Tran NH, et al. (2021) The stress-sensing domain of activated IRE1α forms helical filaments in narrow ER membrane tubes. Science 374(6563):52-57 PMID:34591618
Göke A, et al. (2020) Mrx6 regulates mitochondrial DNA copy number in Saccharomyces cerevisiae by engaging the evolutionarily conserved Lon protease Pim1. Mol Biol Cell 31(7):527-545 PMID:31532710
Wang L and Walter P (2020) Msp1/ATAD1 in Protein Quality Control and Regulation of Synaptic Activities. Annu Rev Cell Dev Biol 36:141-164 PMID:32886535
Peschek J and Walter P (2019) tRNA ligase structure reveals kinetic competition between non-conventional mRNA splicing and mRNA decay. Elife 8 PMID:31237564
Cohen N, et al. (2017) Iron affects Ire1 clustering propensity and the amplitude of endoplasmic reticulum stress signaling. J Cell Sci 130(19):3222-3233 PMID:28794014
Lang AB, et al. (2015) ER-mitochondrial junctions can be bypassed by dominant mutations in the endosomal protein Vps13. J Cell Biol 210(6):883-90 PMID:26370498
Osman C, et al. (2015) Integrity of the yeast mitochondrial genome, but not its distribution and inheritance, relies on mitochondrial fission and fusion. Proc Natl Acad Sci U S A 112(9):E947-56 PMID:25730886
Okreglak V and Walter P (2014) The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins. Proc Natl Acad Sci U S A 111(22):8019-24 PMID:24821790
van Anken E, et al. (2014) Specificity in endoplasmic reticulum-stress signaling in yeast entails a step-wise engagement of HAC1 mRNA to clusters of the stress sensor Ire1. Elife 3:e05031 PMID:25549299
Gardner BM, et al. (2013) Endoplasmic reticulum stress sensing in the unfolded protein response. Cold Spring Harb Perspect Biol 5(3):a013169 PMID:23388626
Murley A, et al. (2013) ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast. Elife 2:e00422 PMID:23682313
Gardner BM and Walter P (2011) Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333(6051):1891-4 PMID:21852455
Kornmann B, et al. (2011) The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections. Proc Natl Acad Sci U S A 108(34):14151-6 PMID:21825164
Aguilar PS, et al. (2010) Structure of sterol aliphatic chains affects yeast cell shape and cell fusion during mating. Proc Natl Acad Sci U S A 107(9):4170-5 PMID:20150508
Aguilar PS, et al. (2010) A plasma-membrane E-MAP reveals links of the eisosome with sphingolipid metabolism and endosomal trafficking. Nat Struct Mol Biol 17(7):901-8 PMID:20526336
Engel A, et al. (2010) The yeast cell fusion protein Prm1p requires covalent dimerization to promote membrane fusion. PLoS One 5(5):e10593 PMID:20485669
Kornmann B and Walter P (2010) ERMES-mediated ER-mitochondria contacts: molecular hubs for the regulation of mitochondrial biology. J Cell Sci 123(Pt 9):1389-93 PMID:20410371
Pincus D, et al. (2010) BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response. PLoS Biol 8(7):e1000415 PMID:20625545
Fröhlich F, et al. (2009) A genome-wide screen for genes affecting eisosomes reveals Nce102 function in sphingolipid signaling. J Cell Biol 185(7):1227-42 PMID:19564405
Jonikas MC, et al. (2009) Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323(5922):1693-7 PMID:19325107
Engel A and Walter P (2008) Membrane lysis during biological membrane fusion: collateral damage by misregulated fusion machines. J Cell Biol 183(2):181-6 PMID:18852300
Aguilar PS, et al. (2007) The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane fusion during yeast mating. Mol Biol Cell 18(2):547-56 PMID:17151357
Haass FA, et al. (2007) Identification of yeast proteins necessary for cell-surface function of a potassium channel. Proc Natl Acad Sci U S A 104(46):18079-84 PMID:17989219
Heiman MG, et al. (2007) The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating. J Cell Biol 176(2):209-22 PMID:17210951
Bernales S, et al. (2006) Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol 4(12):e423 PMID:17132049
Credle JJ, et al. (2005) On the mechanism of sensing unfolded protein in the endoplasmic reticulum. Proc Natl Acad Sci U S A 102(52):18773-84 PMID:16365312
Niwa M, et al. (2005) Genome-scale approaches for discovering novel nonconventional splicing substrates of the Ire1 nuclease. Genome Biol 6(1):R3 PMID:15642095
Patil CK, et al. (2004) Gcn4p and novel upstream activating sequences regulate targets of the unfolded protein response. PLoS Biol 2(8):E246 PMID:15314660
Helenius J, et al. (2002) Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein. Nature 415(6870):447-50 PMID:11807558
Mutka SC and Walter P (2001) Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway. Mol Biol Cell 12(3):577-88 PMID:11251072
Nock S, et al. (2001) Purification and activity assays of the catalytic domains of the kinase/endoribonuclease Ire1p from Saccharomyces cerevisiae. Methods Enzymol 342:3-10 PMID:11586903
Patil C and Walter P (2001) Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13(3):349-55 PMID:11343907
Rüegsegger U, et al. (2001) Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Cell 107(1):103-14 PMID:11595189
Senger B, et al. (2001) Yeast cytoplasmic and mitochondrial methionyl-tRNA synthetases: two structural frameworks for identical functions. J Mol Biol 311(1):205-16 PMID:11469869
Heiman MG and Walter P (2000) Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating. J Cell Biol 151(3):719-30 PMID:11062271
Ng DT, et al. (2000) The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J Cell Biol 150(1):77-88 PMID:10893258
Travers KJ, et al. (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101(3):249-58 PMID:10847680
Barz WP and Walter P (1999) Two endoplasmic reticulum (ER) membrane proteins that facilitate ER-to-Golgi transport of glycosylphosphatidylinositol-anchored proteins. Mol Biol Cell 10(4):1043-59 PMID:10198056
Freymann DM, et al. (1999) Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP. Nat Struct Biol 6(8):793-801 PMID:10426959
Niwa M, et al. (1999) A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell 99(7):691-702 PMID:10619423
Powers T and Walter P (1999) Regulation of ribosome biogenesis by the rapamycin-sensitive TOR-signaling pathway in Saccharomyces cerevisiae. Mol Biol Cell 10(4):987-1000 PMID:10198052
Ogg SC, et al. (1998) A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit. J Cell Biol 142(2):341-54 PMID:9679135
Cox JS, et al. (1997) The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol Biol Cell 8(9):1805-14 PMID:9307975
Nunnari J, et al. (1997) Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol Biol Cell 8(7):1233-42 PMID:9243504
Sidrauski C and Walter P (1997) The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90(6):1031-9 PMID:9323131
Aphasizhev R, et al. (1996) Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site. Biochemistry 35(1):117-23 PMID:8555164
Cox JS and Walter P (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87(3):391-404 PMID:8898193
Shamu CE and Walter P (1996) Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J 15(12):3028-39 PMID:8670804
Miller JD, et al. (1995) The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane. J Cell Biol 128(3):273-82 PMID:7844142
Ogg SC and Walter P (1995) SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation. Cell 81(7):1075-84 PMID:7600575
Senger B, et al. (1995) The presence of a D-stem but not a T-stem is essential for triggering aminoacylation upon anticodon binding in yeast methionine tRNA. J Mol Biol 249(1):45-58 PMID:7776375
Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400 PMID:7925282
Vettese-Dadey M, et al. (1994) Role of the histone amino termini in facilitated binding of a transcription factor, GAL4-AH, to nucleosome cores. Mol Cell Biol 14(2):970-81 PMID:8289837
Nunnari J, et al. (1993) A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262(5142):1997-2004 PMID:8266095
Despons L, et al. (1992) Binding of the yeast tRNA(Met) anticodon by the cognate methionyl-tRNA synthetase involves at least two independent peptide regions. J Mol Biol 225(3):897-907 PMID:1602489
Green N, et al. (1992) Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. J Cell Biol 116(3):597-604 PMID:1730771
Hann BC, et al. (1992) SEC65 gene product is a subunit of the yeast signal recognition particle required for its integrity. Nature 356(6369):532-3 PMID:1313947
Nunnari J and Walter P (1992) Protein targeting to and translocation across the membrane of the endoplasmic reticulum. Curr Opin Cell Biol 4(4):573-80 PMID:1419037
Ogg SC, et al. (1992) Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae. Mol Biol Cell 3(8):895-911 PMID:1327299
Sanni A, et al. (1991) Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase. Proc Natl Acad Sci U S A 88(19):8387-91 PMID:1924298
Zopf D, et al. (1990) The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J 9(13):4511-7 PMID:1702385
Green GN, et al. (1989) The use of gene-fusions to determine membrane protein topology in Saccharomyces cerevisiae. J Cell Sci Suppl 11:109-13 PMID:2693456
Hann BC, et al. (1989) Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth. J Cell Biol 109(6 Pt 2):3223-30 PMID:2557350
Ngsee JK, et al. (1989) Cassette mutagenic analysis of the yeast invertase signal peptide: effects on protein translocation. Mol Cell Biol 9(8):3400-10 PMID:2677671
Strub K and Walter P (1989) Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactions. Proc Natl Acad Sci U S A 86(24):9747-51 PMID:2557625
Walter P, et al. (1989) Deletion analysis in the amino-terminal extension of methionyl-tRNA synthetase from Saccharomyces cerevisiae shows that a small region is important for the activity and stability of the enzyme. J Biol Chem 264(29):17126-30 PMID:2677000
Hansen W and Walter P (1988) Prepro-carboxypeptidase Y and a truncated form of pre-invertase, but not full-length pre-invertase, can be posttranslationally translocated across microsomal vesicle membranes from Saccharomyces cerevisiae. J Cell Biol 106(4):1075-81 PMID:3283144
Fasiolo F, et al. (1985) Cytoplasmic methionyl-tRNA synthetase from Bakers' yeast. A monomer with a post-translationally modified N terminus. J Biol Chem 260(29):15571-6 PMID:3905796
Walter P, et al. (1983) Primary structure of the Saccharomyces cerevisiae gene for methionyl-tRNA synthetase. Proc Natl Acad Sci U S A 80(9):2437-41 PMID:6341994