메뉴 건너뛰기




Volumn 29, Issue 1, 2014, Pages 31-38

Barriers to uniformity within the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; SEPTIN;

EID: 84909578938     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2014.03.007     Document Type: Review
Times cited : (7)

References (48)
  • 1
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann O., Walz B. Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Int Rev Cytol 2001, 205:149-214.
    • (2001) Int Rev Cytol , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 2
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007, 8:519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 3
    • 33746778834 scopus 로고    scopus 로고
    • Rough sheets and smooth tubules
    • Shibata Y., Voeltz G.K., Rapoport T.A. Rough sheets and smooth tubules. Cell 2006, 126:435-439.
    • (2006) Cell , vol.126 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 4
    • 0030780576 scopus 로고    scopus 로고
    • Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores
    • Subramanian K., Meyer T. Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores. Cell 1997, 89:963-971.
    • (1997) Cell , vol.89 , pp. 963-971
    • Subramanian, K.1    Meyer, T.2
  • 6
    • 22344453326 scopus 로고    scopus 로고
    • Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth
    • Luedeke C., Frei S.B., Sbalzarini I., Schwarz H., Spang A., Barral Y. Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth. J Cell Biol 2005, 169:897-908.
    • (2005) J Cell Biol , vol.169 , pp. 897-908
    • Luedeke, C.1    Frei, S.B.2    Sbalzarini, I.3    Schwarz, H.4    Spang, A.5    Barral, Y.6
  • 8
    • 0036951931 scopus 로고    scopus 로고
    • Septins: a ring to part mother and daughter
    • Faty M., Fink M., Barral Y. Septins: a ring to part mother and daughter. Curr Genet 2002, 41:123-131.
    • (2002) Curr Genet , vol.41 , pp. 123-131
    • Faty, M.1    Fink, M.2    Barral, Y.3
  • 9
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot I., Klee S.K., Pellman D. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat Cell Biol 2002, 4:42-50.
    • (2002) Nat Cell Biol , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 12
    • 0037383708 scopus 로고    scopus 로고
    • Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function
    • Casamayor A., Snyder M. Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function. Mol Cell Biol 2003, 23:2762-2777.
    • (2003) Mol Cell Biol , vol.23 , pp. 2762-2777
    • Casamayor, A.1    Snyder, M.2
  • 13
    • 84862908117 scopus 로고    scopus 로고
    • Subunit-dependent modulation of septin assembly: budding yeast septin Shs1 promotes ring and gauze formation
    • Garcia G., Bertin A., Li Z., Song Y., McMurray M.A., Thorner J., Nogales E. Subunit-dependent modulation of septin assembly: budding yeast septin Shs1 promotes ring and gauze formation. J Cell Biol 2011, 195:993-1004.
    • (2011) J Cell Biol , vol.195 , pp. 993-1004
    • Garcia, G.1    Bertin, A.2    Li, Z.3    Song, Y.4    McMurray, M.A.5    Thorner, J.6    Nogales, E.7
  • 14
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentalization of eukaryotic membranes
    • Caudron F., Barral Y. Septins and the lateral compartmentalization of eukaryotic membranes. Dev Cell 2009, 16:493-506.
    • (2009) Dev Cell , vol.16 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 15
    • 49649106438 scopus 로고    scopus 로고
    • A mechanism for asymmetric segregation of age during yeast budding
    • Shcheprova Z., Baldi S., Frei S.B., Gonnet G., Barral Y. A mechanism for asymmetric segregation of age during yeast budding. Nature 2008, 454:728-734.
    • (2008) Nature , vol.454 , pp. 728-734
    • Shcheprova, Z.1    Baldi, S.2    Frei, S.B.3    Gonnet, G.4    Barral, Y.5
  • 17
    • 79151468782 scopus 로고    scopus 로고
    • Artificial tethering to nuclear pores promotes partitioning of extrachromosomal DNA during yeast asymmetric cell division
    • Khmelinskii A., Meurer M., Knop M., Schiebel E. Artificial tethering to nuclear pores promotes partitioning of extrachromosomal DNA during yeast asymmetric cell division. Curr Biol 2011, 21:R17-R18.
    • (2011) Curr Biol , vol.21
    • Khmelinskii, A.1    Meurer, M.2    Knop, M.3    Schiebel, E.4
  • 18
    • 84887515034 scopus 로고    scopus 로고
    • Inheritance of yeast nuclear pore complexes requires the Nsp1p subcomplex
    • Makio T., Lapetina D.L., Wozniak R.W. Inheritance of yeast nuclear pore complexes requires the Nsp1p subcomplex. J Cell Biol 2013, 203:187-196.
    • (2013) J Cell Biol , vol.203 , pp. 187-196
    • Makio, T.1    Lapetina, D.L.2    Wozniak, R.W.3
  • 19
    • 84887522828 scopus 로고    scopus 로고
    • The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1
    • Colombi P., Webster B.M., Fröhlich F., Lusk C.P. The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1. J Cell Biol 2013, 203:215-232.
    • (2013) J Cell Biol , vol.203 , pp. 215-232
    • Colombi, P.1    Webster, B.M.2    Fröhlich, F.3    Lusk, C.P.4
  • 20
    • 79955488489 scopus 로고    scopus 로고
    • A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature
    • West M., Zurek N., Hoenger A., Voeltz G.K. A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. J Cell Biol 2011, 193:333-346.
    • (2011) J Cell Biol , vol.193 , pp. 333-346
    • West, M.1    Zurek, N.2    Hoenger, A.3    Voeltz, G.K.4
  • 21
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz G.K., Prinz W.A., Shibata Y., Rist J.M., Rapoport T.A. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 2006, 124:573-586.
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 26
    • 34447519108 scopus 로고    scopus 로고
    • Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes
    • Nikonov A.V., Hauri H.-P., Lauring B., Kreibich G. Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes. J Cell Sci 2007, 120:2248-2258.
    • (2007) J Cell Sci , vol.120 , pp. 2248-2258
    • Nikonov, A.V.1    Hauri, H.-P.2    Lauring, B.3    Kreibich, G.4
  • 29
    • 35348834213 scopus 로고    scopus 로고
    • Role of septin cytoskeleton in spine morphogenesis and dendrite development in neurons
    • Tada T., Simonetta A., Batterton M., Kinoshita M., Edbauer D., Sheng M. Role of septin cytoskeleton in spine morphogenesis and dendrite development in neurons. Curr Biol 2007, 17:1752-1758.
    • (2007) Curr Biol , vol.17 , pp. 1752-1758
    • Tada, T.1    Simonetta, A.2    Batterton, M.3    Kinoshita, M.4    Edbauer, D.5    Sheng, M.6
  • 30
    • 35348907374 scopus 로고    scopus 로고
    • The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology
    • Xie Y., Vessey J.P., Konecna A., Dahm R., Macchi P., Kiebler M.A. The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology. Curr Biol 2007, 17:1746-1751.
    • (2007) Curr Biol , vol.17 , pp. 1746-1751
    • Xie, Y.1    Vessey, J.P.2    Konecna, A.3    Dahm, R.4    Macchi, P.5    Kiebler, M.A.6
  • 31
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • Levine T. Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol 2004, 14:483-490.
    • (2004) Trends Cell Biol , vol.14 , pp. 483-490
    • Levine, T.1
  • 32
    • 79960739849 scopus 로고    scopus 로고
    • Lipid transfer and signaling at organelle contact sites: the tip of the iceberg
    • Toulmay A., Prinz W.A. Lipid transfer and signaling at organelle contact sites: the tip of the iceberg. Curr Opin Cell Biol 2011, 23:458-463.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 458-463
    • Toulmay, A.1    Prinz, W.A.2
  • 33
    • 79959437055 scopus 로고    scopus 로고
    • STIM proteins and the endoplasmic reticulum-plasma membrane junctions
    • Carrasco S., Meyer T. STIM proteins and the endoplasmic reticulum-plasma membrane junctions. Annu Rev Biochem 2011, 80:973-1000.
    • (2011) Annu Rev Biochem , vol.80 , pp. 973-1000
    • Carrasco, S.1    Meyer, T.2
  • 34
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh B.J., Mastronarde D.N., Buttle K.F., Howell K.E., McIntosh J.R. Organellar relationships in the golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc Natl Acad Sci U S A 2001, 98:2399-2406.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 35
  • 37
    • 84863611406 scopus 로고    scopus 로고
    • Yeast Ist2 recruits the endoplasmic reticulum to the plasma membrane and creates a ribosome-free membrane microcompartment
    • Wolf W., Kilic A., Schrul B., Lorenz H., Schwappach B., Seedorf M. Yeast Ist2 recruits the endoplasmic reticulum to the plasma membrane and creates a ribosome-free membrane microcompartment. PLoS ONE 2012, 7:e39703.
    • (2012) PLoS ONE , vol.7
    • Wolf, W.1    Kilic, A.2    Schrul, B.3    Lorenz, H.4    Schwappach, B.5    Seedorf, M.6
  • 38
    • 36248938166 scopus 로고    scopus 로고
    • Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2+ levels
    • Goetz J.G., Genty H., St-Pierre P., Dang T., Joshi B., Sauve R., Vogl W., Nabi I.R. Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2+ levels. J Cell Sci 2007, 120:3553-3564.
    • (2007) J Cell Sci , vol.120 , pp. 3553-3564
    • Goetz, J.G.1    Genty, H.2    St-Pierre, P.3    Dang, T.4    Joshi, B.5    Sauve, R.6    Vogl, W.7    Nabi, I.R.8
  • 39
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C., Voelker D.R., Langer T. Making heads or tails of phospholipids in mitochondria. J Cell Biol 2011, 192:7-16.
    • (2011) J Cell Biol , vol.192 , pp. 7-16
    • Osman, C.1    Voelker, D.R.2    Langer, T.3
  • 41
    • 84872202122 scopus 로고    scopus 로고
    • ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae
    • Voss C., Lahiri S., Young B.P., Loewen C.J., Prinz W.A. ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae. J Cell Sci 2012, 125:4791-4799.
    • (2012) J Cell Sci , vol.125 , pp. 4791-4799
    • Voss, C.1    Lahiri, S.2    Young, B.P.3    Loewen, C.J.4    Prinz, W.A.5
  • 43
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • Stefan C.J., Manford A.G., Baird D., Yamada-Hanff J., Mao Y., Emr S.D. Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites. Cell 2011, 144:389-401.
    • (2011) Cell , vol.144 , pp. 389-401
    • Stefan, C.J.1    Manford, A.G.2    Baird, D.3    Yamada-Hanff, J.4    Mao, Y.5    Emr, S.D.6
  • 46
    • 84870793680 scopus 로고    scopus 로고
    • ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology
    • Manford A.G., Stefan C.J., Yuan H.L., Macgurn J.A., Emr S.D. ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology. Dev Cell 2012, 23:1129-1140.
    • (2012) Dev Cell , vol.23 , pp. 1129-1140
    • Manford, A.G.1    Stefan, C.J.2    Yuan, H.L.3    Macgurn, J.A.4    Emr, S.D.5
  • 47
    • 84858123139 scopus 로고    scopus 로고
    • A conserved membrane-binding domain targets proteins to organelle contact sites
    • Toulmay A., Prinz W.A. A conserved membrane-binding domain targets proteins to organelle contact sites. J Cell Sci 2012, 10.1242/jcs.085118.
    • (2012) J Cell Sci
    • Toulmay, A.1    Prinz, W.A.2
  • 48
    • 11144246540 scopus 로고    scopus 로고
    • Golgi inheritance in small buds of Saccharomyces cerevisiae is linked to endoplasmic reticulum inheritance
    • Reinke C.A., Kozik P., Glick B.S. Golgi inheritance in small buds of Saccharomyces cerevisiae is linked to endoplasmic reticulum inheritance. Proc Natl Acad Sci U S A 2004, 101:18018-18023.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 18018-18023
    • Reinke, C.A.1    Kozik, P.2    Glick, B.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.