메뉴 건너뛰기




Volumn 22, Issue 4, 2010, Pages 513-518

Converging views of endocytosis in yeast and mammals

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CLATHRIN; DYNAMIN; PROTEIN AP 2; PROTEIN AP180; RETINA S ANTIGEN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 77955055852     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2010.05.009     Document Type: Review
Times cited : (40)

References (52)
  • 1
    • 27644592393 scopus 로고    scopus 로고
    • Dynamics of endocytic vesicle creation
    • Perrais D., Merrifield C.J. Dynamics of endocytic vesicle creation. Dev Cell 2005, 9:581-592.
    • (2005) Dev Cell , vol.9 , pp. 581-592
    • Perrais, D.1    Merrifield, C.J.2
  • 2
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen M., Toret C.P., Drubin D.G. Harnessing actin dynamics for clathrin-mediated endocytosis. Nat Rev Mol Cell Biol 2006, 7:404-414.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 3
    • 0035006256 scopus 로고    scopus 로고
    • Clathrin function in yeast endocytosis
    • Baggett J.J., Wendland B. Clathrin function in yeast endocytosis. Traffic 2001, 2:297-302.
    • (2001) Traffic , vol.2 , pp. 297-302
    • Baggett, J.J.1    Wendland, B.2
  • 4
  • 6
    • 4444317360 scopus 로고    scopus 로고
    • The yeast dynamin-related GTPase Vps1p functions in the organization of the actin cytoskeleton via interaction with Sla1p
    • Yu X., Cai M. The yeast dynamin-related GTPase Vps1p functions in the organization of the actin cytoskeleton via interaction with Sla1p. J Cell Sci 2004, 117:3839-3853.
    • (2004) J Cell Sci , vol.117 , pp. 3839-3853
    • Yu, X.1    Cai, M.2
  • 7
    • 77952010424 scopus 로고    scopus 로고
    • The yeast dynamin-like protein Vps1:vps1 mutations perturb the internalization and the motility of endocytic vesicles and endosomes via disorganization of the actin cytoskeleton
    • Nannapaneni S., Wang D., Jain S., Schroeder B., Highfill C., Reustle L., Pittsley D., Maysent A., Moulder S., McDowell R., et al. The yeast dynamin-like protein Vps1:vps1 mutations perturb the internalization and the motility of endocytic vesicles and endosomes via disorganization of the actin cytoskeleton. Eur J Cell Biol 2010, 89:499-508.
    • (2010) Eur J Cell Biol , vol.89 , pp. 499-508
    • Nannapaneni, S.1    Wang, D.2    Jain, S.3    Schroeder, B.4    Highfill, C.5    Reustle, L.6    Pittsley, D.7    Maysent, A.8    Moulder, S.9    McDowell, R.10
  • 8
    • 70349994670 scopus 로고    scopus 로고
    • A yeast killer toxin screen provides insights into a/b toxin entry, trafficking, and killing mechanisms
    • Carroll S.Y., Stirling P.C., Stimpson H.E.M., Giesselmann E., Schmitt M.J., Drubin D.G. A yeast killer toxin screen provides insights into a/b toxin entry, trafficking, and killing mechanisms. Dev Cell 2009, 17:552-560.
    • (2009) Dev Cell , vol.17 , pp. 552-560
    • Carroll, S.Y.1    Stirling, P.C.2    Stimpson, H.E.M.3    Giesselmann, E.4    Schmitt, M.J.5    Drubin, D.G.6
  • 10
    • 23944499524 scopus 로고    scopus 로고
    • AP180 maintains the distribution of synaptic and vesicle proteins in the nerve terminal and indirectly regulates the efficacy of Ca2+-triggered exocytosis
    • Bao H., Daniels R.W., MacLeod G.T., Charlton M.P., Atwood H.L., Zhang B. AP180 maintains the distribution of synaptic and vesicle proteins in the nerve terminal and indirectly regulates the efficacy of Ca2+-triggered exocytosis. J Neurophysiol 2005, 94:1888-1903.
    • (2005) J Neurophysiol , vol.94 , pp. 1888-1903
    • Bao, H.1    Daniels, R.W.2    MacLeod, G.T.3    Charlton, M.P.4    Atwood, H.L.5    Zhang, B.6
  • 11
    • 33746627569 scopus 로고    scopus 로고
    • Factors regulating the abundance and localization of synaptobrevin in the plasma membrane
    • Dittman J.S., Kaplan J.M. Factors regulating the abundance and localization of synaptobrevin in the plasma membrane. Proc Natl Acad Sci USA 2006, 103:11399-11404.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11399-11404
    • Dittman, J.S.1    Kaplan, J.M.2
  • 12
  • 14
    • 36549042931 scopus 로고    scopus 로고
    • A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles
    • Miller S.E., Collins B.M., McCoy A.J., Robinson M.S., Owen D.J. A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles. Nature 2007, 450:570-574.
    • (2007) Nature , vol.450 , pp. 570-574
    • Miller, S.E.1    Collins, B.M.2    McCoy, A.J.3    Robinson, M.S.4    Owen, D.J.5
  • 15
    • 70350336434 scopus 로고    scopus 로고
    • Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation
    • Reider A., Barker S.L., Mishra S.K., Im Y.J., Maldonado-Báez L., Hurley J.H., Traub L.M., Wendland B. Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. EMBO J 2009, 28:3103-3116.
    • (2009) EMBO J , vol.28 , pp. 3103-3116
    • Reider, A.1    Barker, S.L.2    Mishra, S.K.3    Im, Y.J.4    Maldonado-Báez, L.5    Hurley, J.H.6    Traub, L.M.7    Wendland, B.8
  • 16
    • 73949119447 scopus 로고    scopus 로고
    • Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast
    • E09-05-0429v0421.
    • Stimpson H, Toret C, Cheng A, Pauly B, Drubin D: Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast. Mol Biol Cell 2009:E09-05-0429v0421.
    • (2009) Mol Biol Cell
    • Stimpson, H.1    Toret, C.2    Cheng, A.3    Pauly, B.4    Drubin, D.5
  • 18
    • 77954412857 scopus 로고    scopus 로고
    • Subcellular membrane curvature mediated by the BAR domain superfamily proteins
    • Suetsugu S., Toyooka K., Senju Y. Subcellular membrane curvature mediated by the BAR domain superfamily proteins. Semin Cell Dev Biol 2009.
    • (2009) Semin Cell Dev Biol
    • Suetsugu, S.1    Toyooka, K.2    Senju, Y.3
  • 20
    • 69249135065 scopus 로고    scopus 로고
    • Tickets to ride: selecting cargo for clathrin-regulated internalization
    • Traub L.M., Traub L.M. Tickets to ride: selecting cargo for clathrin-regulated internalization. Nat Rev Mol Cell Biol 2009, 10:583.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 583
    • Traub, L.M.1    Traub, L.M.2
  • 21
    • 55549102963 scopus 로고    scopus 로고
    • Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface
    • Lin C., Macgurn J., Chu T., Stefan C., Emr S. Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface. Cell 2008.
    • (2008) Cell
    • Lin, C.1    Macgurn, J.2    Chu, T.3    Stefan, C.4    Emr, S.5
  • 22
    • 57049101734 scopus 로고    scopus 로고
    • Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1
    • Nikko E., Sullivan J., Pelham H. Arrestin-like proteins mediate ubiquitination and endocytosis of the yeast metal transporter Smf1. EMBO Rep 2008.
    • (2008) EMBO Rep
    • Nikko, E.1    Sullivan, J.2    Pelham, H.3
  • 23
    • 65949089009 scopus 로고    scopus 로고
    • The arrestin fold: variations on a theme
    • Aubry L., Guetta D., Klein G. The arrestin fold: variations on a theme. Curr Genomics 2009, 10:133-142.
    • (2009) Curr Genomics , vol.10 , pp. 133-142
    • Aubry, L.1    Guetta, D.2    Klein, G.3
  • 24
    • 70649112359 scopus 로고    scopus 로고
    • Arrestin-mediated endocytosis of yeast plasma membrane transporters
    • Nikko E., Pelham H.R.B. Arrestin-mediated endocytosis of yeast plasma membrane transporters. Traffic 2009, 10:1856-1867.
    • (2009) Traffic , vol.10 , pp. 1856-1867
    • Nikko, E.1    Pelham, H.R.B.2
  • 25
    • 34548546480 scopus 로고    scopus 로고
    • Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase
    • Liu J., Sitaram A., Burd C.G. Regulation of copper-dependent endocytosis and vacuolar degradation of the yeast copper transporter, Ctr1p, by the Rsp5 ubiquitin ligase. Traffic 2007, 8:1375-1384.
    • (2007) Traffic , vol.8 , pp. 1375-1384
    • Liu, J.1    Sitaram, A.2    Burd, C.G.3
  • 26
    • 51349159616 scopus 로고    scopus 로고
    • Different ubiquitin signals act at the golgi and plasma membrane to direct GAP1 trafficking
    • Risinger A.L., Kaiser C.A. Different ubiquitin signals act at the golgi and plasma membrane to direct GAP1 trafficking. Mol Biol Cell 2008, 19:2962-2972.
    • (2008) Mol Biol Cell , vol.19 , pp. 2962-2972
    • Risinger, A.L.1    Kaiser, C.A.2
  • 29
    • 73849117900 scopus 로고    scopus 로고
    • Requirements for recruitment of a G protein-coupled receptor to clathrin-coated pits in budding yeast
    • Toshima J.Y., Nakanishi J-i, Mizuno K., Toshima J., Drubin D.G. Requirements for recruitment of a G protein-coupled receptor to clathrin-coated pits in budding yeast. Mol Biol Cell 2009, 20:5039-5050.
    • (2009) Mol Biol Cell , vol.20 , pp. 5039-5050
    • Toshima, J.Y.1    Nakanishi J-i2    Mizuno, K.3    Toshima, J.4    Drubin, D.G.5
  • 30
    • 52049117442 scopus 로고    scopus 로고
    • Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor
    • Shenoy S.K., Xiao K., Venkataramanan V., Snyder P.M., Freedman N.J., Weissman A.M. Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor. J Biol Chem 2008, 283:22166-22176.
    • (2008) J Biol Chem , vol.283 , pp. 22166-22176
    • Shenoy, S.K.1    Xiao, K.2    Venkataramanan, V.3    Snyder, P.M.4    Freedman, N.J.5    Weissman, A.M.6
  • 31
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih S.C., Katzmann D.J., Schnell J.D., Sutanto M., Emr S.D., Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat Cell Biol 2002, 4:389-393.
    • (2002) Nat Cell Biol , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 32
    • 71849101657 scopus 로고    scopus 로고
    • The function of yeast epsin and Ede1 ubiquitin-binding domains during receptor internalization
    • Dores M.R., Schnell J.D., Maldonado-Baez L., Wendland B., Hicke L. The function of yeast epsin and Ede1 ubiquitin-binding domains during receptor internalization. Traffic 2010, 11:151-160.
    • (2010) Traffic , vol.11 , pp. 151-160
    • Dores, M.R.1    Schnell, J.D.2    Maldonado-Baez, L.3    Wendland, B.4    Hicke, L.5
  • 34
    • 0037092043 scopus 로고    scopus 로고
    • Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis
    • Howard J.P., Hutton J.L., Olson J.M., Payne G.S. Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. J Cell Biol 2002, 157:315-326.
    • (2002) J Cell Biol , vol.157 , pp. 315-326
    • Howard, J.P.1    Hutton, J.L.2    Olson, J.M.3    Payne, G.S.4
  • 35
    • 34247243351 scopus 로고    scopus 로고
    • Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif
    • Mahadev R.K., Di Pietro S.M., Olson J.M., Piao H.L., Payne G.S., Overduin M. Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif. EMBO J 2007, 26:1963-1971.
    • (2007) EMBO J , vol.26 , pp. 1963-1971
    • Mahadev, R.K.1    Di Pietro, S.M.2    Olson, J.M.3    Piao, H.L.4    Payne, G.S.5    Overduin, M.6
  • 36
    • 16344371089 scopus 로고    scopus 로고
    • Highly cooperative control of endocytosis by clathrin
    • Moskowitz H.S., Yokoyama C.T., Ryan T.A. Highly cooperative control of endocytosis by clathrin. Mol Biol Cell 2005, 16:1769-1776.
    • (2005) Mol Biol Cell , vol.16 , pp. 1769-1776
    • Moskowitz, H.S.1    Yokoyama, C.T.2    Ryan, T.A.3
  • 37
    • 12844265252 scopus 로고    scopus 로고
    • A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
    • Yarar D., Waterman-Storer C.M., Schmid S.L. A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis. Mol Biol Cell 2005, 16:964-975.
    • (2005) Mol Biol Cell , vol.16 , pp. 964-975
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 38
    • 70349764506 scopus 로고    scopus 로고
    • Distinct dynamics of endocytic clathrin-coated pits and coated plaques
    • Saffarian S., Cocucci E., Kirchhausen T. Distinct dynamics of endocytic clathrin-coated pits and coated plaques. PLoS Biol 2009, 7:e1000191.
    • (2009) PLoS Biol , vol.7
    • Saffarian, S.1    Cocucci, E.2    Kirchhausen, T.3
  • 39
    • 68249085870 scopus 로고    scopus 로고
    • Differential requirements for actin during yeast and mammalian endocytosis
    • Aghamohammadzadeh S., Ayscough K. Differential requirements for actin during yeast and mammalian endocytosis. Nat Cell Biol 2009.
    • (2009) Nat Cell Biol
    • Aghamohammadzadeh, S.1    Ayscough, K.2
  • 40
    • 70349780604 scopus 로고    scopus 로고
    • Clathrin couture: fashioning distinctive membrane coats at the cell surface
    • Traub L.M. Clathrin couture: fashioning distinctive membrane coats at the cell surface. PLoS Biol 2009, 7:e1000192.
    • (2009) PLoS Biol , vol.7
    • Traub, L.M.1
  • 44
    • 33745882646 scopus 로고    scopus 로고
    • Endocytic vesicle scission by lipid phase boundary forces
    • Liu J., Kaksonen M., Drubin D.G., Oster G. Endocytic vesicle scission by lipid phase boundary forces. Proc Natl Acad Sci USA 2006, 103:10277-10282.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10277-10282
    • Liu, J.1    Kaksonen, M.2    Drubin, D.G.3    Oster, G.4
  • 45
    • 34247526437 scopus 로고    scopus 로고
    • PtdIns(4,5)P2 turnover is required for multiple stages during clathrin- and actin-dependent endocytic internalization
    • Sun Y., Carroll S., Kaksonen M., Toshima J.Y., Drubin D.G. PtdIns(4,5)P2 turnover is required for multiple stages during clathrin- and actin-dependent endocytic internalization. J Cell Biol 2007, 177:355-367.
    • (2007) J Cell Biol , vol.177 , pp. 355-367
    • Sun, Y.1    Carroll, S.2    Kaksonen, M.3    Toshima, J.Y.4    Drubin, D.G.5
  • 47
    • 0033042659 scopus 로고    scopus 로고
    • Regulatory role of SH3 domain-mediated protein-protein interactions in synaptic vesicle endocytosis
    • McPherson P.S. Regulatory role of SH3 domain-mediated protein-protein interactions in synaptic vesicle endocytosis. Cell Signal 1999, 11:229-238.
    • (1999) Cell Signal , vol.11 , pp. 229-238
    • McPherson, P.S.1
  • 48
    • 33846821794 scopus 로고    scopus 로고
    • Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis
    • Krendel M., Osterweil E.K., Mooseker M.S. Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett 2007, 581:644-650.
    • (2007) FEBS Lett , vol.581 , pp. 644-650
    • Krendel, M.1    Osterweil, E.K.2    Mooseker, M.S.3
  • 51
    • 33846053104 scopus 로고    scopus 로고
    • NPFXD-mediated endocytosis is required for polarity and function of a yeast cell wall stress sensor
    • Piao H.L., Machado I.M., Payne G.S. NPFXD-mediated endocytosis is required for polarity and function of a yeast cell wall stress sensor. Mol Biol Cell 2007, 18:57-65.
    • (2007) Mol Biol Cell , vol.18 , pp. 57-65
    • Piao, H.L.1    Machado, I.M.2    Payne, G.S.3
  • 52
    • 75749137330 scopus 로고    scopus 로고
    • Recruitment of the ESCRT machinery to a putative seven-transmembrane-domain receptor is mediated by an arrestin-related protein
    • Herrador A., Herranz S., Lara D., Vincent O. Recruitment of the ESCRT machinery to a putative seven-transmembrane-domain receptor is mediated by an arrestin-related protein. Mol Cell Biol 2010, 30:897-907.
    • (2010) Mol Cell Biol , vol.30 , pp. 897-907
    • Herrador, A.1    Herranz, S.2    Lara, D.3    Vincent, O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.