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Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
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Hicke L, Riezman H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell. 84:1996;277-287.
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Hicke, L.1
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Ubiquitination of the yeast a factor receptor
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Roth AF, Davis NG. Ubiquitination of the yeast a factor receptor. J Cell Biol. 134:1996;661-674.
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Agonist-specific conformational changes in the yeast α-factor pheromone receptor
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Bukusoglu G, Jenness DD. Agonist-specific conformational changes in the yeast α-factor pheromone receptor. Mol Cell Biol. 16:1996;4818-4823.
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Bukusoglu, G.1
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Mutations that alter the third cytoplasmic loop of the a-factor receptor lead to a constitutive and hypersensitive phenotype
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Boone C, Davis NG, Sprague GF. Mutations that alter the third cytoplasmic loop of the a-factor receptor lead to a constitutive and hypersensitive phenotype. Proc Natl Acad Sci USA. 90:1993;9921-9925.
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Boone, C.1
Davis, N.G.2
Sprague, G.F.3
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0028273467
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The third cytoplasmic loop of a yeast G-protein-coupled receptor controls pathway activation, ligand discrimination, and receptor internalization
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Stefan CJ, Blumer KJ. The third cytoplasmic loop of a yeast G-protein-coupled receptor controls pathway activation, ligand discrimination, and receptor internalization. Mol Cell Biol. 14:1994;3339-3349.
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Stefan, C.J.1
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0029900790
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Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled alpha-factor receptor
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Konopka JB, Margarit SM, Dube P. Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled alpha-factor receptor. Proc Natl Acad Sci USA. 93:1996;6764-6769.
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Konopka, J.B.1
Margarit, S.M.2
Dube, P.3
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Regulation of the α-factor receptor by phosphorylation
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Chen Q, Konopka JB. Regulation of the α-factor receptor by phosphorylation. Mol Cell Biol. 16:1996;247-257.
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Mol Cell Biol
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Chen, Q.1
Konopka, J.B.2
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0028860268
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Heterotrimeric G proteins: Organizers of transmembrane signals
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Neer EJ. Heterotrimeric G proteins: organizers of transmembrane signals. Cell. 80:1995;247-257.
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Neer, E.J.1
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9
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0028289437
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Genetic identification of residues involved in association of α and β G-protein subunits
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Whiteway M, Clark KL, Leberer E, Dignard D, Thomas DY. Genetic identification of residues involved in association of α and β G-protein subunits. Mol Cell Biol. 14:1994;3223-3229.
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Mol Cell Biol
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Whiteway, M.1
Clark, K.L.2
Leberer, E.3
Dignard, D.4
Thomas, D.Y.5
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10
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0028840683
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Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway
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Price LA, Kajkowski EM, Hadcock JR, Ozenberger BA, Pausch MH. Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway. Mol Cell Biol. 15:1995;6188-6195.
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Price, L.A.1
Kajkowski, E.M.2
Hadcock, J.R.3
Ozenberger, B.A.4
Pausch, M.H.5
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11
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0029058433
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Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae
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of special interest. Null mutations of the Sst2 gene lead to pheromone hypersensitivity. The authors identify a mutant Sst2 protein which blocks normal signal transduction and use the mutant to map the point of action of Sst2p to the G protein.
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Dohlman HG, Apaniesk D, Chen Y, Song J, Nusskern D. Inhibition of G-protein signaling by dominant gain-of-function mutations in Sst2p, a pheromone desensitization factor in Saccharomyces cerevisiae. of special interest Mol Cell Biol. 15:1996;3635-3643 Null mutations of the Sst2 gene lead to pheromone hypersensitivity. The authors identify a mutant Sst2 protein which blocks normal signal transduction and use the mutant to map the point of action of Sst2p to the G protein.
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(1996)
Mol Cell Biol
, vol.15
, pp. 3635-3643
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Dohlman, H.G.1
Apaniesk, D.2
Chen, Y.3
Song, J.4
Nusskern, D.5
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12
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0030029727
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Inhibition of a G protein-mediated MAP kinase activation by a new mammalian gene family
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of special interest. The authors identify mammalian proteins that can complement the pheromone sensitivity of sst2 mutants, establishing functional as well as structural similarity between the RGS proteins and Sst2p. See also [13].
-
Druey KM, Blumer KJ, Kang VH, Kehri JH. Inhibition of a G protein-mediated MAP kinase activation by a new mammalian gene family. of special interest Nature. 379:1996;742-746 The authors identify mammalian proteins that can complement the pheromone sensitivity of sst2 mutants, establishing functional as well as structural similarity between the RGS proteins and Sst2p. See also [13].
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(1996)
Nature
, vol.379
, pp. 742-746
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Druey, K.M.1
Blumer, K.J.2
Kang, V.H.3
Kehri, J.H.4
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13
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0030087943
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A new family of regulators of G-protein-coupled receptors?
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Siderovski DP, Hessel A, Chung S, Mak TW, Tyers M. A new family of regulators of G-protein-coupled receptors? Curr Biol. 6:1996;211-212.
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Curr Biol
, vol.6
, pp. 211-212
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Siderovski, D.P.1
Hessel, A.2
Chung, S.3
Mak, T.W.4
Tyers, M.5
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14
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0030032001
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Egl-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins
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Koelle MR, Horvitz HR. Egl-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell. 84:1996;115-125.
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(1996)
Cell
, vol.84
, pp. 115-125
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Koelle, M.R.1
Horvitz, H.R.2
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15
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0029559788
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GAIP, a protein that specifically interacts with the trimeric G protein Gα (i3) is a member of a protein family with a highly conserved core domain
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De Vries L, Mousli M, Wurmser A, Farquhar M. GAIP, a protein that specifically interacts with the trimeric G protein Gα (i3) is a member of a protein family with a highly conserved core domain. Proc Natl Acad Sci USA. 92:1995;11916-11920.
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Proc Natl Acad Sci USA
, vol.92
, pp. 11916-11920
-
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De Vries, L.1
Mousli, M.2
Wurmser, A.3
Farquhar, M.4
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16
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0030576518
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GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein α subunits
-
of outstanding interest. This paper provides biochemical evidence that two members of the RGS protein family can act as GAP functions for the alpha subunits of the Gi class of mammalian G proteins. It remains to be established if all the RGS proteins are specific for Gi family members or can act on other G protein classes. The multiplicity of both G alpha subunits and RGS proteins could provide an enormous scope for regulation of signalling pathways.
-
Berman DM, Wilkie TM, Gilman AG. GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein α subunits. of outstanding interest Cell. 86:1996;445-452 This paper provides biochemical evidence that two members of the RGS protein family can act as GAP functions for the alpha subunits of the Gi class of mammalian G proteins. It remains to be established if all the RGS proteins are specific for Gi family members or can act on other G protein classes. The multiplicity of both G alpha subunits and RGS proteins could provide an enormous scope for regulation of signalling pathways.
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(1996)
Cell
, vol.86
, pp. 445-452
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Berman, D.M.1
Wilkie, T.M.2
Gilman, A.G.3
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17
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0027048684
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The protein kinase homologue Ste20p is required to link the yeast pheromone response G-protein βγ subunits to downstream signalling components
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Leberer E, Dignard D, Harcus D, Thomas DY, Whiteway M. The protein kinase homologue Ste20p is required to link the yeast pheromone response G-protein βγ subunits to downstream signalling components. EMBO J. 11:1992;4815-4824.
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(1992)
EMBO J
, vol.11
, pp. 4815-4824
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Leberer, E.1
Dignard, D.2
Harcus, D.3
Thomas, D.Y.4
Whiteway, M.5
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18
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0029960339
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Genetic relationships between the G protein βγ complex, Ste5p, Ste20p and Cdc42p: Investigation of effector roles in the yeast pheromone response pathway
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Akada R, Kallal L, Johnson DI, Kurjan J. Genetic relationships between the G protein βγ complex, Ste5p, Ste20p and Cdc42p: investigation of effector roles in the yeast pheromone response pathway. Genetics. 143:1996;103-117.
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(1996)
Genetics
, vol.143
, pp. 103-117
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Akada, R.1
Kallal, L.2
Johnson, D.I.3
Kurjan, J.4
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19
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0029012079
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Ste5: A meeting place for MAP kinases and their associates
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Elion EA. Ste5: a meeting place for MAP kinases and their associates. Trends Cell Biol. 5:1995;322-327.
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(1995)
Trends Cell Biol
, vol.5
, pp. 322-327
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Elion, E.A.1
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20
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0028884447
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Pheromone response in yeast: Association of Bem1p with proteins of the MAP kinase cascade and actin
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of special interest. This study describes a large pheromone signalling complex associated with actin. The interaction of Bem1p with Ste20p and Ste5p and its association with actin is demonstrated. Mutants of Bem1p which are defective in the cytoskeletal response towards the mating partner are defective for interaction with Ste20p, suggesting that Bem1p may link the signalling complex to the cytoskeleton.
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Leeuw T, Fourest A, Wu C, Chenevert J, Clark K, Whiteway M, Thomas DY, Leberer E. Pheromone response in yeast: association of Bem1p with proteins of the MAP kinase cascade and actin. of special interest Science. 270:1995;1210-1213 This study describes a large pheromone signalling complex associated with actin. The interaction of Bem1p with Ste20p and Ste5p and its association with actin is demonstrated. Mutants of Bem1p which are defective in the cytoskeletal response towards the mating partner are defective for interaction with Ste20p, suggesting that Bem1p may link the signalling complex to the cytoskeleton.
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(1995)
Science
, vol.270
, pp. 1210-1213
-
-
Leeuw, T.1
Fourest, A.2
Wu, C.3
Chenevert, J.4
Clark, K.5
Whiteway, M.6
Thomas, D.Y.7
Leberer, E.8
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21
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0029146796
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Association of the yeast pheromone response G protein βγ subunits with the MAP kinase scaffold Ste5p
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of special interest. This work establishes a physical association between the G protein βγ subunit and Ste5p. This provides a connection between the G protein and the MAP kinase cascade members, and suggests that Ste5p may play more than just a scaffolding function in the pheromone response.
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Whiteway MS, Wu C, Leeuw T, Clark K, Fourest A, Thomas DY, Leberer E. Association of the yeast pheromone response G protein βγ subunits with the MAP kinase scaffold Ste5p. of special interest Science. 269:1995;1572-1575 This work establishes a physical association between the G protein βγ subunit and Ste5p. This provides a connection between the G protein and the MAP kinase cascade members, and suggests that Ste5p may play more than just a scaffolding function in the pheromone response.
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(1995)
Science
, vol.269
, pp. 1572-1575
-
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Whiteway, M.S.1
Wu, C.2
Leeuw, T.3
Clark, K.4
Fourest, A.5
Thomas, D.Y.6
Leberer, E.7
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22
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0028863672
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Truncated forms of a novel yeast protein suppress the lethality of a G protein α subunit deficiency by interacting with the β subunit
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Spain B, Koo D, Ramakrishnan M, Dzudzor B, Colicelli J. Truncated forms of a novel yeast protein suppress the lethality of a G protein α subunit deficiency by interacting with the β subunit. J Biol Chem. 270:1995;25435-25444.
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(1995)
J Biol Chem
, vol.270
, pp. 25435-25444
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Spain, B.1
Koo, D.2
Ramakrishnan, M.3
Dzudzor, B.4
Colicelli, J.5
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23
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0029655984
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Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae
-
of special interest. See annotation [24].
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Kao L-R, Peterson J, Ji R, Bender L, Bender A. Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae. of special interest Mol Cell Biol. 16:1996;168-178 See annotation [24].
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(1996)
Mol Cell Biol
, vol.16
, pp. 168-178
-
-
Kao, L.-R.1
Peterson, J.2
Ji, R.3
Bender, L.4
Bender, A.5
-
24
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0029954765
-
AKR1 encodes a candidate effector of the Gβγ complex in the Saccharomyces cerevisiae pheromone response pathway and contributes to control of both cell shape and signal transduction
-
of special interest. Together with [24] identifies the Akr1 product. Akr1p acts in both the pheromone response pathway as a negative element as well as in the regulation of cell shape. As Akr1p was identified as a synthetic lethal with Bem1p, it is possible that Akr1p is part of a Bem1-containing complex involved in the control of morphology.
-
Pryciak P, Hartwell LH. AKR1 encodes a candidate effector of the Gβγ complex in the Saccharomyces cerevisiae pheromone response pathway and contributes to control of both cell shape and signal transduction. of special interest Mol Cell Biol. 16:1996;2614-2626 Together with [24] identifies the Akr1 product. Akr1p acts in both the pheromone response pathway as a negative element as well as in the regulation of cell shape. As Akr1p was identified as a synthetic lethal with Bem1p, it is possible that Akr1p is part of a Bem1-containing complex involved in the control of morphology.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 2614-2626
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-
Pryciak, P.1
Hartwell, L.H.2
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25
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0029999863
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Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae
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Xu G, Jansen G, Thomas DY, Hollenberg CP, Ramezani Rad M. Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae. Mol Microbiol. 20:1996;773-783.
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(1996)
Mol Microbiol
, vol.20
, pp. 773-783
-
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Xu, G.1
Jansen, G.2
Thomas, D.Y.3
Hollenberg, C.P.4
Ramezani Rad, M.5
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26
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0028786020
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A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
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of special interest. Putative effector proteins for Cdc42 and Rac are identified by screening a protein data base with the Cdc42 and Rac binding motif of PAK. Cdc42/Rac binding is confirmed biochemically for several of the identified proteins using a filter-binding assay.
-
Burbelo PD, Drechsel D, Hall A. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. of special interest J Biol Chem. 270:1995;29071-29074 Putative effector proteins for Cdc42 and Rac are identified by screening a protein data base with the Cdc42 and Rac binding motif of PAK. Cdc42/Rac binding is confirmed biochemically for several of the identified proteins using a filter-binding assay.
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(1995)
J Biol Chem
, vol.270
, pp. 29071-29074
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Burbelo, P.D.1
Drechsel, D.2
Hall, A.3
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27
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0030021649
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Signal transduction and actin filament organization
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Zigmond SH. Signal transduction and actin filament organization. Curr Opin Cell Biol. 8:1996;66-73.
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(1996)
Curr Opin Cell Biol
, vol.8
, pp. 66-73
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Zigmond, S.H.1
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28
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0030198344
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Protein kinase cascades activated by stress and inflammatory cytokines
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Kyriakis JM, Avruch J. Protein kinase cascades activated by stress and inflammatory cytokines. BioEssays. 18:1996;567-577.
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(1996)
BioEssays
, vol.18
, pp. 567-577
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Kyriakis, J.M.1
Avruch, J.2
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29
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0030222309
-
Generation of cell polarity in yeast
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of special interest. This paper is an excellent review of the role of BUD gene products in bud site selection and the orientation of the budding axis, and of the polarity establishment gene products Cdc42p, Cdc24p, and Bem1p in the formation of buds.
-
Chant J. Generation of cell polarity in yeast. of special interest Curr Opin Cell Biol. 8:1996;557-565 This paper is an excellent review of the role of BUD gene products in bud site selection and the orientation of the budding axis, and of the polarity establishment gene products Cdc42p, Cdc24p, and Bem1p in the formation of buds.
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(1996)
Curr Opin Cell Biol
, vol.8
, pp. 557-565
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Chant, J.1
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30
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0025847665
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Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity
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Ziman FJM, O'Brien M, Ouellette LA, Church WR, Johnson DI. Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity. Mol Cell Biol. 11:1991;3537-3544.
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(1991)
Mol Cell Biol
, vol.11
, pp. 3537-3544
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Ziman, F.J.M.1
O'Brien, M.2
Ouellette, L.A.3
Church, W.R.4
Johnson, D.I.5
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31
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0029157469
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Role for the Rho-family GTPase Cdc42 in yeast mating-pheromone signal pathway
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Simon M-N, De Virgilio C, Souza B, Pringle JR, Abo A, Reed SI. Role for the Rho-family GTPase Cdc42 in yeast mating-pheromone signal pathway. Nature. 376:1995;702-705.
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(1995)
Nature
, vol.376
, pp. 702-705
-
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Simon, M.-N.1
De Virgilio, C.2
Souza, B.3
Pringle, J.R.4
Abo, A.5
Reed, S.I.6
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32
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0029118202
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Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24
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Zhao Z-S, Leung T, Manser E, Lim L. Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24. Mol Cell Biol. 15:1995;5246-5257.
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(1995)
Mol Cell Biol
, vol.15
, pp. 5246-5257
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Zhao, Z.-S.1
Leung, T.2
Manser, E.3
Lim, L.4
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33
-
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0031015562
-
Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase
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of outstanding interest. See annotation [34].
-
Leberer E, Wu C, Leeuw T, Fourest-Lieuvin A, Segall JE, Thomas DY. Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase. of outstanding interest EMBO J. 16:1997;83-97 See annotation [34].
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(1997)
EMBO J
, vol.16
, pp. 83-97
-
-
Leberer, E.1
Wu, C.2
Leeuw, T.3
Fourest-Lieuvin, A.4
Segall, J.E.5
Thomas, D.Y.6
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34
-
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0030465534
-
Functional analysis of the interaction between the small GTP-binding protein Cdc42 and the Ste20 protein kinase in yeast
-
of outstanding interest. This work shows, together with [33], that physical interaction between Cdc42p and Ste20p is not required for pheromone signal transduction but plays a role in cell - cell adhesion during mating and is needed to induce morphological switching in response to nitrogen starvation. Cdc42p binding to Ste20p is also essential for budding in the absence of Cla4p. Fusions with green fluorescent protein demonstrate that the Cdc42p binding site of Ste20p plays a role in directing Ste20p to regions of polarized growth during budding and mating.
-
Peter M, Neiman A, Park H-O, Van Lohuizen M, Herskowitz I. Functional analysis of the interaction between the small GTP-binding protein Cdc42 and the Ste20 protein kinase in yeast. of outstanding interest EMBO J. 15:1996;7046-7059 This work shows, together with [33], that physical interaction between Cdc42p and Ste20p is not required for pheromone signal transduction but plays a role in cell - cell adhesion during mating and is needed to induce morphological switching in response to nitrogen starvation. Cdc42p binding to Ste20p is also essential for budding in the absence of Cla4p. Fusions with green fluorescent protein demonstrate that the Cdc42p binding site of Ste20p plays a role in directing Ste20p to regions of polarized growth during budding and mating.
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(1996)
EMBO J
, vol.15
, pp. 7046-7059
-
-
Peter, M.1
Neiman, A.2
Park, H.-O.3
Van Lohuizen, M.4
Herskowitz, I.5
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35
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0028867027
-
Mutation of RGA1, which encodes a putative GTPase-activating protein for the polarity-establishment protein Cdc42p, activates the pheromone-response pathway in the yeast Saccharomyces cerevisiae
-
Stevenson BJ, Ferguson B, De Virgilio C, Bi E, Pringle JR, Ammerer G, Sprague GF Jr. Mutation of RGA1, which encodes a putative GTPase-activating protein for the polarity-establishment protein Cdc42p, activates the pheromone-response pathway in the yeast Saccharomyces cerevisiae. Genes Dev. 9:1995;2949-2963.
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(1995)
Genes Dev
, vol.9
, pp. 2949-2963
-
-
Stevenson, B.J.1
Ferguson, B.2
De Virgilio, C.3
Bi, E.4
Pringle, J.R.5
Ammerer, G.6
Sprague G.F., Jr.7
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36
-
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0029066439
-
Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae
-
of special interest. The authors describe a biochemical characterization of Ste20p and identify Ste11p as an in vitro substrate of Ste20p. Ste20p may thus act as a MEK kinase kinase to activate a conserved MAP kinase cascade.
-
Wu C, Whiteway M, Thomas DY, Leberer E. Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae. of special interest J Biol Chem. 270:1995;15984-15992 The authors describe a biochemical characterization of Ste20p and identify Ste11p as an in vitro substrate of Ste20p. Ste20p may thus act as a MEK kinase kinase to activate a conserved MAP kinase cascade.
-
(1995)
J Biol Chem
, vol.270
, pp. 15984-15992
-
-
Wu, C.1
Whiteway, M.2
Thomas, D.Y.3
Leberer, E.4
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37
-
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0029857110
-
Genetic interactions indicate a role for Mdg1p and SH3 domain protein Bem1p in linking the G-protein mediated yeast pheromone signalling pathway to regulators of cell polarity
-
Leberer E, Chenevert J, Leeuw T, Harcus D, Herskowitz I, Thomas DY. Genetic interactions indicate a role for Mdg1p and SH3 domain protein Bem1p in linking the G-protein mediated yeast pheromone signalling pathway to regulators of cell polarity. Mol Gen Genet. 252:1996;608-621.
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(1996)
Mol Gen Genet
, vol.252
, pp. 608-621
-
-
Leberer, E.1
Chenevert, J.2
Leeuw, T.3
Harcus, D.4
Herskowitz, I.5
Thomas, D.Y.6
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38
-
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0029091498
-
Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast
-
of outstanding interest. This work shows that Cla4p binds Cdc42p and has homology to Ste20p. Cla4p shares functional redundancy with Ste20p in cell polarization during budding.
-
Cvrckova F, De Virgilio C, Manser E, Pringle JR, Nasmyth K. Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. of outstanding interest Genes Dev. 9:1995;1817-1830 This work shows that Cla4p binds Cdc42p and has homology to Ste20p. Cla4p shares functional redundancy with Ste20p in cell polarization during budding.
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(1995)
Genes Dev
, vol.9
, pp. 1817-1830
-
-
Cvrckova, F.1
De Virgilio, C.2
Manser, E.3
Pringle, J.R.4
Nasmyth, K.5
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39
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0026588787
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Unipolar cell divisions in the yeast S. cerevisiae lead to filamentous growth: Regulation by starvation and Ras
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Gimeno CJ, Ljungdahl PO, Styles CA, Fink GR. Unipolar cell divisions in the yeast S. cerevisiae lead to filamentous growth: regulation by starvation and Ras. Cell. 68:1992;1077-1090.
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Elements of a single MAP kinase cascade in Saccharomyces cerevisiae mediate two developmental programs in the same cell type: Mating and invasive growth
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Roberts RL, Fink GR. Elements of a single MAP kinase cascade in Saccharomyces cerevisiae mediate two developmental programs in the same cell type: mating and invasive growth. Genes Dev. 8:1994;2974-2985.
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Elements of the yeast pheromone response pathway required for filamentous growth of diploids
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Liu H, Styles C, Fink GR. Elements of the yeast pheromone response pathway required for filamentous growth of diploids. Science. 262:1993;1741-1744.
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Yeast MEK-dependent signal transduction: Response thresholds and parameters affecting fidelity
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Yashar B, Irie K, Printen JA, Stevenson BJ, Sprague GF Jr, Matsumoto K, Errede B. Yeast MEK-dependent signal transduction: response thresholds and parameters affecting fidelity. Mol Cell Biol. 15:1995;6545-6553.
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Yashar, B.1
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43
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0029895340
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Ras2 signals via the Cdc42/Ste20/mitogen-activated protein kinase module to induce filamentous growth in Saccharomyces cerevisiae
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of outstanding interest. Cdc42p acts upstream of Ste20p and downstream of Ras2p in the pseudohyphal MAP kinase pathway. Specificity of this signalling pathway is demonstrated by using FUS1 and Ty1 reporter genes. This study demonstrates for the first time that an H-Ras homolog of yeast is involved in the activation of a conserved MAP kinase cascade.
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Mösch H-U, Roberts RL, Fink GR. Ras2 signals via the Cdc42/Ste20/mitogen-activated protein kinase module to induce filamentous growth in Saccharomyces cerevisiae. of outstanding interest Proc Natl Acad Sci USA. 93:1996;5352-5356 Cdc42p acts upstream of Ste20p and downstream of Ras2p in the pseudohyphal MAP kinase pathway. Specificity of this signalling pathway is demonstrated by using FUS1 and Ty1 reporter genes. This study demonstrates for the first time that an H-Ras homolog of yeast is involved in the activation of a conserved MAP kinase cascade.
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Proc Natl Acad Sci USA
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Mösch, H.-U.1
Roberts, R.L.2
Fink, G.R.3
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44
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0029070887
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Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
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Minden A, Lin A, Claret F-X, Abo A, Karin M. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell. 81:1995;1147-1157.
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Minden, A.1
Lin, A.2
Claret, F.-X.3
Abo, A.4
Karin, M.5
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45
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0029055812
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The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
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Coso OA, Chiariello M, Yu J-C, Teramoto H, Crespo P, Xu N, Miki T, Gutkind S. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell. 81:1995;1137-1146.
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Coso, O.A.1
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Miki, T.7
Gutkind, S.8
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0026052120
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S. cerevisiae α-pheromone receptors activate a novel signal transduction pathway for mating partner discrimination.
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Jackson CL, Konopka JB, Hartwell LH. S. cerevisiae α-pheromone receptors activate a novel signal transduction pathway for mating partner discrimination. Cell. 67:1991;389-402.
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Jackson, C.L.1
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Polarization of yeast cells in spatial gradients of α-mating factor
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Segall JE. Polarization of yeast cells in spatial gradients of α-mating factor. Proc Natl Acad Sci USA. 90:1993;8332-8336.
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Segall, J.E.1
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48
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0028805208
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Saccharomyces cerevisiae cells execute a default pathway to select a mate in the absence of pheromone gradients
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of special interest. See annotation [49].
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Dorer R, Pryciak PM, Hartwell LH. Saccharomyces cerevisiae cells execute a default pathway to select a mate in the absence of pheromone gradients. of special interest J Cell Biol. 131:1995;845-861 See annotation [49].
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Dorer, R.1
Pryciak, P.M.2
Hartwell, L.H.3
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49
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0028889717
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FAR1 is required for oriented polarization of yeast cells in response to mating pheromones
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of special interest. Far1p, identified previously as a negative regulator of cyclin/Cdc28p kinase, is shown to have a role in polarizing a projection towards the mating partner; Far1p, thus, has multiple roles in cell cycle regulation and polarized morphogenesis.
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Valtz N, Peter M, Herskowitz I. FAR1 is required for oriented polarization of yeast cells in response to mating pheromones. of special interest J Cell Biol. 131:1995;863-873 Far1p, identified previously as a negative regulator of cyclin/Cdc28p kinase, is shown to have a role in polarizing a projection towards the mating partner; Far1p, thus, has multiple roles in cell cycle regulation and polarized morphogenesis.
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Valtz, N.1
Peter, M.2
Herskowitz, I.3
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50
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The SPA2 genes of Saccharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating
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Gehrung S, Snyder M. The SPA2 genes of Saccharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating. J Cell Biol. 111:1990;1451-1464.
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51
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0029892972
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The SH3-domain protein Bem1 coordinates mitogen-activated protein kinase cascade activation with cell cycle control in Saccharomyces cerevisiae
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Lyons DM, Mahanty SK, Choi K-Y, Manandhar M, Elion EA. The SH3-domain protein Bem1 coordinates mitogen-activated protein kinase cascade activation with cell cycle control in Saccharomyces cerevisiae. Mol Cell Biol. 16:1996;4095-4106.
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Elion, E.A.5
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52
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Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast
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Peterson J, Zheng Y, Bender L, Myers A, Cerione R, Bender A. Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast. J Cell Biol. 127:1994;1395-1406.
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Peterson, J.1
Zheng, Y.2
Bender, L.3
Myers, A.4
Cerione, R.5
Bender, A.6
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53
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0028871169
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Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast
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Li R, Zheng Y, Drubin DG. Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. J Cell Biol. 128:1995;599-615.
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Li, R.1
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0030026017
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The SLT2 (MPK1) MAP kinase is activated during periods of polarized cell growth in yeast
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Zarzov P, Mazzoni C, Mann C. The SLT2 (MPK1) MAP kinase is activated during periods of polarized cell growth in yeast. EMBO J. 15:1996;83-91.
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0027494567
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AFR1 acts in conjunction with the α-factor receptor to promote morphogenesis and adaptation
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Konopka JB. AFR1 acts in conjunction with the α-factor receptor to promote morphogenesis and adaptation. Mol Cell Biol. 13:1993;6876-6888.
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Konopka, J.B.1
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56
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0028872312
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AFR1 promotes polarized apical morphogenesis in Saccharomyces cerevisiae
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Konopka JB, DeMattei C, Davis C. AFR1 promotes polarized apical morphogenesis in Saccharomyces cerevisiae. Mol Cell Biol. 15:1995;723-730.
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Konopka, J.B.1
Demattei, C.2
Davis, C.3
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57
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0029923034
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Role of type I myosins in receptor-mediated endocytosis in yeast
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of special interest. This study demonstrates that Myo5p, an unconventional myosin-l isoform, is required for yeast pheromone receptor endocytosis. This provides the first genetic evidence for a defined function of a myosin-l isoform.
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Geli MI, Riezman H. Role of type I myosins in receptor-mediated endocytosis in yeast. of special interest Science. 272:1996;533-535 This study demonstrates that Myo5p, an unconventional myosin-l isoform, is required for yeast pheromone receptor endocytosis. This provides the first genetic evidence for a defined function of a myosin-l isoform.
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Science
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Geli, M.I.1
Riezman, H.2
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58
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0029910216
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Cloning and characterization of a Dictyostelium myosin l heavy chain kinase activated by Cdc42 and Rac
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2+-ATPase activity of myosin-ID. This study provides the first evidence for a potential dual role of members of the Ste20p/PAK family in stimulating transcriptional activation of genes by MAP kinase cascades and inducing morphogenetic processes through direct stimulation of myosin-l.
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2+-ATPase activity of myosin-ID. This study provides the first evidence for a potential dual role of members of the Ste20p/PAK family in stimulating transcriptional activation of genes by MAP kinase cascades and inducing morphogenetic processes through direct stimulation of myosin-l.
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(1996)
J Biol Chem
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Lee, S.-F.1
Egelhoff, T.T.2
Mahasneh, A.3
Côté, G.P.4
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59
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0029984773
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Synthetic lethality screen identifies a novel yeast myosin l gene (MYO5): Myosin l proteins are required for polarization of the actin cytoskeleton
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of special interest. This paper demonstrates that the unconventional myosin-l isoforms Myo3p and Myo5p share overlapping functions required for polarization of the yeast actin cytoskeleton during yeast budding. This suggests that morphological processes driven by myosin-l may contribute to polarized growth during cellular division.
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Goodson HV, Anderson BL, Warrick HM, Pon LA, Spudich JA. Synthetic lethality screen identifies a novel yeast myosin l gene (MYO5): myosin l proteins are required for polarization of the actin cytoskeleton. of special interest J Cell Biol. 133:1996;1277-1291 This paper demonstrates that the unconventional myosin-l isoforms Myo3p and Myo5p share overlapping functions required for polarization of the yeast actin cytoskeleton during yeast budding. This suggests that morphological processes driven by myosin-l may contribute to polarized growth during cellular division.
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(1996)
J Cell Biol
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Goodson, H.V.1
Anderson, B.L.2
Warrick, H.M.3
Pon, L.A.4
Spudich, J.A.5
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60
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10544236114
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Activation of myosin l by members of the Step20 protein kinase family
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Wu C, Lee S-F, Furmaniak-Kazmierczak E, Côté GP, Thomas DY, Leberer E. Activation of myosin l by members of the Step20 protein kinase family. J Biol Chem. 271:1996;31787-31790.
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J Biol Chem
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Wu, C.1
Lee, S.-F.2
Furmaniak-Kazmierczak, E.3
Côté, G.P.4
Thomas, D.Y.5
Leberer, E.6
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