메뉴 건너뛰기




Volumn 5, Issue 10, 2010, Pages

The snx-px-bar family in macropinocytosis: The regulation of macropinosome formation by snx-px-bar proteins

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANE PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; SORTING NEXIN; SORTING NEXIN 1; SORTING NEXIN 18; SORTING NEXIN 33; SORTING NEXIN 5; SORTING NEXIN 9; UNCLASSIFIED DRUG; PROTEIN;

EID: 78149448083     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0013763     Document Type: Article
Times cited : (54)

References (70)
  • 3
    • 63049113263 scopus 로고    scopus 로고
    • Defining macropinocytosis
    • Kerr MC, Teasdale RD (2009) Defining macropinocytosis. Traffic 10: 364-371.
    • (2009) Traffic , vol.10 , pp. 364-371
    • Kerr, M.C.1    Teasdale, R.D.2
  • 4
    • 0006496113 scopus 로고
    • Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles
    • Pearse BM (1976) Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles. Proc Natl Acad Sci USA 73: 1255-1259.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 1255-1259
    • Pearse, B.M.1
  • 5
  • 6
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epithelium of the mouse
    • Yamada E (1955) The fine structure of the gall bladder epithelium of the mouse. J Biophys Biochem Cytol 1: 445-458.
    • (1955) J Biophys Biochem Cytol , vol.1 , pp. 445-458
    • Yamada, E.1
  • 7
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • Parton RG, Richards AA (2003) Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic 4: 724-738.
    • (2003) Traffic , vol.4 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 8
    • 13444310587 scopus 로고    scopus 로고
    • Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
    • Kirkham M, Fujita A, Chadda R, Nixon SJ, Kurzchalia TV, et al. (2005) Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles. J Cell Biol 168: 465-476.
    • (2005) J Cell Biol , vol.168 , pp. 465-476
    • Kirkham, M.1    Fujita, A.2    Chadda, R.3    Nixon, S.J.4    Kurzchalia, T.V.5
  • 9
    • 0030175501 scopus 로고    scopus 로고
    • Mechanisms of antigen uptake for presentation
    • Lanzavecchia A (1996) Mechanisms of antigen uptake for presentation. Curr Opin Immunol 8: 348-354.
    • (1996) Curr Opin Immunol , vol.8 , pp. 348-354
    • Lanzavecchia, A.1
  • 10
    • 0033783042 scopus 로고    scopus 로고
    • Constitutive macropinocytosis in oncogene-transformed fibroblasts depends on sequential permanent activation of phosphoinositide 3-kinase and phospholipase C
    • Amyere M, Payrastre B, Krause U, Van Der Smissen P, Veithen A, et al. (2000) Constitutive macropinocytosis in oncogene-transformed fibroblasts depends on sequential permanent activation of phosphoinositide 3-kinase and phospholipase C. Mol Biol Cell 11: 3453-3467.
    • (2000) Mol Biol Cell , vol.11 , pp. 3453-3467
    • Amyere, M.1    Payrastre, B.2    Krause, U.3    van der Smissen, P.4    Veithen, A.5
  • 11
    • 0036192679 scopus 로고    scopus 로고
    • Origin, originality, functions, subversions and molecular signalling of macro-pinocytosis
    • Amyere M, Mettlen M, Van Der Smissen P, Platek A, Payrastre B, et al. (2002) Origin, originality, functions, subversions and molecular signalling of macro-pinocytosis. Int J Med Microbiol 291: 487-494.
    • (2002) Int J Med Microbiol , vol.291 , pp. 487-494
    • Amyere, M.1    Mettlen, M.2    van der Smissen, P.3    Platek, A.4    Payrastre, B.5
  • 12
    • 33847632094 scopus 로고    scopus 로고
    • Role of Src-family kinases in formation and trafficking of macropinosomes
    • Kasahara K, Nakayama Y, Sato I, Ikeda K, Hoshino M, et al. (2007) Role of Src-family kinases in formation and trafficking of macropinosomes. J Cell Physiol 211: 220-232.
    • (2007) J Cell Physiol , vol.211 , pp. 220-232
    • Kasahara, K.1    Nakayama, Y.2    Sato, I.3    Ikeda, K.4    Hoshino, M.5
  • 13
    • 0018581544 scopus 로고
    • Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor
    • Haigler HT, McKanna JA, Cohen S (1979) Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor. J Cell Biol 83: 82-90.
    • (1979) J Cell Biol , vol.83 , pp. 82-90
    • Haigler, H.T.1    McKanna, J.A.2    Cohen, S.3
  • 14
    • 33750451559 scopus 로고    scopus 로고
    • Visualisation of macropinosome maturation by the recruitment of sorting nexins
    • Kerr MC, Lindsay MR, Luetterforst R, Hamilton N, Simpson F, et al. (2006) Visualisation of macropinosome maturation by the recruitment of sorting nexins. J Cell Sci 119: 3967-3980.
    • (2006) J Cell Sci , vol.119 , pp. 3967-3980
    • Kerr, M.C.1    Lindsay, M.R.2    Luetterforst, R.3    Hamilton, N.4    Simpson, F.5
  • 15
    • 0037423280 scopus 로고    scopus 로고
    • Small GTPase Rah/Rab34 is associated with membrane ruffles and macropinosomes and promotes macropinosome formation
    • Sun P, Yamamoto H, Suetsugu S, Miki H, Takenawa T, et al. (2003) Small GTPase Rah/Rab34 is associated with membrane ruffles and macropinosomes and promotes macropinosome formation. J Biol Chem 278: 4063-4071.
    • (2003) J Biol Chem , vol.278 , pp. 4063-4071
    • Sun, P.1    Yamamoto, H.2    Suetsugu, S.3    Miki, H.4    Takenawa, T.5
  • 16
    • 0027185578 scopus 로고
    • Circular ruffle formation and closure lead to macropinocytosis in hepatocyte growth factor/scatter factor-treated cells
    • Dowrick P, Kenworthy P, McCann B, Warn R (1993) Circular ruffle formation and closure lead to macropinocytosis in hepatocyte growth factor/scatter factor-treated cells. Eur J Cell Biol 61: 44-53.
    • (1993) Eur J Cell Biol , vol.61 , pp. 44-53
    • Dowrick, P.1    Kenworthy, P.2    McCann, B.3    Warn, R.4
  • 17
    • 0027218124 scopus 로고
    • Ruffles induced by Salmonella and other stimuli direct macropinocytosis of bacteria
    • Francis CL, Ryan TA, Jones BD, Smith SJ, Falkow S (1993) Ruffles induced by Salmonella and other stimuli direct macropinocytosis of bacteria. Nature 364: 639-642.
    • (1993) Nature , vol.364 , pp. 639-642
    • Francis, C.L.1    Ryan, T.A.2    Jones, B.D.3    Smith, S.J.4    Falkow, S.5
  • 18
    • 0028117273 scopus 로고
    • Salmonella stimulate macrophage macropinocytosis and persist within spacious phago-somes
    • Alpuche-Aranda CM, Racoosin EL, Swanson JA, Miller SI (1994) Salmonella stimulate macrophage macropinocytosis and persist within spacious phago-somes. J Exp Med 179: 601-608.
    • (1994) J Exp Med , vol.179 , pp. 601-608
    • Alpuche-Aranda, C.M.1    Racoosin, E.L.2    Swanson, J.A.3    Miller, S.I.4
  • 19
    • 0028022694 scopus 로고
    • Salmonella invasion of nonphagocytic cells induces formation of macropinosomes in the host cell
    • Garcia-del Portillo F, Finlay BB (1994) Salmonella invasion of nonphagocytic cells induces formation of macropinosomes in the host cell. Infect Immun 62: 4641-4645.
    • (1994) Infect Immun , vol.62 , pp. 4641-4645
    • del portillo, F.G.1    Finlay, B.B.2
  • 20
    • 0031238379 scopus 로고    scopus 로고
    • Molecular and cellular bases of intestinal epithelial cell invasion by Shigella flexneri
    • Sansonetti PJ (1997) [Molecular and cellular bases of intestinal epithelial cell invasion by Shigella flexneri]. C R Acad Sci III 320: 729-734.
    • (1997) C R Acad Sci , vol.320 , pp. 729-734
    • Sansonetti, P.J.1
  • 21
    • 0030994387 scopus 로고    scopus 로고
    • Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin
    • Tran Van Nhieu G, Ben-Ze'ev A, Sansonetti PJ (1997) Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin. Embo J 16: 2717-2729.
    • (1997) Embo J , vol.16 , pp. 2717-2729
    • van Nhieu, G.T.1    Ben-Zeev, A.2    Sansonetti, P.J.3
  • 22
    • 0032462193 scopus 로고    scopus 로고
    • Molecular bases of epithelial cell invasion by Shigella flexneri
    • Sansonetti PJ, Egile C (1998) Molecular bases of epithelial cell invasion by Shigella flexneri. Antonie Van Leeuwenhoek 74: 191-197.
    • (1998) Antonie Van Leeuwenhoek , vol.74 , pp. 191-197
    • Sansonetti, P.J.1    Egile, C.2
  • 23
    • 44649193792 scopus 로고    scopus 로고
    • Internalization of a non-pathogenic mycobacteria by macropinocytosis in human alveolar epithelial A549 cells
    • Garcia-Perez BE, Hernandez-Gonzalez JC, Garcia-Nieto S, Luna-Herrera J (2008) Internalization of a non-pathogenic mycobacteria by macropinocytosis in human alveolar epithelial A549 cells. Microb Pathog 45: 1-6.
    • (2008) Microb Pathog , vol.45 , pp. 1-6
    • Garcia-Perez, B.E.1    Hernandez-Gonzalez, J.C.2    Garcia-Nieto, S.3    Luna-Herrera, J.4
  • 24
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J, Helenius A (2008) Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 320: 531-535.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 25
    • 34548433948 scopus 로고    scopus 로고
    • Coxsackievirus entry across epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5
    • Coyne CB, Shen L, Turner JR, Bergelson JM (2007) Coxsackievirus entry across epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5. Cell Host Microbe 2: 181-192.
    • (2007) Cell Host Microbe , vol.2 , pp. 181-192
    • Coyne, C.B.1    Shen, L.2    Turner, J.R.3    Bergelson, J.M.4
  • 26
    • 0024836461 scopus 로고
    • Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells
    • West MA, Bretscher MS, Watts C (1989) Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J Cell Biol 109: 2731-2739.
    • (1989) J Cell Biol , vol.109 , pp. 2731-2739
    • West, M.A.1    Bretscher, M.S.2    Watts, C.3
  • 27
    • 77149129342 scopus 로고    scopus 로고
    • Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling
    • Koivusalo M, Welch C, Hayashi H, Scott CC, Kim M, et al. (2010) Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling. J Cell Biol 188: 547-563.
    • (2010) J Cell Biol , vol.188 , pp. 547-563
    • Koivusalo, M.1    Welch, C.2    Hayashi, H.3    Scott, C.C.4    Kim, M.5
  • 28
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • Araki N, Johnson MT, Swanson JA (1996) A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J Cell Biol 135: 1249-1260.
    • (1996) J Cell Biol , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 29
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phospho-inositide 3-kinases
    • Lindmo K, Stenmark H (2006) Regulation of membrane traffic by phospho-inositide 3-kinases. J Cell Sci 119: 605-614.
    • (2006) J Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 30
    • 33947718766 scopus 로고    scopus 로고
    • Phosphoinositide metabolism during membrane ruffling and macropinosome formation in EGF-stimulated A431 cells
    • Araki N, Egami Y, Watanabe Y, Hatae T (2007) Phosphoinositide metabolism during membrane ruffling and macropinosome formation in EGF-stimulated A431 cells. Exp Cell Res 313: 1496-1507.
    • (2007) Exp Cell Res , vol.313 , pp. 1496-1507
    • Araki, N.1    Egami, Y.2    Watanabe, Y.3    Hatae, T.4
  • 31
    • 78149427671 scopus 로고    scopus 로고
    • A Unique Platform for H-Ras Signaling Involving Clathrin-independent Endocytosis
    • Porat-Shliom N, Kloog Y, Donaldson JG (2007) A Unique Platform for H-Ras Signaling Involving Clathrin-independent Endocytosis. Mol Biol Cell.
    • (2007) Mol Biol Cell
    • Porat-Shliom, N.1    Kloog, Y.2    Donaldson, J.G.3
  • 32
    • 70350349921 scopus 로고    scopus 로고
    • Sequential signaling in plasma-membrane domains during macropinosome formation in macrophages
    • Yoshida S, Hoppe AD, Araki N, Swanson JA (2009) Sequential signaling in plasma-membrane domains during macropinosome formation in macrophages. J Cell Sci 122: 3250-3261.
    • (2009) J Cell Sci , vol.122 , pp. 3250-3261
    • Yoshida, S.1    Hoppe, A.D.2    Araki, N.3    Swanson, J.A.4
  • 33
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M, McBride H (2001) Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2: 107-117.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 35
    • 33748461590 scopus 로고    scopus 로고
    • The Phox (PX) domain proteins and membrane traffic
    • Seet LF, Hong W (2006) The Phox (PX) domain proteins and membrane traffic. Biochim Biophys Acta 1761: 878-896.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 878-896
    • Seet, L.F.1    Hong, W.2
  • 36
    • 0035941208 scopus 로고    scopus 로고
    • All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phos-phate
    • Yu JW, Lemmon MA (2001) All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phos-phate. J Biol Chem 276: 44179-44184.
    • (2001) J Biol Chem , vol.276 , pp. 44179-44184
    • Yu, J.W.1    Lemmon, M.A.2
  • 37
    • 0034946472 scopus 로고    scopus 로고
    • The PX domains of p47phox and p40phox bind to lipid products of PI(3)K
    • Kanai F, Liu H, Field SJ, Akbary H, Matsuo T, et al. (2001) The PX domains of p47phox and p40phox bind to lipid products of PI(3)K. Nat Cell Biol 3: 675-678.
    • (2001) Nat Cell Biol , vol.3 , pp. 675-678
    • Kanai, F.1    Liu, H.2    Field, S.J.3    Akbary, H.4    Matsuo, T.5
  • 38
    • 0034947026 scopus 로고    scopus 로고
    • Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
    • Cheever ML, Sato TK, de Beer T, Kutateladze TG, Emr SD, et al. (2001) Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nat Cell Biol 3: 613-618.
    • (2001) Nat Cell Biol , vol.3 , pp. 613-618
    • Cheever, M.L.1    Sato, T.K.2    de Beer, T.3    Kutateladze, T.G.4    Emr, S.D.5
  • 40
    • 34250844333 scopus 로고    scopus 로고
    • SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis
    • Yarar D, Waterman-Storer CM, Schmid SL (2007) SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Dev Cell 13: 43-56.
    • (2007) Dev Cell , vol.13 , pp. 43-56
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 41
    • 37249017978 scopus 로고    scopus 로고
    • SNX9 activities are regulated by multiple phosphoinositides through both PX and BAR domains
    • Yarar D, Surka MC, Leonard MC, Schmid SL (2008) SNX9 activities are regulated by multiple phosphoinositides through both PX and BAR domains. Traffic 9: 133-146.
    • (2008) Traffic , vol.9 , pp. 133-146
    • Yarar, D.1    Surka, M.C.2    Leonard, M.C.3    Schmid, S.L.4
  • 42
    • 0034944422 scopus 로고    scopus 로고
    • SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P
    • Xu Y, Hortsman H, Seet L, Wong SH, Hong W (2001) SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P. Nat Cell Biol 3: 658-666.
    • (2001) Nat Cell Biol , vol.3 , pp. 658-666
    • Xu, Y.1    Hortsman, H.2    Seet, L.3    Wong, S.H.4    Hong, W.5
  • 43
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides
    • Carlton J, Bujny M, Peter BJ, Oorschot VM, Rutherford A, et al. (2004) Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides. Curr Biol 14: 1791-1800.
    • (2004) Curr Biol , vol.14 , pp. 1791-1800
    • Carlton, J.1    Bujny, M.2    Peter, B.J.3    Oorschot, V.M.4    Rutherford, A.5
  • 44
    • 0037073673 scopus 로고    scopus 로고
    • The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation
    • Cozier GE, Carlton J, McGregor AH, Gleeson PA, Teasdale RD, et al. (2002) The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation. J Biol Chem 277: 48730-48736.
    • (2002) J Biol Chem , vol.277 , pp. 48730-48736
    • Cozier, G.E.1    Carlton, J.2    McGregor, A.H.3    Gleeson, P.A.4    Teasdale, R.D.5
  • 45
    • 12744264409 scopus 로고    scopus 로고
    • Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation
    • Merino-Trigo A, Kerr MC, Houghton F, Lindberg A, Mitchell C, et al. (2004) Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation. J Cell Sci 117: 6413-6424.
    • (2004) J Cell Sci , vol.117 , pp. 6413-6424
    • Merino-Trigo, A.1    Kerr, M.C.2    Houghton, F.3    Lindberg, A.4    Mitchell, C.5
  • 46
    • 45849110080 scopus 로고    scopus 로고
    • SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking
    • Haberg K, Lundmark R, Carlsson SR (2008) SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking. J Cell Sci 121: 1495-1505.
    • (2008) J Cell Sci , vol.121 , pp. 1495-1505
    • Haberg, K.1    Lundmark, R.2    Carlsson, S.R.3
  • 47
    • 33748288113 scopus 로고    scopus 로고
    • BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • Itoh T, De Camilli P (2006) BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim Biophys Acta 1761: 897-912.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    de Camilli, P.2
  • 48
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: The amphiphysin BAR structure
    • Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, et al. (2004) BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303: 495-499.
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.5
  • 49
    • 1842483252 scopus 로고    scopus 로고
    • Membrane curvature: How BAR domains bend bilayers
    • Zimmerberg J, McLaughlin S (2004) Membrane curvature: how BAR domains bend bilayers. Curr Biol 14: R250-252.
    • (2004) Curr Biol , vol.14
    • Zimmerberg, J.1    McLaughlin, S.2
  • 50
    • 3543025954 scopus 로고    scopus 로고
    • The BAR-domain family of proteins: A case of bending and binding?
    • Habermann B (2004) The BAR-domain family of proteins: a case of bending and binding? EMBO Rep 5: 250-255.
    • (2004) EMBO Rep , vol.5 , pp. 250-255
    • Habermann, B.1
  • 51
    • 25844454807 scopus 로고    scopus 로고
    • Coincidence detection in phosphoinositide signaling
    • Carlton JG, Cullen PJ (2005) Coincidence detection in phosphoinositide signaling. Trends Cell Biol 15: 540-547.
    • (2005) Trends Cell Biol , vol.15 , pp. 540-547
    • Carlton, J.G.1    Cullen, P.J.2
  • 53
    • 0028261425 scopus 로고
    • Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis
    • Stenmark H, Parton RG, Steele-Mortimer O, Lutcke A, Gruenberg J, et al. (1994) Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis. Embo J 13: 1287-1296.
    • (1994) Embo J , vol.13 , pp. 1287-1296
    • Stenmark, H.1    Parton, R.G.2    Steele-Mortimer, O.3    Lutcke, A.4    Gruenberg, J.5
  • 54
    • 69249156036 scopus 로고    scopus 로고
    • Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein
    • Zhang J, Zhang X, Guo Y, Xu L, Pei D (2009) Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein. J Biol Chem 284: 21659-21669.
    • (2009) J Biol Chem , vol.284 , pp. 21659-21669
    • Zhang, J.1    Zhang, X.2    Guo, Y.3    Xu, L.4    Pei, D.5
  • 55
    • 33846242222 scopus 로고    scopus 로고
    • Effect of 3-methyladenine on the fusion process of macropinosomes in EGF-stimulated A431 cells
    • Araki N, Hamasaki M, Egami Y, Hatae T (2006) Effect of 3-methyladenine on the fusion process of macropinosomes in EGF-stimulated A431 cells. Cell Struct Funct 31: 145-157.
    • (2006) Cell Struct Funct , vol.31 , pp. 145-157
    • Araki, N.1    Hamasaki, M.2    Egami, Y.3    Hatae, T.4
  • 56
    • 0032515042 scopus 로고    scopus 로고
    • Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains
    • Kavran JM, Klein DE, Lee A, Falasca M, Isakoff SJ, et al. (1998) Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains. J Biol Chem 273: 30497-30508.
    • (1998) J Biol Chem , vol.273 , pp. 30497-30508
    • Kavran, J.M.1    Klein, D.E.2    Lee, A.3    Falasca, M.4    Isakoff, S.J.5
  • 57
    • 0032805160 scopus 로고    scopus 로고
    • EGF-and NGF-stimulated translocation of cytohesin-1 to the plasma membrane of PC12 cells requires PI 3-kinase activation and a functional cytohesin-1 PH domain
    • Venkateswarlu K, Gunn-Moore F, Tavare JM, Cullen PJ (1999) EGF-and NGF-stimulated translocation of cytohesin-1 to the plasma membrane of PC12 cells requires PI 3-kinase activation and a functional cytohesin-1 PH domain. J Cell Sci 112 (Pt 12): 1957-1965.
    • (1999) J Cell Sci , vol.112 , Issue.12 , pp. 1957-1965
    • Venkateswarlu, K.1    Gunn-Moore, F.2    Tavare, J.M.3    Cullen, P.J.4
  • 58
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trispho-sphate
    • Maehama T, Dixon JE (1998) The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trispho-sphate. J Biol Chem 273: 13375-13378.
    • (1998) J Biol Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 59
    • 34249284831 scopus 로고    scopus 로고
    • PTEN catalysis of phospholipid dephosphorylation reaction follows a two-step mechanism in which the conserved aspartate-92 does not function as the general acid--mechanistic analysis of a familial Cowden disease-associated PTEN mutation
    • Xiao Y, Yeong Chit Chia J, Gajewski JE, Sio Seng Lio D, Mulhern TD, et al. (2007) PTEN catalysis of phospholipid dephosphorylation reaction follows a two-step mechanism in which the conserved aspartate-92 does not function as the general acid--mechanistic analysis of a familial Cowden disease-associated PTEN mutation. Cell Signal 19: 1434-1445.
    • (2007) Cell Signal , vol.19 , pp. 1434-1445
    • Xiao, Y.1    Yeong, C.C.J.2    Gajewski, J.E.3    Sio, S.L.D.4    Mulhern, T.D.5
  • 61
    • 0028211773 scopus 로고
    • The coated pit and macropinocytic pathways serve distinct endosome populations
    • Hewlett LJ, Prescott AR, Watts C (1994) The coated pit and macropinocytic pathways serve distinct endosome populations. J Cell Biol 124: 689-703.
    • (1994) J Cell Biol , vol.124 , pp. 689-703
    • Hewlett, L.J.1    Prescott, A.R.2    Watts, C.3
  • 62
    • 0027278232 scopus 로고
    • Macropinosome maturation and fusion with tubular lysosomes in macrophages
    • Racoosin EL, Swanson JA (1993) Macropinosome maturation and fusion with tubular lysosomes in macrophages. J Cell Biol 121: 1011-1020.
    • (1993) J Cell Biol , vol.121 , pp. 1011-1020
    • Racoosin, E.L.1    Swanson, J.A.2
  • 63
    • 77951460389 scopus 로고    scopus 로고
    • Inhibition of the PtdIns(5) kinase PIKfyve disrupts intracellular replication of Salmonella
    • Kerr MC, Wang JTH, Castro NA, Hamilton NA, Town L, et al. (2010) Inhibition of the PtdIns(5) kinase PIKfyve disrupts intracellular replication of Salmonella. Embo J 29: 1331-1347.
    • (2010) Embo J , vol.29 , pp. 1331-1347
    • Kerr, M.C.1    Wang, J.T.H.2    Castro, N.A.3    Hamilton, N.A.4    Town, L.5
  • 64
    • 78149460078 scopus 로고    scopus 로고
    • Analysing real-time video microscopy: The dynamics and geometry of vesicles and tubules in endocytosis
    • in press
    • Hamilton N, Kerr M, Burrage K, Teasdale R (2005) Analysing real-time video microscopy: the dynamics and geometry of vesicles and tubules in endocytosis. Current Protocols in Cell Biology, in press.
    • (2005) Current Protocols In Cell Biology
    • Hamilton, N.1    Kerr, M.2    Burrage, K.3    Teasdale, R.4
  • 65
  • 66
    • 33846811334 scopus 로고    scopus 로고
    • A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer
    • Wassmer T, Attar N, Bujny MV, Oakley J, Traer CJ, et al. (2007) A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J Cell Sci 120: 45-54.
    • (2007) J Cell Sci , vol.120 , pp. 45-54
    • Wassmer, T.1    Attar, N.2    Bujny, M.V.3    Oakley, J.4    Traer, C.J.5
  • 67
    • 77952393464 scopus 로고    scopus 로고
    • SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane
    • Park J, Kim Y, Lee S, Park JJ, Park ZY, et al. (2010) SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane. J Cell Sci 123: 1742-1750.
    • (2010) J Cell Sci , vol.123 , pp. 1742-1750
    • Park, J.1    Kim, Y.2    Lee, S.3    Park, J.J.4    Park, Z.Y.5
  • 68
    • 44449169861 scopus 로고    scopus 로고
    • SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2
    • Shin N, Ahn N, Chang-Ileto B, Park J, Takei K, et al. (2008) SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2. J Cell Sci 121: 1252-1263.
    • (2008) J Cell Sci , vol.121 , pp. 1252-1263
    • Shin, N.1    Ahn, N.2    Chang-Ileto, B.3    Park, J.4    Takei, K.5
  • 69
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen B, De Renzis S, Nielsen E, Rietdorf J, Zerial M (2000) Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 149: 901-914.
    • (2000) J Cell Biol , vol.149 , pp. 901-914
    • Sonnichsen, B.1    de Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 70
    • 0346752323 scopus 로고    scopus 로고
    • Rab23, a negative regulator of hedgehog signaling, localizes to the plasma membrane and the endocytic pathway
    • Evans TM, Ferguson C, Wainwright BJ, Parton RG, Wicking C (2003) Rab23, a negative regulator of hedgehog signaling, localizes to the plasma membrane and the endocytic pathway. Traffic 4: 869-884.
    • (2003) Traffic , vol.4 , pp. 869-884
    • Evans, T.M.1    Ferguson, C.2    Wainwright, B.J.3    Parton, R.G.4    Wicking, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.