메뉴 건너뛰기




Volumn 291, Issue 2, 2016, Pages 691-704

Ankyrin-G inhibits endocytosis of cadherin dimers

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; BINS; BIOLOGICAL MEMBRANES; CELL ADHESION; CELL MEMBRANES; ENDOTHELIAL CELLS; MOLECULAR BIOLOGY; PROTEINS;

EID: 84954160944     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.648386     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 0037699955 scopus 로고    scopus 로고
    • Angiogenesis in health and disease
    • Carmeliet, P. (2003) Angiogenesis in health and disease. Nat. Med. 9, 653-660
    • (2003) Nat. Med. , vol.9 , pp. 653-660
    • Carmeliet, P.1
  • 2
    • 48049094159 scopus 로고    scopus 로고
    • The role of adherens junctions and VE-cadherin in the control of vascular permeability
    • Dejana, E., Orsenigo, F., and Lampugnani, M. G. (2008) The role of adherens junctions and VE-cadherin in the control of vascular permeability. J. Cell Sci. 121, 2115-2122
    • (2008) J. Cell Sci. , vol.121 , pp. 2115-2122
    • Dejana, E.1    Orsenigo, F.2    Lampugnani, M.G.3
  • 5
    • 77957233298 scopus 로고    scopus 로고
    • VE-cadherin: At the front, center, and sides of endothelial cell organization and function
    • Harris, E. S., and Nelson, W. J. (2010) VE-cadherin: at the front, center, and sides of endothelial cell organization and function. Curr Opin Cell Biol. 22, 651-658
    • (2010) Curr Opin Cell Biol. , vol.22 , pp. 651-658
    • Harris, E.S.1    Nelson, W.J.2
  • 7
    • 65249178992 scopus 로고    scopus 로고
    • P120-catenin inhibits VE-cadherin internalization through a Rho-independent mechanism
    • Chiasson, C. M., Wittich, K. B., Vincent, P. A., Faundez, V., and Kowalczyk, A. P. (2009) p120-catenin inhibits VE-cadherin internalization through a Rho-independent mechanism. Mol. Biol. Cell 20, 1970-1980
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1970-1980
    • Chiasson, C.M.1    Wittich, K.B.2    Vincent, P.A.3    Faundez, V.4    Kowalczyk, A.P.5
  • 8
    • 0242708621 scopus 로고    scopus 로고
    • A core function for p120-catenin in cadherin turnover
    • Davis, M. A., Ireton, R. C., and Reynolds, A. B. (2003) A core function for p120-catenin in cadherin turnover. J. Cell Biol. 163, 525-534
    • (2003) J. Cell Biol. , vol.163 , pp. 525-534
    • Davis, M.A.1    Ireton, R.C.2    Reynolds, A.B.3
  • 9
    • 0242456021 scopus 로고    scopus 로고
    • Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells
    • Xiao, K., Allison, D. F., Buckley, K. M., Kottke, M. D., Vincent, P. A., Faundez, V., and Kowalczyk, A. P. (2003) Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells. J. Cell Biol. 163, 535-545
    • (2003) J. Cell Biol. , vol.163 , pp. 535-545
    • Xiao, K.1    Allison, D.F.2    Buckley, K.M.3    Kottke, M.D.4    Vincent, P.A.5    Faundez, V.6    Kowalczyk, A.P.7
  • 12
    • 80052614857 scopus 로고    scopus 로고
    • Mechanosensitive EPLIN-dependent remodeling of adherens junctions regulates epithelial reshaping
    • Taguchi, K., Ishiuchi, T., and Takeichi, M. (2011) Mechanosensitive EPLIN-dependent remodeling of adherens junctions regulates epithelial reshaping. J. Cell Biol. 194, 643-656
    • (2011) J. Cell Biol. , vol.194 , pp. 643-656
    • Taguchi, K.1    Ishiuchi, T.2    Takeichi, M.3
  • 13
    • 28344433073 scopus 로고    scopus 로고
    • Deconstructing the cadherin-catenin-actin complex
    • Yamada, S., Pokutta, S., Drees, F., Weis, W. I., and Nelson, W. J. (2005) Deconstructing the cadherin-catenin-actin complex. Cell 123, 889-901
    • (2005) Cell , vol.123 , pp. 889-901
    • Yamada, S.1    Pokutta, S.2    Drees, F.3    Weis, W.I.4    Nelson, W.J.5
  • 15
    • 42449102211 scopus 로고    scopus 로고
    • Biochemical and structural analysis of α-catenin in cell-cell contacts
    • Pokutta, S., Drees, F., Yamada, S., Nelson, W. J., and Weis, W. I. (2008) Biochemical and structural analysis of α-catenin in cell-cell contacts. Biochem. Soc. Trans. 36, 141-147
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 141-147
    • Pokutta, S.1    Drees, F.2    Yamada, S.3    Nelson, W.J.4    Weis, W.I.5
  • 16
    • 84861778995 scopus 로고    scopus 로고
    • Thinking outside the cell: How cadherins drive adhesion
    • Brasch, J., Harrison, O. J., Honig, B., and Shapiro, L. (2012) Thinking outside the cell: how cadherins drive adhesion. Trends Cell Biol. 22, 299-310
    • (2012) Trends Cell Biol. , vol.22 , pp. 299-310
    • Brasch, J.1    Harrison, O.J.2    Honig, B.3    Shapiro, L.4
  • 17
    • 58549115688 scopus 로고    scopus 로고
    • Resolving cadherin interactions and binding cooperativity at the single-molecule level
    • Zhang, Y., Sivasankar, S., Nelson, W. J., and Chu, S. (2009) Resolving cadherin interactions and binding cooperativity at the single-molecule level. Proc. Natl. Acad. Sci. U.S.A. 106, 109-114
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 109-114
    • Zhang, Y.1    Sivasankar, S.2    Nelson, W.J.3    Chu, S.4
  • 21
    • 59849129267 scopus 로고    scopus 로고
    • The actin cytoskeleton in endothelial cell phenotypes
    • Prasain, N., and Stevens, T. (2009) The actin cytoskeleton in endothelial cell phenotypes. Microvasc. Res. 77, 53-63
    • (2009) Microvasc. Res. , vol.77 , pp. 53-63
    • Prasain, N.1    Stevens, T.2
  • 22
    • 77955882462 scopus 로고    scopus 로고
    • Membrane domains based on ankyrin and spectrin associated with cell-cell interactions
    • Bennett, V., and Healy, J. (2009) Membrane domains based on ankyrin and spectrin associated with cell-cell interactions. Cold Spring Harb. Perspect. Biol. 1, a003012
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , pp. a003012
    • Bennett, V.1    Healy, J.2
  • 23
    • 34548827681 scopus 로고    scopus 로고
    • Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos
    • Kizhatil, K., Davis, J. Q., Davis, L., Hoffman, J., Hogan, B. L., and Bennett, V. (2007) Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. J. Biol. Chem. 282, 26552-26561
    • (2007) J. Biol. Chem. , vol.282 , pp. 26552-26561
    • Kizhatil, K.1    Davis, J.Q.2    Davis, L.3    Hoffman, J.4    Hogan, B.L.5    Bennett, V.6
  • 24
    • 84877911596 scopus 로고    scopus 로고
    • E-cadherin polarity is determined by a multifunction motif mediating lateral membrane retention through ankyrin-G and apical-lateral transcytosis through clathrin
    • Jenkins, P. M., Vasavda, C., Hostettler, J., Davis, J. Q., Abdi, K., and Bennett, V. (2013) E-cadherin polarity is determined by a multifunction motif mediating lateral membrane retention through ankyrin-G and apical-lateral transcytosis through clathrin. J. Biol. Chem. 288, 14018-14031
    • (2013) J. Biol. Chem. , vol.288 , pp. 14018-14031
    • Jenkins, P.M.1    Vasavda, C.2    Hostettler, J.3    Davis, J.Q.4    Abdi, K.5    Bennett, V.6
  • 26
    • 1942533405 scopus 로고    scopus 로고
    • Lateral membrane biogenesis in human bronchial epithelial cells requires 190-kDa ankyrin-G
    • Kizhatil, K., and Bennett, V. (2004) Lateral membrane biogenesis in human bronchial epithelial cells requires 190-kDa ankyrin-G. J. Biol. Chem. 279, 16706-16714
    • (2004) J. Biol. Chem. , vol.279 , pp. 16706-16714
    • Kizhatil, K.1    Bennett, V.2
  • 27
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 28
    • 21144433924 scopus 로고    scopus 로고
    • Identification of a transiently exposed VE-cadherin epitope that allows for specific targeting of an antibody to the tumor neovasculature
    • May, C., Doody, J. F., Abdullah, R., Balderes, P., Xu, X., Chen, C. P., Zhu, Z., Shapiro, L., Kussie, P., Hicklin, D. J., Liao, F., and Bohlen, P. (2005) Identification of a transiently exposed VE-cadherin epitope that allows for specific targeting of an antibody to the tumor neovasculature. Blood 105, 4337-4344
    • (2005) Blood , vol.105 , pp. 4337-4344
    • May, C.1    Doody, J.F.2    Abdullah, R.3    Balderes, P.4    Xu, X.5    Chen, C.P.6    Zhu, Z.7    Shapiro, L.8    Kussie, P.9    Hicklin, D.J.10    Liao, F.11    Bohlen, P.12
  • 31
    • 27644578567 scopus 로고    scopus 로고
    • Regulated dimerization of the thyrotropin-releasing hormone receptor affects receptor trafficking but not signaling
    • Song, G. J., and Hinkle, P. M. (2005) Regulated dimerization of the thyrotropin-releasing hormone receptor affects receptor trafficking but not signaling. Mol. Endocrinol. 19, 2859-2870
    • (2005) Mol. Endocrinol. , vol.19 , pp. 2859-2870
    • Song, G.J.1    Hinkle, P.M.2
  • 33
    • 0031149109 scopus 로고    scopus 로고
    • Lateral clustering of the adhesive ectodomain: A fundamental determinant of cadherin function
    • Yap, A. S., Brieher, W. M., Pruschy, M., and Gumbiner, B. M. (1997) Lateral clustering of the adhesive ectodomain: a fundamental determinant of cadherin function. Curr. Biol. 7, 308-315
    • (1997) Curr. Biol. , vol.7 , pp. 308-315
    • Yap, A.S.1    Brieher, W.M.2    Pruschy, M.3    Gumbiner, B.M.4
  • 34
    • 0034623227 scopus 로고    scopus 로고
    • Receptor clustering drives polarized assembly of ankyrin
    • Jefford, G., and Dubreuil, R. R. (2000) Receptor clustering drives polarized assembly of ankyrin. J. Biol. Chem. 275, 27726-27732
    • (2000) J. Biol. Chem. , vol.275 , pp. 27726-27732
    • Jefford, G.1    Dubreuil, R.R.2
  • 36
    • 84904645592 scopus 로고    scopus 로고
    • Ankyrin-G palmitoylation and βII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly
    • He, M., Abdi, K. M., and Bennett, V. (2014) Ankyrin-G palmitoylation and βII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly. J. Cell Biol. 206, 273-288
    • (2014) J. Cell Biol. , vol.206 , pp. 273-288
    • He, M.1    Abdi, K.M.2    Bennett, V.3
  • 37
    • 84921932679 scopus 로고    scopus 로고
    • Giant ankyrin-G stabilizes somatodendritic GABAergic synapses through opposing endocytosis of GABAA receptors
    • Tseng, W. C., Jenkins, P. M., Tanaka, M., Mooney, R., and Bennett, V. (2015) Giant ankyrin-G stabilizes somatodendritic GABAergic synapses through opposing endocytosis of GABAA receptors. Proc. Natl. Acad. Sci. U.S.A. 112, 1214-1219
    • (2015) Proc. Natl. Acad. Sci. U.S.A. , vol.112 , pp. 1214-1219
    • Tseng, W.C.1    Jenkins, P.M.2    Tanaka, M.3    Mooney, R.4    Bennett, V.5
  • 38
    • 84954110832 scopus 로고    scopus 로고
    • Dynamic spectrin/ankyrin-G microdomains promote lateral membrane assembly by opposing endocytosis
    • Jenkins, P., Meng, H., Bennett, V. (2015) Dynamic spectrin/ankyrin-G microdomains promote lateral membrane assembly by opposing endocytosis. Sci. Adv. 1, e1500301
    • (2015) Sci. Adv. , vol.1
    • Jenkins, P.1    Meng, H.2    Bennett, V.3
  • 39
    • 84884149475 scopus 로고    scopus 로고
    • VE-cadherin and endothelial adherens junctions: Active guardians of vascular integrity
    • Giannotta, M., Trani, M., and Dejana, E. (2013) VE-cadherin and endothelial adherens junctions: active guardians of vascular integrity. Dev. Cell 26, 441-454
    • (2013) Dev. Cell , vol.26 , pp. 441-454
    • Giannotta, M.1    Trani, M.2    Dejana, E.3
  • 40
    • 0032776062 scopus 로고    scopus 로고
    • Vascular-endothelial-cadherin modulates endothelial monolayer permeability
    • Hordijk, P. L., Anthony, E., Mul, F. P., Rientsma, R., Oomen, L. C., and Roos, D. (1999) Vascular-endothelial-cadherin modulates endothelial monolayer permeability. J. Cell Sci. 112, 1915-1923
    • (1999) J. Cell Sci. , vol.112 , pp. 1915-1923
    • Hordijk, P.L.1    Anthony, E.2    Mul, F.P.3    Rientsma, R.4    Oomen, L.C.5    Roos, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.