. Asakura, H. Nakanishi, T. Sakisaka, K. Takahashi, K. Mandai, M. Nishimura, T. Sasaki, and Y. Takai Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells Genes Cells 4 1999 573 581
    • (1999) Genes Cells , vol.4 , pp. 573-581
    • Asakura, T.1    Nakanishi, H.2    Sakisaka, T.3    Takahashi, K.4    Mandai, K.5    Nishimura, M.6    Sasaki, T.7    Takai, Y.8
  • 21
    • 33645525311 scopus 로고    scopus 로고
    • Absence of the tight junctional protein AF-6 disrupts epithelial cell-cell junctions and cell polarity during mouse development
    • A.B. Zhadanov, D.W. Provance Jr., C.A. Speer, J.D. Coffin, D. Goss, J.A. Blixt, C.M. Reichert, and J.A. Mercer Absence of the tight junctional protein AF-6 disrupts epithelial cell-cell junctions and cell polarity during mouse development Curr Biol 9 1999 880 888
    • (1999) Curr Biol , vol.9 , pp. 880-888
    • Zhadanov, A.B.1    Provance Jr., D.W.2    Speer, C.A.3    Coffin, J.D.4    Goss, D.5    Blixt, J.A.6    Reichert, C.M.7    Mercer, J.A.8
  • 22
    • 0141566657 scopus 로고    scopus 로고
    • The AF-6 homolog canoe acts as a Rap1 effector during dorsal closure of the Drosophila embryo
    • B. Boettner, P. Harjes, S. Ishimaru, M. Heke, H.Q. Fan, Y. Qin, L. Van Aelst, and U. Gaul The AF-6 homolog canoe acts as a Rap1 effector during dorsal closure of the Drosophila embryo Genetics 165 2003 159 169 This paper provides strong genetic evidence that AF6 is an effector of Rap in dorsal closure in Drosophila.
    • (2003) Genetics , vol.165 , pp. 159-169
    • Boettner, B.1    Harjes, P.2    Ishimaru, S.3    Heke, M.4    Fan, H.Q.5    Qin, Y.6    Van Aelst, L.7    Gaul, U.8
  • 23
    • 0038350597 scopus 로고    scopus 로고
    • AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1
    • L. Su, M. Hattori, M. Moriyama, N. Murata, M. Harazaki, K. Kaibuchi, and N. Minato AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1 J Biol Chem 278 2003 15232 15238
    • (2003) J Biol Chem , vol.278 , pp. 15232-15238
    • Su, L.1    Hattori, M.2    Moriyama, M.3    Murata, N.4    Harazaki, M.5    Kaibuchi, K.6    Minato, N.7
  • 24
    • 0034254923 scopus 로고    scopus 로고
    • The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profiling
    • B. Boettner, E.E. Govek, J. Cross, and L. Van Aelst The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profiling Proc Natl Acad Sci USA 97 2000 9064 9069
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9064-9069
    • Boettner, B.1    Govek, E.E.2    Cross, J.3    Van Aelst, L.4
  • 25
    • 5444267347 scopus 로고    scopus 로고
    • Crucial functions of the Rap1 effector molecule RAPL in lymphocyte and dendritic cell trafficking
    • ••] show that RapL is an effector of Rap1, mediating integrin clustering in T-cells. It describes knockout mice of RapL that show a defect in T- and B-cell migration and a defect in the homing of T- and B-cells, as well as dendritic cells, to peripheral organs.
    • (2004) Nat Immunol , vol.5 , pp. 1045-1051
    • Katagiri, K.1    Ohnishi, N.2    Kabashima, K.3    Iyoda, T.4    Takeda, N.5    Shinkai, Y.6    Inaba, K.7    Kinashi, T.8
  • 27
  • 28
    • 4143053729 scopus 로고    scopus 로고
    • ARAP3 is a PI3K- and rap-regulated GAP for RhoA
    • S. Krugmann, R. Williams, L. Stephens, and P.T. Hawkins ARAP3 is a PI3K- and rap-regulated GAP for RhoA Curr Biol 14 2004 1380 1384 This paper demonstrates that Rap1 binds to Arap3 and regulates the RhoGAP activity of this protein.
    • (2004) Curr Biol , vol.14 , pp. 1380-1384
    • Krugmann, S.1    Williams, R.2    Stephens, L.3    Hawkins, P.T.4
  • 29
    • 5444230311 scopus 로고    scopus 로고
    • Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors
    • W.T. Arthur, L.A. Quilliam, and J.A. Cooper Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors J Cell Biol 167 2004 111 122 This paper shows that Rap1 binds to the RacGEFs Vav2 and Tiam1, and that Rap1 is required for the correct location of these GEFs to induce Rac-mediated cell spreading. This result provides a direct link from Rap1 to the regulation of the actin cytoskeleton in mammalian cells as was shown previously for yeast [31].
    • (2004) J Cell Biol , vol.167 , pp. 111-122
    • Arthur, W.T.1    Quilliam, L.A.2    Cooper, J.A.3
  • 31
    • 0035906952 scopus 로고    scopus 로고
    • A GDP/GTP exchange factor involved in linking a spatial landmark to cell polarity
    • P.J. Kang, A. Sanson, B. Lee, and H.O. Park A GDP/GTP exchange factor involved in linking a spatial landmark to cell polarity Science 292 2001 1376 1378
    • (2001) Science , vol.292 , pp. 1376-1378
    • Kang, P.J.1    Sanson, A.2    Lee, B.3    Park, H.O.4
  • 32
    • 0037178792 scopus 로고    scopus 로고
    • Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast
    • H.O. Park, P.J. Kang, and A.W. Rachfal Localization of the Rsr1/Bud1 GTPase involved in selection of a proper growth site in yeast J Biol Chem 277 2002 26721 26724
    • (2002) J Biol Chem , vol.277 , pp. 26721-26724
    • Park, H.O.1    Kang, P.J.2    Rachfal, A.W.3
  • 34
    • 0035958929 scopus 로고    scopus 로고
    • RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by translocation induced by association with Rap1*GTP and enhances Rap1-dependent B-Raf activation
    • Y. Liao, T. Satoh, X. Gao, T.G. Jin, C.D. Hu, and T. Kataoka RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by translocation induced by association with Rap1*GTP and enhances Rap1-dependent B-Raf activation J Biol Chem 276 2001 28478 28483
    • (2001) J Biol Chem , vol.276 , pp. 28478-28483
    • Liao, Y.1    Satoh, T.2    Gao, X.3    Jin, T.G.4    Hu, C.D.5    Kataoka, T.6
  • 35
    • 0142211303 scopus 로고    scopus 로고
    • Activation of the Rap GTPases in B lymphocytes modulates B cell antigen receptor-induced activation of Akt but has no effect on MAPK activation
    • S.L. Christian, R.L. Lee, S.J. McLeod, A.E. Burgess, A.H. Li, M. Dang-Lawson, K.B. Lin, and M.R. Gold Activation of the Rap GTPases in B lymphocytes modulates B cell antigen receptor-induced activation of Akt but has no effect on MAPK activation J Biol Chem 278 2003 41756 41767
    • (2003) J Biol Chem , vol.278 , pp. 41756-41767
    • Christian, S.L.1    Lee, R.L.2    McLeod, S.J.3    Burgess, A.E.4    Li, A.H.5    Dang-Lawson, M.6    Lin, K.B.7    Gold, M.R.8
  • 36
    • 2942678693 scopus 로고    scopus 로고
    • Bmx is a downstream Rap1 effector in VEGF-induced endothelial cell activation
    • K.V. Stoletov, and B.I. Terman Bmx is a downstream Rap1 effector in VEGF-induced endothelial cell activation Biochem Biophys Res Commun 320 2004 70 75
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 70-75
    • Stoletov, K.V.1    Terman, B.I.2
  • 37
    • 0037084658 scopus 로고    scopus 로고
    • KRIT1 association with the integrin-binding protein ICAP-1: A new direction in the elucidation of cerebral cavernous malformations (CCM1) pathogenesis
    • J.S. Zawistowski, I.G. Serebriiskii, M.F. Lee, E.A. Golemis, and D.A. Marchuk KRIT1 association with the integrin-binding protein ICAP-1: a new direction in the elucidation of cerebral cavernous malformations (CCM1) pathogenesis Hum Mol Genet 11 2002 389 396
    • (2002) Hum Mol Genet , vol.11 , pp. 389-396
    • Zawistowski, J.S.1    Serebriiskii, I.G.2    Lee, M.F.3    Golemis, E.A.4    Marchuk, D.A.5
  • 40
    • 4344594485 scopus 로고    scopus 로고
    • The sequential activity of the GTPases Rap1B and Cdc42 determines neuronal polarity
    • J.C. Schwamborn, and A.W. Puschel The sequential activity of the GTPases Rap1B and Cdc42 determines neuronal polarity Nat Neurosci 7 2004 923 929 This study shows that the recruitment of Rap1 to a developing neurite determines the fate of this neurite to become an axon. This demonstrates for the first time that Rap1 is a crucial determinant of cell polarity in mammalian cells.
    • (2004) Nat Neurosci , vol.7 , pp. 923-929
    • Schwamborn, J.C.1    Puschel, A.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.