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Volumn 9, Issue 10, 2010, Pages 1538-1548

Prm1 targeting to contact sites enhances fusion during mating in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PRM1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 77957773483     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00116-10     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 33846820100 scopus 로고    scopus 로고
    • The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane fusion during yeast mating
    • doi:10.1091/mbc.E06-09-0776
    • Aguilar, P. S., A. Engel, and P. Walter. 2007. The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane fusion during yeast mating. Mol. Biol. Cell 18:547-556. doi:10.1091/mbc.E06-09-0776.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 547-556
    • Aguilar, P.S.1    Engel, A.2    Walter, P.3
  • 2
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • doi:10.1093/emboj/16.8.1820
    • Babst, M., T. K. Sato, L. M. Banta, and S. D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831. doi:10.1093/emboj/16.8.1820.
    • (1997) EMBO J , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 3
    • 0037195112 scopus 로고    scopus 로고
    • Cell surface polarization during yeast mating
    • doi:10.1073/ pnas.172517799
    • Bagnat, M., and K. Simons. 2002. Cell surface polarization during yeast mating. Proc. Natl. Acad. Sci. U. S. A. 99:14183-14188. doi:10.1073/ pnas.172517799.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 14183-14188
    • Bagnat, M.1    Simons, K.2
  • 4
    • 0038148746 scopus 로고    scopus 로고
    • Architecture of the influenza hemagglutinin membrane fusion site
    • Bentz, J., and A. Mittal. 2003. Architecture of the influenza hemagglutinin membrane fusion site. Biochim. Biophys. Acta 1614:24-35.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 24-35
    • Bentz, J.1    Mittal, A.2
  • 5
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd, C. G., and S. D. Emr. 1998. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol. Cell 2:157-162.
    • (1998) Mol. Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 6
    • 34248138335 scopus 로고    scopus 로고
    • Cell-cell fusion
    • doi:10.1016/j.febslet.2007.03.033
    • Chen, E. H., E. Grote, W. Mohler, and A. Vignery. 2007. Cell-cell fusion. FEBS Lett. 581:2181-2193. doi:10.1016/j.febslet.2007.03.033.
    • (2007) FEBS Lett , vol.581 , pp. 2181-2193
    • Chen, E.H.1    Grote, E.2    Mohler, W.3    Vignery, A.4
  • 7
    • 14744270939 scopus 로고    scopus 로고
    • Fusogenic activity of EFF-1 is regulated via dynamic localization in fusing somatic cells of C. elegans
    • doi:10.1016/j.cub.2005.01.054
    • del Campo, J. J., E. Opoku-Serebuoh, A. B. Isaacson, V. L. Scranton, M. Tucker, M. Han, and W. A. Mohler. 2005. Fusogenic activity of EFF-1 is regulated via dynamic localization in fusing somatic cells of C. elegans. Curr. Biol. 15:413-423. doi:10.1016/j.cub.2005.01.054.
    • (2005) Curr. Biol , vol.15 , pp. 413-423
    • del Campo, J.J.1    Opoku-Serebuoh, E.2    Isaacson, A.B.3    Scranton, V.L.4    Tucker, M.5    Han, M.6    Mohler, W.A.7
  • 8
    • 70450235266 scopus 로고    scopus 로고
    • Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion
    • doi:10.1074/jbc.M109.047381
    • Domanska, M. K., V. Kiessling, A. Stein, D. Fasshauer, and L. K. Tamm. 2009. Single vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion. J. Biol. Chem. 284:32158-32166. doi:10.1074/jbc.M109.047381.
    • (2009) J. Biol. Chem , vol.284 , pp. 32158-32166
    • Domanska, M.K.1    Kiessling, V.2    Stein, A.3    Fasshauer, D.4    Tamm, L.K.5
  • 9
    • 62449182535 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae PRM1 homolog in Neurospora crassa is involved in vegetative and sexual cell fusion events but also has postfertilization functions
    • doi:10.1534/genetics.108.096149
    • Fleissner, A., S. Diamond, and N. L. Glass. 2009. The Saccharomyces cerevisiae PRM1 homolog in Neurospora crassa is involved in vegetative and sexual cell fusion events but also has postfertilization functions. Genetics 181:497-510. doi:10.1534/genetics.108.096149.
    • (2009) Genetics , vol.181 , pp. 497-510
    • Fleissner, A.1    Diamond, S.2    Glass, N.L.3
  • 10
    • 7244239508 scopus 로고    scopus 로고
    • SNS: Adhesive properties, localization requirements and ectodomain dependence in S2 cells and embryonic myoblasts
    • doi: 10.1016/j.mod.2004.08.001
    • Galletta, B. J., M. Chakravarti, R. Banerjee, and S. M. Abmayr. 2004. SNS: adhesive properties, localization requirements and ectodomain dependence in S2 cells and embryonic myoblasts. Mech. Dev. 121:1455-1468. doi: 10.1016/j.mod.2004.08.001.
    • (2004) Mech. Dev , vol.121 , pp. 1455-1468
    • Galletta, B.J.1    Chakravarti, M.2    Banerjee, R.3    Abmayr, S.M.4
  • 11
    • 0031867273 scopus 로고    scopus 로고
    • Distinct morphological phenotypes of cell fusion mutants
    • Gammie, A. E., V. Brizzio, and M. D. Rose. 1998. Distinct morphological phenotypes of cell fusion mutants. Mol. Biol. Cell 9:1395-1410.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1395-1410
    • Gammie, A.E.1    Brizzio, V.2    Rose, M.D.3
  • 12
    • 0037173615 scopus 로고    scopus 로고
    • Functional profiling of the Saccharomyces cerevisiae genome
    • Giaever, G., et al. 2002. Functional profiling of the Saccharomyces cerevisiae genome. Nature 418:387-391.
    • (2002) Nature , vol.418 , pp. 387-391
    • Giaever, G.1
  • 13
    • 0034735578 scopus 로고    scopus 로고
    • Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating
    • Heiman, M. G., and P. Walter. 2000. Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating. J. Cell Biol. 151:719-730.
    • (2000) J. Cell Biol , vol.151 , pp. 719-730
    • Heiman, M.G.1    Walter, P.2
  • 14
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M. R., T. Nilsson, and P. A. Peterson. 1993. Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121:317-333.
    • (1993) J. Cell Biol , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 15
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., T. Lang, and T. C. Sudhof. 2003. Membrane fusion. Cell 112:519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 16
    • 11144335897 scopus 로고    scopus 로고
    • Prm1 prevents contactdependent lysis of yeast mating pairs
    • doi: 10.1128/EC.3.6.1664-1673.2004
    • Jin, H., C. Carlile, S. Nolan, and E. Grote. 2004. Prm1 prevents contactdependent lysis of yeast mating pairs. Eukaryot. Cell 3:1664-1673. doi: 10.1128/EC.3.6.1664-1673.2004.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1664-1673
    • Jin, H.1    Carlile, C.2    Nolan, S.3    Grote, E.4
  • 17
    • 40849120821 scopus 로고    scopus 로고
    • Ergosterol promotes pheromone signaling and plasma membrane fusion in mating yeast
    • doi:10.1083/jcb.200705076
    • Jin, H., J. M. McCaffery, and E. Grote. 2008. Ergosterol promotes pheromone signaling and plasma membrane fusion in mating yeast. J. Cell Biol. 180:813-826. doi:10.1083/jcb.200705076.
    • (2008) J. Cell Biol , vol.180 , pp. 813-826
    • Jin, H.1    McCaffery, J.M.2    Grote, E.3
  • 18
    • 22044445588 scopus 로고    scopus 로고
    • SEC18/NSFindependent, protein-sorting pathway from the yeast cortical ER to the plasma membrane
    • doi:10.1083/jcb.200503033
    • Juschke, C., A. Wachter, B. Schwappach, and M. Seedorf. 2005. SEC18/NSFindependent, protein-sorting pathway from the yeast cortical ER to the plasma membrane. J. Cell Biol. 169:613-622. doi:10.1083/jcb.200503033.
    • (2005) J. Cell Biol , vol.169 , pp. 613-622
    • Juschke, C.1    Wachter, A.2    Schwappach, B.3    Seedorf, M.4
  • 19
    • 1642356961 scopus 로고    scopus 로고
    • The internalization of yeast Ste6p follows an ordered series of events involving phosphorylation, ubiquitination, recognition and endocytosis
    • doi: 10.1111/j.1600-0854.2004.00168.x
    • Kelm, K. B., G. Huyer, J. C. Huang, and S. Michaelis. 2004. The internalization of yeast Ste6p follows an ordered series of events involving phosphorylation, ubiquitination, recognition and endocytosis. Traffic 5:165-180. doi: 10.1111/j.1600-0854.2004.00168.x.
    • (2004) Traffic , vol.5 , pp. 165-180
    • Kelm, K.B.1    Huyer, G.2    Huang, J.C.3    Michaelis, S.4
  • 21
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., R. Muller, and M. Funk. 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156:119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 22
    • 33745286618 scopus 로고    scopus 로고
    • FUS1 regulates the opening and expansion of fusion pores between mating yeast
    • doi:10.1091/mbc.E05-11-1015
    • Nolan, S., A. E. Cowan, D. E. Koppel, H. Jin, and E. Grote. 2006. FUS1 regulates the opening and expansion of fusion pores between mating yeast. Mol. Biol. Cell 17:2439-2450. doi:10.1091/mbc.E05-11-1015.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2439-2450
    • Nolan, S.1    Cowan, A.E.2    Koppel, D.E.3    Jin, H.4    Grote, E.5
  • 23
    • 77449141497 scopus 로고    scopus 로고
    • PRM1 functions as a disulfide-linked complex in yeast mating
    • doi:10.1074/jbc.M109.068874
    • Olmo, V. N., and E. Grote. 2010. PRM1 functions as a disulfide-linked complex in yeast mating. J. Biol. Chem. 285:2274-2283. doi:10.1074/jbc.M109.068874.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2274-2283
    • Olmo, V.N.1    Grote, E.2
  • 24
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., J. Rohrer, F. Crausaz, and H. Riezman. 1993. end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120:55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 25
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants
    • Raymond, C. K., I. Howald-Stevenson, C. A. Vater, and T. H. Stevens. 1992. Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell 3:1389-1402.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 28
    • 67449133514 scopus 로고    scopus 로고
    • The class V myosin Myo2p is required for Fus2p transport and actin polarization during the yeast mating response
    • doi:10.1091/mbc.E08-09-0923
    • Sheltzer, J. M., and M. D. Rose. 2009. The class V myosin Myo2p is required for Fus2p transport and actin polarization during the yeast mating response. Mol. Biol. Cell 20:2909-2919. doi:10.1091/mbc.E08-09-0923.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2909-2919
    • Sheltzer, J.M.1    Rose, M.D.2
  • 29
    • 0036181710 scopus 로고    scopus 로고
    • The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)- bisphosphate
    • doi:10.1091/mbc.01-10-0476
    • Stefan, C. J., A. Audhya, and S. D. Emr. 2002. The yeast synaptojanin-like proteins control the cellular distribution of phosphatidylinositol (4,5)- bisphosphate. Mol. Biol. Cell 13:542-557. doi:10.1091/mbc.01-10-0476.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 542-557
    • Stefan, C.J.1    Audhya, A.2    Emr, S.D.3
  • 30
    • 0030459065 scopus 로고    scopus 로고
    • The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae
    • Tan, P. K., J. P. Howard, and G. S. Payne. 1996. The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae. J. Cell Biol. 135:1789-1800.
    • (1996) J. Cell Biol. , vol.135 , pp. 1789-1800
    • Tan, P.K.1    Howard, J.P.2    Payne, G.S.3
  • 31
    • 0023376280 scopus 로고
    • Two genes required for cell fusion during yeast conjugation: Evidence for a pheromone-induced surface protein
    • Trueheart, J., J. D. Boeke, and G. R. Fink. 1987. Two genes required for cell fusion during yeast conjugation: evidence for a pheromone-induced surface protein. Mol. Cell. Biol. 7:2316-2328.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2316-2328
    • Trueheart, J.1    Boeke, J.D.2    Fink, G.R.3
  • 32
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • Valdez-Taubas, J., and H. R. Pelham. 2003. Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling. Curr. Biol. 13:1636-1640.
    • (2003) Curr. Biol. , vol.13 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.2
  • 33
    • 84934442503 scopus 로고    scopus 로고
    • Yeast mating: A model system for studying cell and nuclear fusion
    • doi:10.1007/978-1-59745-250-2_1
    • Ydenberg, C. A., and M. D. Rose. 2008. Yeast mating: a model system for studying cell and nuclear fusion. Methods Mol. Biol. 475:3-20. doi:10.1007/978-1-59745-250-2_1.
    • (2008) Methods Mol. Biol. , vol.475 , pp. 3-20
    • Ydenberg, C.A.1    Rose, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.