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Volumn 128, Issue 5, 2015, Pages 979-991

Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of caveolae

Author keywords

Caveolae; Caveolin1; Cavin1; Cavin3; EHD2

Indexed keywords

CAVEOLIN 1; CAVIN 1; CAVIN 3; CHOLESTEROL; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; PRKCDBP PROTEIN, HUMAN; PTRF PROTEIN, HUMAN; RNA BINDING PROTEIN; SIGNAL PEPTIDE;

EID: 84924871461     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.161463     Document Type: Article
Times cited : (45)

References (43)
  • 2
    • 78649729522 scopus 로고    scopus 로고
    • Caveolae at a glance
    • Bastiani, M. and Parton, R. G. (2010). Caveolae at a glance. J. Cell Sci. 123, 3831-3836.
    • (2010) J. Cell Sci. , vol.123 , pp. 3831-3836
    • Bastiani, M.1    Parton, R.G.2
  • 5
    • 84859508881 scopus 로고    scopus 로고
    • Cholesterol depletion in adipocytes causes caveolae collapse concomitant with proteosomal degradation of cavin-2 in a switch-like fashion
    • Breen, M. R., Camps, M., Carvalho-Simoes, F., Zorzano, A. and Pilch, P. F. (2012). Cholesterol depletion in adipocytes causes caveolae collapse concomitant with proteosomal degradation of cavin-2 in a switch-like fashion. PLoS ONE 7, e34516.
    • (2012) PLoS ONE , vol.7
    • Breen, M.R.1    Camps, M.2    Carvalho-Simoes, F.3    Zorzano, A.4    Pilch, P.F.5
  • 6
    • 84866443110 scopus 로고    scopus 로고
    • Evaluating caveolin interactions: do proteins interact with the caveolin scaffolding domain through a widespread aromatic residue-rich motif?
    • Byrne, D. P., Dart, C. and Rigden, D. J. (2012). Evaluating caveolin interactions: do proteins interact with the caveolin scaffolding domain through a widespread aromatic residue-rich motif? PLoS ONE 7, e44879.
    • (2012) PLoS ONE , vol.7
    • Byrne, D.P.1    Dart, C.2    Rigden, D.J.3
  • 7
    • 84864025624 scopus 로고    scopus 로고
    • Structurebased reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions? Dev
    • Collins, B. M., Davis, M. J., Hancock, J. F. and Parton, R. G. (2012). Structurebased reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions? Dev. Cell 23, 11-20.
    • (2012) Cell , vol.23 , pp. 11-20
    • Collins, B.M.1    Davis, M.J.2    Hancock, J.F.3    Parton, R.G.4
  • 8
    • 0016754249 scopus 로고
    • The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths
    • Dulhunty, A. F. and Franzini-Armstrong, C. (1975). The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths. J. Physiol. 250, 513-539.
    • (1975) J. Physiol. , vol.250 , pp. 513-539
    • Dulhunty, A.F.1    Franzini-Armstrong, C.2
  • 10
    • 67249137553 scopus 로고    scopus 로고
    • A distinct pool of phosphatidylinositol 4,5-bisphosphate in caveolae revealed by a nanoscale labeling technique
    • Fujita, A., Cheng, J., Tauchi-Sato, K., Takenawa, T. and Fujimoto, T. (2009). A distinct pool of phosphatidylinositol 4,5-bisphosphate in caveolae revealed by a nanoscale labeling technique. Proc. Natl. Acad. Sci. USA 106, 9256-9261.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9256-9261
    • Fujita, A.1    Cheng, J.2    Tauchi-Sato, K.3    Takenawa, T.4    Fujimoto, T.5
  • 12
    • 67650072744 scopus 로고    scopus 로고
    • SDPR induces membrane curvature and functions in the formation of caveolae
    • Hansen, C. G., Bright, N. A., Howard, G. and Nichols, B. J. (2009). SDPR induces membrane curvature and functions in the formation of caveolae. Nat. Cell Biol. 11, 807-814.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 807-814
    • Hansen, C.G.1    Bright, N.A.2    Howard, G.3    Nichols, B.J.4
  • 13
    • 84878592690 scopus 로고    scopus 로고
    • Deletion of cavin genes reveals tissue-specific mechanisms for morphogenesis of endothelial caveolae
    • Hansen, C. G., Shvets, E., Howard, G., Riento, K. and Nichols, B. J. (2013). Deletion of cavin genes reveals tissue-specific mechanisms for morphogenesis of endothelial caveolae. Nat. Commun. 4, 1831.
    • (2013) Nat. Commun. , vol.4 , pp. 1831
    • Hansen, C.G.1    Shvets, E.2    Howard, G.3    Riento, K.4    Nichols, B.J.5
  • 14
    • 77949557277 scopus 로고    scopus 로고
    • Biogenesis of caveolae: stepwise assembly of large caveolin and cavin complexes
    • Hayer, A., Stoeber, M., Bissig, C. and Helenius, A. (2010). Biogenesis of caveolae: stepwise assembly of large caveolin and cavin complexes. Traffic 11, 361-382.
    • (2010) Traffic , vol.11 , pp. 361-382
    • Hayer, A.1    Stoeber, M.2    Bissig, C.3    Helenius, A.4
  • 15
    • 0024501531 scopus 로고
    • Effects of cytoplasmic acidification on clathrin lattice morphology
    • Heuser, J. (1989). Effects of cytoplasmic acidification on clathrin lattice morphology. J. Cell Biol. 108, 401-411.
    • (1989) J. Cell Biol. , vol.108 , pp. 401-411
    • Heuser, J.1
  • 16
    • 0024595608 scopus 로고
    • Hypertonic media inhibit receptormediated endocytosis by blocking clathrin-coated pit formation
    • Heuser, J. E. and Anderson, R. G. (1989). Hypertonic media inhibit receptormediated endocytosis by blocking clathrin-coated pit formation. J. Cell Biol. 108, 389-400.
    • (1989) J. Cell Biol. , vol.108 , pp. 389-400
    • Heuser, J.E.1    Anderson, R.G.2
  • 18
    • 0029294497 scopus 로고
    • Biomechanics of skeletal muscle capillaries: hemodynamic resistance, endothelial distensibility, and pseudopod formation
    • Lee, J. and Schmid-Schönbein, G. W. (1995). Biomechanics of skeletal muscle capillaries: hemodynamic resistance, endothelial distensibility, and pseudopod formation. Ann. Biomed. Eng. 23, 226-246.
    • (1995) Ann. Biomed. Eng. , vol.23 , pp. 226-246
    • Lee, J.1    Schmid-Schönbein, G.W.2
  • 19
  • 20
    • 84904582330 scopus 로고    scopus 로고
    • Cavin-3 knockout mice show that cavin-3 is not essential for caveolae formation, for maintenance of body composition, or for glucose tolerance
    • Liu, L., Hansen, C. G., Honeyman, B. J., Nichols, B. J. and Pilch, P. F. (2014). Cavin-3 knockout mice show that cavin-3 is not essential for caveolae formation, for maintenance of body composition, or for glucose tolerance. PLoS ONE 9, e102935.
    • (2014) PLoS ONE , vol.9
    • Liu, L.1    Hansen, C.G.2    Honeyman, B.J.3    Nichols, B.J.4    Pilch, P.F.5
  • 24
    • 0037113074 scopus 로고    scopus 로고
    • Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton
    • Mundy, D. I., Machleidt, T., Ying, Y. S., Anderson, R. G. and Bloom, G. S. (2002). Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton. J. Cell Sci. 115, 4327-4339.
    • (2002) J. Cell Sci. , vol.115 , pp. 4327-4339
    • Mundy, D.I.1    Machleidt, T.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5
  • 26
    • 84862759223 scopus 로고    scopus 로고
    • Stressing caveolae new role in cell mechanics
    • Nassoy, P. and Lamaze, C. (2012). Stressing caveolae new role in cell mechanics. Trends Cell Biol. 22, 381-389.
    • (2012) Trends Cell Biol. , vol.22 , pp. 381-389
    • Nassoy, P.1    Lamaze, C.2
  • 27
    • 0034052505 scopus 로고    scopus 로고
    • Caveolin-1 regulates shear stress-dependent activation of extracellular signal-regulated kinase
    • Park, H., Go, Y. M., Darji, R., Choi, J. W., Lisanti, M. P., Maland, M. C. and Jo, H. (2000). Caveolin-1 regulates shear stress-dependent activation of extracellular signal-regulated kinase. Am. J. Physiol. 278, H1285-H1293.
    • (2000) Am. J. Physiol. , vol.278 , pp. H1285-H1293
    • Park, H.1    Go, Y.M.2    Darji, R.3    Choi, J.W.4    Lisanti, M.P.5    Maland, M.C.6    Jo, H.7
  • 28
    • 84872959202 scopus 로고    scopus 로고
    • Caveolae as plasma membrane sensors, protectors and organizers
    • Parton, R. G. and del Pozo, M. A. (2013). Caveolae as plasma membrane sensors, protectors and organizers. Nat. Rev. Mol. Cell Biol. 14, 98-112.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 98-112
    • Parton, R.G.1    del Pozo, M.A.2
  • 29
    • 21844454457 scopus 로고    scopus 로고
    • Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae
    • Pelkmans, L. and Zerial, M. (2005). Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae. Nature 436, 128-133.
    • (2005) Nature , vol.436 , pp. 128-133
    • Pelkmans, L.1    Zerial, M.2
  • 30
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
    • Pelkmans, L., Fava, E., Grabner, H., Hannus, M., Habermann, B., Krausz, E. and Zerial, M. (2005). Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 436, 78-86.
    • (2005) Nature , vol.436 , pp. 78-86
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3    Hannus, M.4    Habermann, B.5    Krausz, E.6    Zerial, M.7
  • 31
    • 36248988035 scopus 로고    scopus 로고
    • The PX-BAR membrane-remodeling unit of sorting nexin 9
    • Pylypenko, O., Lundmark, R., Rasmuson, E., Carlsson, S. R. and Rak, A. (2007). The PX-BAR membrane-remodeling unit of sorting nexin 9. EMBO J. 26, 4788-4800.
    • (2007) EMBO J. , vol.26 , pp. 4788-4800
    • Pylypenko, O.1    Lundmark, R.2    Rasmuson, E.3    Carlsson, S.R.4    Rak, A.5
  • 32
    • 0035213597 scopus 로고    scopus 로고
    • Caveolin-deficient mice: insights into caveolar function human disease
    • Razani, B. and Lisanti, M. P. (2001). Caveolin-deficient mice: insights into caveolar function human disease. J. Clin. Invest. 108, 1553-1561.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1553-1561
    • Razani, B.1    Lisanti, M.P.2
  • 33
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: from cell biology to animal physiology
    • Razani, B., Woodman, S. E. and Lisanti, M. P. (2002). Caveolae: from cell biology to animal physiology. Pharmacol. Rev. 54, 431-467.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 35
    • 84901981250 scopus 로고    scopus 로고
    • News from the caves: update on the structure and function of caveolae
    • Shvets, E., Ludwig, A. and Nichols, B. J. (2014). News from the caves: update on the structure and function of caveolae. Curr. Opin. Cell Biol. 29, 99-106.
    • (2014) Curr. Opin. Cell Biol. , vol.29 , pp. 99-106
    • Shvets, E.1    Ludwig, A.2    Nichols, B.J.3
  • 37
    • 84861183378 scopus 로고    scopus 로고
    • Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin
    • Stoeber, M., Stoeck, I. K., Hänni, C., Bleck, C. K., Balistreri, G. and Helenius, A. (2012). Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin. EMBO J. 31, 2350-2364.
    • (2012) EMBO J. , vol.31 , pp. 2350-2364
    • Stoeber, M.1    Stoeck, I.K.2    Hänni, C.3    Bleck, C.K.4    Balistreri, G.5    Helenius, A.6
  • 38
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005). Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 39
    • 45349103038 scopus 로고    scopus 로고
    • Mps1 kinase activity restrains anaphase during an unperturbed mitosis and targets Mad2 to kinetochores
    • Tighe, A., Staples, O. and Taylor, S. (2008). Mps1 kinase activity restrains anaphase during an unperturbed mitosis and targets Mad2 to kinetochores. J. Cell Biol. 181, 893-901.
    • (2008) J. Cell Biol. , vol.181 , pp. 893-901
    • Tighe, A.1    Staples, O.2    Taylor, S.3
  • 40
    • 84867552055 scopus 로고    scopus 로고
    • Use of the unroofing technique for atomic force microscopic imaging of the intra-cellular cytoskeleton under aqueous conditions
    • Usukura, J., Yoshimura, A., Minakata, S., Youn, D., Ahn, J. and Cho, S. J. (2012). Use of the unroofing technique for atomic force microscopic imaging of the intra-cellular cytoskeleton under aqueous conditions. J. Electron Microsc. (Tokyo) 61, 321-326.
    • (2012) J. Electron Microsc. (Tokyo) , vol.61 , pp. 321-326
    • Usukura, J.1    Yoshimura, A.2    Minakata, S.3    Youn, D.4    Ahn, J.5    Cho, S.J.6


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