메뉴 건너뛰기




Volumn 118, Issue 1, 2005, Pages 65-77

Ice2p is important for the distribution and structure of the cortical ER network in Saccharomyces cerevisiae

Author keywords

Cortical ER; ER maintenance; Ice2p; Saccharomyces cerevisiae

Indexed keywords

CELL MEMBRANE PROTEIN; PROTEIN ICE2P; UNCLASSIFIED DRUG;

EID: 14044255694     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01583     Document Type: Article
Times cited : (45)

References (49)
  • 1
    • 0033199506 scopus 로고    scopus 로고
    • Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
    • Achleitner, G., Gaigg, B., Krasser, A., Kainersdorfer, E., Kohlwein, S. D., Perktold, A., Zellnig, G. and Daum, G. (1999). Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur. J. Biochem. 264, 545-553.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 545-553
    • Achleitner, G.1    Gaigg, B.2    Krasser, A.3    Kainersdorfer, E.4    Kohlwein, S.D.5    Perktold, A.6    Zellnig, G.7    Daum, G.8
  • 3
    • 0027097849 scopus 로고
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 3, 633-654.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 4
    • 0025363363 scopus 로고
    • Revision of the oligosaccharide structures of yeast carboxypeptidase Y
    • Ballou, L., Hernandez, L., Alvarado, E. and Ballou, C. (1990). Revision of the oligosaccharide structures of yeast carboxypeptidase Y. Proc. Natl. Acad. Sci. USA 87, 3368-3372.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3368-3372
    • Ballou, L.1    Hernandez, L.2    Alvarado, E.3    Ballou, C.4
  • 5
    • 0034161259 scopus 로고    scopus 로고
    • TRAPP stably associates with the Golgi and is required for vesicle docking
    • Barrowman, J., Sacher, M. and Ferro-Novick, S. (2000). TRAPP stably associates with the Golgi and is required for vesicle docking. EMBO J. 19, 862-869.
    • (2000) EMBO J. , vol.19 , pp. 862-869
    • Barrowman, J.1    Sacher, M.2    Ferro-Novick, S.3
  • 6
    • 0023680876 scopus 로고
    • The STE2 gene product is the ligand-binding component of the alpha-factor receptor of Saccharomyces cerevisiae
    • Blumer, K., Reneke, J. and Thorner, J. (1988). The STE2 gene product is the ligand-binding component of the alpha-factor receptor of Saccharomyces cerevisiae. J. Biol. Chem. 263, 10836-10842.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10836-10842
    • Blumer, K.1    Reneke, J.2    Thorner, J.3
  • 7
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J. S. and Glick, B. S. (2004). The mechanisms of vesicle budding and fusion. Cell 116, 153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 8
    • 0028215472 scopus 로고
    • Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae
    • Burns, N., Grimwade, B., Ross-Macdonald, P. B., Choi, E. Y., Finberg, K., Roeder, G. S. and Snyder, M. (1994). Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae. Genes Dev. 8, 1087-1105.
    • (1994) Genes Dev. , vol.8 , pp. 1087-1105
    • Burns, N.1    Grimwade, B.2    Ross-Macdonald, P.B.3    Choi, E.Y.4    Finberg, K.5    Roeder, G.S.6    Snyder, M.7
  • 9
    • 0034599993 scopus 로고    scopus 로고
    • Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes
    • Cao, X. and Barlowe, C. (2000). Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes. J. Cell Biol. 149, 55-66.
    • (2000) J. Cell Biol. , vol.149 , pp. 55-66
    • Cao, X.1    Barlowe, C.2
  • 10
    • 0034611014 scopus 로고    scopus 로고
    • Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p
    • Cronin, S. R., Khoury, A., Ferry, D. K. and Hampton, R. Y. (2000). Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p. J. Cell Biol. 148, 915-924.
    • (2000) J. Cell Biol. , vol.148 , pp. 915-924
    • Cronin, S.R.1    Khoury, A.2    Ferry, D.K.3    Hampton, R.Y.4
  • 11
    • 0035158456 scopus 로고    scopus 로고
    • Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae
    • Du, Y., Pypaert, M., Novick, P. and Ferro-Novick, S. (2001). Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae. Mol. Biol. Cell 12, 2614-2628.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2614-2628
    • Du, Y.1    Pypaert, M.2    Novick, P.3    Ferro-Novick, S.4
  • 12
    • 0028245510 scopus 로고
    • Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends
    • Endow, S. A., Kang, S. J., Satterwhite, L. L., Rose, M. D., Skeen, V. P. and Salmon, E. D. (1994). Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends. EMBO J. 13, 2708-2713.
    • (1994) EMBO J. , vol.13 , pp. 2708-2713
    • Endow, S.A.1    Kang, S.J.2    Satterwhite, L.L.3    Rose, M.D.4    Skeen, V.P.5    Salmon, E.D.6
  • 14
    • 0037036391 scopus 로고    scopus 로고
    • Quality control in the yeast secretory pathway. A misfolded PMA1 H+-ATPase reveals two checkpoints
    • Ferreira, T., Mason, A. B., Pypaert, M., Allen, K. E. and Slayman, C. W. (2002). Quality control in the yeast secretory pathway. A misfolded PMA1 H+-ATPase reveals two checkpoints. J. Biol. Chem. 277, 21027-21040.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21027-21040
    • Ferreira, T.1    Mason, A.B.2    Pypaert, M.3    Allen, K.E.4    Slayman, C.W.5
  • 15
    • 0037144427 scopus 로고    scopus 로고
    • YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins
    • Friedmann, E., Salzberg, Y., Weinberger, A., Shaltiel, S. and Gerst, J. E. (2002). YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins. J. Biol. Chem. 277, 35274-35281.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35274-35281
    • Friedmann, E.1    Salzberg, Y.2    Weinberger, A.3    Shaltiel, S.4    Gerst, J.E.5
  • 16
    • 0028916511 scopus 로고
    • Characterization of a microsomal subtraction associated with mitochondria of the yeast, Saccharomyces cerevisiae. Involvement in synthesis and import of phospholipids into mitochondria
    • Gaigg, B., Simbeni, R., Hrastnik, C., Paltauf, F. and Daum, G. (1995). Characterization of a microsomal subtraction associated with mitochondria of the yeast, Saccharomyces cerevisiae Involvement in synthesis and import of phospholipids into mitochondria. Biochim. Biophys. Acta 1234, 214-220.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 214-220
    • Gaigg, B.1    Simbeni, R.2    Hrastnik, C.3    Paltauf, F.4    Daum, G.5
  • 17
    • 0030069686 scopus 로고    scopus 로고
    • In vivo examination of membrane protein localization and degradation with green fluorescent protein
    • Hampton, R. Y., Koning, A., Wright, R. and Rine, J. (1996). In vivo examination of membrane protein localization and degradation with green fluorescent protein. Proc. Natl. Acad. Sci. USA 93, 828-833.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 828-833
    • Hampton, R.Y.1    Koning, A.2    Wright, R.3    Rine, J.4
  • 18
    • 0032516841 scopus 로고    scopus 로고
    • 5 in the endoplasmic reticulum is transmembrane and luminal domain-dependent
    • 5 in the endoplasmic reticulum is transmembrane and luminal domain-dependent. J. Biol. Chem. 273, 20860-20866.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20860-20866
    • Honsho, M.1    Mitoma, J.-Y.2    Ito, A.3
  • 20
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson, M. R., Nilsson, T. and Peterson, P. A. (1990). Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 9, 3153-3162.
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 21
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • Johnson, A. E. and van Waes, M. A. (1999). The translocon: a dynamic gateway at the ER membrane. Annu. Rev. Cell Dev. Biol. 15, 799-842.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 799-842
    • Johnson, A.E.1    van Waes, M.A.2
  • 22
    • 0028040839 scopus 로고
    • Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multispan membrane glycoproteins
    • Landolt-Marticorena, C. and Reithmeier, R. (1994). Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multispan membrane glycoproteins. Biochem. J. 302 253-260.
    • (1994) Biochem. J. , vol.302 , pp. 253-260
    • Landolt-Marticorena, C.1    Reithmeier, R.2
  • 23
    • 0023693945 scopus 로고
    • Dynamic behavior of endoplasmic reticulum in living cells
    • Lee, C. and Chen, L. B. (1988). Dynamic behavior of endoplasmic reticulum in living cells. Cell 54, 37-46.
    • (1988) Cell , vol.54 , pp. 37-46
    • Lee, C.1    Chen, L.B.2
  • 24
    • 0032509208 scopus 로고    scopus 로고
    • Targeting to the endoplasmic reticulum in yeast cells by determinants present in transmembrane domains
    • Letourneur, F. and Cosson, P. (1998). Targeting to the endoplasmic reticulum in yeast cells by determinants present in transmembrane domains. J. Biol. Chem. 273, 33273-33278.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33273-33278
    • Letourneur, F.1    Cosson, P.2
  • 25
    • 0034799695 scopus 로고    scopus 로고
    • Regulation of organelle membrane fusion by Pkc1p
    • Lin, A., Patel, S. and Latterich, M. (2001). Regulation of organelle membrane fusion by Pkc1p. Traffic 2, 698-704.
    • (2001) Traffic , vol.2 , pp. 698-704
    • Lin, A.1    Patel, S.2    Latterich, M.3
  • 26
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., Mckenzie, A., III, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P. and Pringle, J. R. (1998). Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    Mckenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 27
    • 0024417113 scopus 로고
    • +-ATPase are cytoplasmically located
    • +-ATPase are cytoplasmically located. J. Biol. Chem. 264, 16276-16281.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16276-16281
    • Mandala, S.1    Slayman, C.2
  • 28
    • 0025309665 scopus 로고
    • KAR3, a kinesin-related gene required for yeast nuclear fusion
    • Meluh, P. and Rose, M. (1990). KAR3, a kinesin-related gene required for yeast nuclear fusion. Cell 60 1029-1041.
    • (1990) Cell , vol.60 , pp. 1029-1041
    • Meluh, P.1    Rose, M.2
  • 29
    • 0028361985 scopus 로고
    • KAR3-encoded kinesin is a minus-end-directed motor that functions with centromere binding proteins (CBF3) on an in vitro yeast kinetochore
    • Middleton, K. and Carbon, J. (1994). KAR3-encoded kinesin is a minus-end-directed motor that functions with centromere binding proteins (CBF3) on an in vitro yeast kinetochore. Proc. Natl. Acad. Sci. USA 91, 7212-7216.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7212-7216
    • Middleton, K.1    Carbon, J.2
  • 30
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy, A. D., McCaffery, J. M. and Shaw, J. M. (2000). Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151, 367-380.
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 31
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S. and Pelham, H. R. (1987). A C-terminal signal prevents secretion of luminal ER proteins. Cell 48, 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 32
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I. and von Heijne, G. (1993). Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268, 5798-5801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.1    von Heijne, G.2
  • 34
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham, H. R. (1988). Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J. 7, 913-918.
    • (1988) EMBO J. , vol.7 , pp. 913-918
    • Pelham, H.R.1
  • 35
    • 0033602030 scopus 로고    scopus 로고
    • SNARES and the secretory pathway - Lessons from yeast
    • Pelham, H. R. (1999). SNARES and the secretory pathway - lessons from yeast. Exp. Cell Res. 247, 1-8.
    • (1999) Exp. Cell Res. , vol.247 , pp. 1-8
    • Pelham, H.R.1
  • 36
    • 0032734577 scopus 로고    scopus 로고
    • The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells
    • Pitts, K. R., Yoon, Y., Krueger, E. W. and McNiven, M. A. (1999). The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells. Mol. Biol. Cell 10, 4403-4417.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4403-4417
    • Pitts, K.R.1    Yoon, Y.2    Krueger, E.W.3    McNiven, M.A.4
  • 37
    • 0026335172 scopus 로고
    • Structure of the yeast endoplasmic reticulum: Localization of ER proteins using immunofluorescence and immunoelectron microscopy
    • Preuss, D., Mulholland, J., Kaiser, C. A., Orlean, P., Albright, C., Rose, M. D., Robbins, P. W. and Botstein, D. (1991). Structure of the yeast endoplasmic reticulum: localization of ER proteins using immunofluorescence and immunoelectron microscopy. Yeast 7 891-911.
    • (1991) Yeast , vol.7 , pp. 891-911
    • Preuss, D.1    Mulholland, J.2    Kaiser, C.A.3    Orlean, P.4    Albright, C.5    Rose, M.D.6    Robbins, P.W.7    Botstein, D.8
  • 38
    • 0034618102 scopus 로고    scopus 로고
    • Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae
    • Prinz, W. A., Grzyb, L., Veenhuis, M., Kahana, J. A., Silver, P. A. and Rapoport, T. A. (2000). Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Biol. 150, 461-474.
    • (2000) J. Cell Biol. , vol.150 , pp. 461-474
    • Prinz, W.A.1    Grzyb, L.2    Veenhuis, M.3    Kahana, J.A.4    Silver, P.A.5    Rapoport, T.A.6
  • 39
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
    • Roberg, K. J., Rowley, N. and Kaiser, C. A. (1997). Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. J. Cell Biol. 137 1469-1482.
    • (1997) J. Cell Biol. , vol.137 , pp. 1469-1482
    • Roberg, K.J.1    Rowley, N.2    Kaiser, C.A.3
  • 40
    • 0033577803 scopus 로고    scopus 로고
    • LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum
    • Roberg, K. J., Crotwell, M., Espenshade, P., Gimeno, R. and Kaiser, C. A. (1999). LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J. Cell Biol. 145, 659-672.
    • (1999) J. Cell Biol. , vol.145 , pp. 659-672
    • Roberg, K.J.1    Crotwell, M.2    Espenshade, P.3    Gimeno, R.4    Kaiser, C.A.5
  • 41
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose, M. D., Misra, L. M. and Vogel, J. P. (1989). KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 42
    • 0030932017 scopus 로고    scopus 로고
    • Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins
    • Sato, K., Sato, M. and Nakano, A. (1997). Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins. Proc. Natl. Acad. Sci. USA 94, 9693-9698.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9693-9698
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 43
    • 0141856357 scopus 로고    scopus 로고
    • Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes
    • Sato, K., Sato, M. and Nakano, A. (2003). Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes. Mol. Biol. Cell 14, 3605-3616.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3605-3616
    • Sato, K.1    Sato, M.2    Nakano, A.3
  • 44
    • 0034722347 scopus 로고    scopus 로고
    • Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae
    • Shimoni, Y., Kurihara, T., Ravazzola, M., Amherdt, M., Orci, L. and Schekman, R. (2000). Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J. Cell Biol. 151, 973-984.
    • (2000) J. Cell Biol. , vol.151 , pp. 973-984
    • Shimoni, Y.1    Kurihara, T.2    Ravazzola, M.3    Amherdt, M.4    Orci, L.5    Schekman, R.6
  • 45
    • 0025329534 scopus 로고
    • Recent progress on structural interactions of the endoplasmic reticulum
    • Terasaki, M. (1990). Recent progress on structural interactions of the endoplasmic reticulum. Cell Motil. Cytoskeleton 15, 71-75.
    • (1990) Cell Motil. Cytoskeleton , vol.15 , pp. 71-75
    • Terasaki, M.1
  • 46
    • 0023025842 scopus 로고
    • Microtubules and the endoplasmic reticulum are highly interdependent structures
    • Terasaki, M., Chen, L. and Fujiwara, K. (1986). Microtubules and the endoplasmic reticulum are highly interdependent structures. J. Cell Biol. 103, 1557-1568.
    • (1986) J. Cell Biol. , vol.103 , pp. 1557-1568
    • Terasaki, M.1    Chen, L.2    Fujiwara, K.3
  • 48
    • 0344875517 scopus 로고    scopus 로고
    • Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum
    • Wiederkehr, A., Du, Y., Pypaert, M., Ferro-Novick, S. and Novick, P. (2003). Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum. Mol. Biol. Cell 14, 4770-4782.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4770-4782
    • Wiederkehr, A.1    Du, Y.2    Pypaert, M.3    Ferro-Novick, S.4    Novick, P.5
  • 49
    • 0031028166 scopus 로고    scopus 로고
    • The transmembrane domain of a carboxyl-terminal anchored protein determines localization to the endoplasmic reticulum
    • Yang, M., Ellenberg, J., Bonifacino, J. S. and Weissman, A. M. (1997). The transmembrane domain of a carboxyl-terminal anchored protein determines localization to the endoplasmic reticulum. J. Biol. Chem. 272, 1970-1975.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1970-1975
    • Yang, M.1    Ellenberg, J.2    Bonifacino, J.S.3    Weissman, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.