메뉴 건너뛰기




Volumn 581, Issue 11, 2007, Pages 2119-2124

Spatial regulation of exocytosis and cell polarity: Yeast as a model for animal cells

Author keywords

Cell polarity; Exocytosis; Lgl; Rho GTPases

Indexed keywords

GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; PROTEIN CDC42; REGULATOR PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; SRO7 PROTEIN; UNCLASSIFIED DRUG;

EID: 34248217508     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.03.043     Document Type: Short Survey
Times cited : (44)

References (42)
  • 1
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan B., Bowser R., and Novick P. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128 (1995) 1055-1068
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 2
    • 0030930514 scopus 로고    scopus 로고
    • Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles
    • Walch-Solimena C., Collins R.N., and Novick P. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137 (1997) 1495-1509
    • (1997) J. Cell Biol. , vol.137 , pp. 1495-1509
    • Walch-Solimena, C.1    Collins, R.N.2    Novick, P.3
  • 3
    • 0029843493 scopus 로고    scopus 로고
    • The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush D.R., Maurice T., Roth D., and Novick P. The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15 (1996) 6483-6494
    • (1996) EMBO J. , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 4
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo W., Roth D., Walch-Solimena C., and Novick P. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J. 18 (1999) 1071-1080
    • (1999) EMBO J. , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 5
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton R.B., Fasshauer D., Jahn R., and Brunger A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395 (1998) 347-353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 6
    • 0037018149 scopus 로고    scopus 로고
    • The role of cell cycle-regulated expression in the localization of spatial landmark proteins in yeast
    • Schenkman L.R., Caruso C., Page N., and Pringle J.R. The role of cell cycle-regulated expression in the localization of spatial landmark proteins in yeast. J. Cell Biol. 156 (2002) 829-841
    • (2002) J. Cell Biol. , vol.156 , pp. 829-841
    • Schenkman, L.R.1    Caruso, C.2    Page, N.3    Pringle, J.R.4
  • 7
    • 0028925711 scopus 로고
    • Rho-related proteins: actin cytoskeleton and cell cycle
    • Ridley A.J. Rho-related proteins: actin cytoskeleton and cell cycle. Curr. Opin. Genet. Dev. 5 (1995) 24-30
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 24-30
    • Ridley, A.J.1
  • 8
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin D.G., and Nelson W.J. Origins of cell polarity. Cell 84 (1996) 335-344
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 9
    • 0032740682 scopus 로고    scopus 로고
    • The Rho GTPase, Rho3, has a direct role in exocytosis which is distinct from its role in actin polarity
    • Adamo J., Rossi G., and Brennwald P. The Rho GTPase, Rho3, has a direct role in exocytosis which is distinct from its role in actin polarity. Mol. Biol. Cell 10 (1999) 4121-4133
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4121-4133
    • Adamo, J.1    Rossi, G.2    Brennwald, P.3
  • 10
    • 0032938745 scopus 로고    scopus 로고
    • Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70
    • Robinson N.G., Guo L., Imai J., Toh E.A., Matsui Y., and Tamanoi F. Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol. Cell. Biol. 19 (1999) 3580-3587
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3580-3587
    • Robinson, N.G.1    Guo, L.2    Imai, J.3    Toh, E.A.4    Matsui, Y.5    Tamanoi, F.6
  • 11
    • 28544432477 scopus 로고    scopus 로고
    • The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
    • Dong G., Hutagalung A.H., Fu C., Novick P., and Reinisch K.M. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat. Struct. Mol. Biol. 12 (2005) 1094-1100
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1094-1100
    • Dong, G.1    Hutagalung, A.H.2    Fu, C.3    Novick, P.4    Reinisch, K.M.5
  • 12
  • 13
    • 0035969248 scopus 로고    scopus 로고
    • Yeast Cdc42 functions at a late step in exocytosis specifically during polarized growth of the emerging bud
    • Adamo J.E., Moskow J.J., Gladfelter A.S., Viterbo D., Lew D.J., and Brennwald P.J. Yeast Cdc42 functions at a late step in exocytosis specifically during polarized growth of the emerging bud. J. Cell Biol. 155 (2001) 581-592
    • (2001) J. Cell Biol. , vol.155 , pp. 581-592
    • Adamo, J.E.1    Moskow, J.J.2    Gladfelter, A.S.3    Viterbo, D.4    Lew, D.J.5    Brennwald, P.J.6
  • 14
    • 23944480474 scopus 로고    scopus 로고
    • Rho GTPase regulation of exocytosis in yeast is independent of GTP hydrolysis and polarization of the exocyst complex
    • Roumanie O., Wu H., Molk J.N., Rossi G., Bloom K., and Brennwald P. Rho GTPase regulation of exocytosis in yeast is independent of GTP hydrolysis and polarization of the exocyst complex. J. Cell Biol. 170 (2005) 583-594
    • (2005) J. Cell Biol. , vol.170 , pp. 583-594
    • Roumanie, O.1    Wu, H.2    Molk, J.N.3    Rossi, G.4    Bloom, K.5    Brennwald, P.6
  • 15
    • 0032548828 scopus 로고    scopus 로고
    • Sec3p is a spatial landmark for polarized secretion in budding yeast
    • Finger F.P., Hughes T.E., and Novick P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 92 (1998) 559-571
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.P.1    Hughes, T.E.2    Novick, P.3
  • 16
    • 33745841364 scopus 로고    scopus 로고
    • The exocyst defrocked, a framework of rods revealed
    • Munson M., and Novick P. The exocyst defrocked, a framework of rods revealed. Nat. Struct. Mol. Biol. 13 (2006) 557-581
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 557-581
    • Munson, M.1    Novick, P.2
  • 17
    • 0030054647 scopus 로고    scopus 로고
    • The tumor suppressor gene, lethal(2)giant larvae (1(2)g1), is required for cell shape change of epithelial cells during Drosophila development
    • Manfruelli P., Arquier N., Hanratty W.P., and Semeriva M. The tumor suppressor gene, lethal(2)giant larvae (1(2)g1), is required for cell shape change of epithelial cells during Drosophila development. Development 122 (1996) 2283-2294
    • (1996) Development , vol.122 , pp. 2283-2294
    • Manfruelli, P.1    Arquier, N.2    Hanratty, W.P.3    Semeriva, M.4
  • 18
    • 0034617129 scopus 로고    scopus 로고
    • Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors
    • Bilder D., Li M., and Perrimon N. Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors. Science 289 (2000) 113-116
    • (2000) Science , vol.289 , pp. 113-116
    • Bilder, D.1    Li, M.2    Perrimon, N.3
  • 19
    • 0034735789 scopus 로고    scopus 로고
    • Role of cortical tumour-suppressor proteins in asymmetric division of Drosophila neuroblast
    • Ohshiro T., Yagami T., Zhang C., and Matsuzaki F. Role of cortical tumour-suppressor proteins in asymmetric division of Drosophila neuroblast. Nature 408 (2000) 593-596
    • (2000) Nature , vol.408 , pp. 593-596
    • Ohshiro, T.1    Yagami, T.2    Zhang, C.3    Matsuzaki, F.4
  • 20
    • 0034735753 scopus 로고    scopus 로고
    • The tumour-suppressor genes lgl and dlg regulate basal protein targeting in Drosophila neuroblasts
    • Peng C.Y., Manning L., Albertson R., and Doe C.Q. The tumour-suppressor genes lgl and dlg regulate basal protein targeting in Drosophila neuroblasts. Nature 408 (2000) 596-600
    • (2000) Nature , vol.408 , pp. 596-600
    • Peng, C.Y.1    Manning, L.2    Albertson, R.3    Doe, C.Q.4
  • 21
    • 0018099247 scopus 로고
    • Malignant neoplasms of genetic origin in Drosophila melanogaster
    • Gateff E. Malignant neoplasms of genetic origin in Drosophila melanogaster. Science 200 (1978) 1448-1459
    • (1978) Science , vol.200 , pp. 1448-1459
    • Gateff, E.1
  • 22
    • 33646540110 scopus 로고    scopus 로고
    • Lethal giant larvae take on a life of their own
    • Wirtz-Peitz F., and Knoblich J.A. Lethal giant larvae take on a life of their own. Trends Cell Biol. 16 (2006) 234-241
    • (2006) Trends Cell Biol. , vol.16 , pp. 234-241
    • Wirtz-Peitz, F.1    Knoblich, J.A.2
  • 23
    • 33644625714 scopus 로고    scopus 로고
    • Lethal giant puzzle of Lgl
    • Vasioukhin V. Lethal giant puzzle of Lgl. Dev. Neurosci. 28 (2006) 13-24
    • (2006) Dev. Neurosci. , vol.28 , pp. 13-24
    • Vasioukhin, V.1
  • 24
    • 0031904190 scopus 로고    scopus 로고
    • Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor l(2)gl protein, is related to myosins in function
    • Kagami M., Toh-e A., and Matsui Y. Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor l(2)gl protein, is related to myosins in function. Genetics 149 (1998) 1717-1727
    • (1998) Genetics , vol.149 , pp. 1717-1727
    • Kagami, M.1    Toh-e, A.2    Matsui, Y.3
  • 25
    • 0033549568 scopus 로고    scopus 로고
    • Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9
    • Lehman K., Rossi G., Adamo J., and Brennwald P. Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. J. Cell Biol. 146 (1999) 125-140
    • (1999) J. Cell Biol. , vol.146 , pp. 125-140
    • Lehman, K.1    Rossi, G.2    Adamo, J.3    Brennwald, P.4
  • 26
    • 0032509503 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation homeostasis, can be functionally substituted by the Drosophila lethal(2)giant larvae tumor suppressor gene
    • Larsson K., Bohl F., Sjostrom I., Akhtar N., Strand D., Mechler B.M., Grabowski R., and Alder L. The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation homeostasis, can be functionally substituted by the Drosophila lethal(2)giant larvae tumor suppressor gene. J. Biol. Chem. 273 (1998) 33610-33618
    • (1998) J. Biol. Chem. , vol.273 , pp. 33610-33618
    • Larsson, K.1    Bohl, F.2    Sjostrom, I.3    Akhtar, N.4    Strand, D.5    Mechler, B.M.6    Grabowski, R.7    Alder, L.8
  • 28
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D., Sutton R.B., Brünger A.T., and Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA 95 (1998) 15781-15786
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brünger, A.T.3    Jahn, R.4
  • 29
    • 0031696595 scopus 로고    scopus 로고
    • Tomosyn binds t-SNARE proteins via a VAMP-like coiled coil
    • Masuda E.S., Huang B.C., Fisher J.M., Luo Y., and Scheller R.H. Tomosyn binds t-SNARE proteins via a VAMP-like coiled coil. Neuron 21 (1998) 479-480
    • (1998) Neuron , vol.21 , pp. 479-480
    • Masuda, E.S.1    Huang, B.C.2    Fisher, J.M.3    Luo, Y.4    Scheller, R.H.5
  • 30
    • 33845438665 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae tumour suppressor homologue Sro7p/Sop1p is required for targeting of the sodium transporting ATPase to the cell surface
    • Wadskog I., Forsmark A., Rossi G., Schowe C., Öyen M., Goksör M., Ronne H., Brennwald P., and Adler L. The Saccharomyces cerevisiae tumour suppressor homologue Sro7p/Sop1p is required for targeting of the sodium transporting ATPase to the cell surface. Mol. Biol. Cell 12 (2006) 4988-5003
    • (2006) Mol. Biol. Cell , vol.12 , pp. 4988-5003
    • Wadskog, I.1    Forsmark, A.2    Rossi, G.3    Schowe, C.4    Öyen, M.5    Goksör, M.6    Ronne, H.7    Brennwald, P.8    Adler, L.9
  • 31
    • 0029112236 scopus 로고
    • A human homologue of the Drosophila tumour suppressor gene l(2)gl maps to 17p11.2-12 and codes for a cytoskeletal protein that associates with nonmuscle myosin II heavy chain
    • Strand D., Unger S., Corvi R., Hartenstein K., Schenkel H., Kalmes A., Merdes G., Neumann B., Krieg-Schneider F., Coy J.F., et al. A human homologue of the Drosophila tumour suppressor gene l(2)gl maps to 17p11.2-12 and codes for a cytoskeletal protein that associates with nonmuscle myosin II heavy chain. Oncogene 11 (1995) 291-301
    • (1995) Oncogene , vol.11 , pp. 291-301
    • Strand, D.1    Unger, S.2    Corvi, R.3    Hartenstein, K.4    Schenkel, H.5    Kalmes, A.6    Merdes, G.7    Neumann, B.8    Krieg-Schneider, F.9    Coy, J.F.10
  • 32
    • 0027359668 scopus 로고
    • A mouse homologue of the Drosophila tumour-suppressor gene l(2)gl controlled by Hox-C8 in vivo
    • Tomotsune D., Shoji H., Wakamatsu Y., Kondoh H., and Takahashi N. A mouse homologue of the Drosophila tumour-suppressor gene l(2)gl controlled by Hox-C8 in vivo. Nature 365 (1993) 69-72
    • (1993) Nature , vol.365 , pp. 69-72
    • Tomotsune, D.1    Shoji, H.2    Wakamatsu, Y.3    Kondoh, H.4    Takahashi, N.5
  • 33
    • 0036156362 scopus 로고    scopus 로고
    • A mammalian homologue of the Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in MDCK cells
    • Müsch A., Cohen D., Yeaman C.A., Nelson W.J., Rodriguez-Boulan E., and Brennwald P.J. A mammalian homologue of the Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in MDCK cells. Mol. Biol. Cell 13 (2002) 158-168
    • (2002) Mol. Biol. Cell , vol.13 , pp. 158-168
    • Müsch, A.1    Cohen, D.2    Yeaman, C.A.3    Nelson, W.J.4    Rodriguez-Boulan, E.5    Brennwald, P.J.6
  • 34
    • 0028051486 scopus 로고
    • The Drosophila lethal(2)giant larvae tumor suppressor protein is a component of the cytoskeleton
    • Strand D., Raska I., and Mechler B.M. The Drosophila lethal(2)giant larvae tumor suppressor protein is a component of the cytoskeleton. J. Cell Biol. 127 (1994) 1345-1360
    • (1994) J. Cell Biol. , vol.127 , pp. 1345-1360
    • Strand, D.1    Raska, I.2    Mechler, B.M.3
  • 35
    • 20544459380 scopus 로고    scopus 로고
    • Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function
    • Gangar A., Rossi G., Andreeva A., Hales R., and Brennwald P. Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function. Curr. Biol. 15 (2005) 1136-1142
    • (2005) Curr. Biol. , vol.15 , pp. 1136-1142
    • Gangar, A.1    Rossi, G.2    Andreeva, A.3    Hales, R.4    Brennwald, P.5
  • 38
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments
    • Hsu S.C., Hazuka C.D., Roth R., Foletti D.L., Heuser J., and Scheller R.H. Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 20 (1998) 1111-1122
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.C.1    Hazuka, C.D.2    Roth, R.3    Foletti, D.L.4    Heuser, J.5    Scheller, R.H.6
  • 39
    • 0037431329 scopus 로고    scopus 로고
    • The Exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin
    • Inoue M., Chang L., Hwang J., Chiang S.H., and Saltiel A.R. The Exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin. Nature 422 (2003) 629-633
    • (2003) Nature , vol.422 , pp. 629-633
    • Inoue, M.1    Chang, L.2    Hwang, J.3    Chiang, S.H.4    Saltiel, A.R.5
  • 40
    • 27144456598 scopus 로고    scopus 로고
    • Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo
    • Wu S., Mehta S.Q., Pichaud F., Bellen H.J., and Quiocho F.A. Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo. Nat. Struct. Mol. Biol. 12 (2005) 879-885
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 879-885
    • Wu, S.1    Mehta, S.Q.2    Pichaud, F.3    Bellen, H.J.4    Quiocho, F.A.5
  • 41
  • 42
    • 0034056057 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast
    • Pruyne D., and Bretscher A. Polarization of cell growth in yeast. J. Cell Sci. 113 (2000) 571-585
    • (2000) J. Cell Sci. , vol.113 , pp. 571-585
    • Pruyne, D.1    Bretscher, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.