Genomes and Genes
Gene Symbol: SLN1
Alias: YPD2, Sln1p
Species: Saccharomyces cerevisiae S288c
- Escote X, Zapater M, Clotet J, Posas F. Hog1 mediates cell-cycle arrest in G1 phase by the dual targeting of Sic1. Nat Cell Biol. 2004;6:997-1002 pubmed..Together, our data indicate that the Sic1 CDK-inhibitor is the molecular target for the SAPK Hog1 that is required to modulate cell-cycle progression in response to stress. ..
- Vendrell A, Martínez Pastor M, Gonzalez Novo A, Pascual Ahuir A, Sinclair D, Proft M, et al. Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase. EMBO Rep. 2011;12:1062-8 pubmed publisher..Sir2 is involved in protection against Hog1-induced cell death and can suppress Hog1-induced ROS accumulation. Therefore, cell death seems to be dictated by the balance of ROS induced by Hog1 and the protective effect of Sir2. ..
- Reiser V, Raitt D, Saito H. Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure. J Cell Biol. 2003;161:1035-40 pubmed..Here, we report that in yeast, Sln1 osmosensor histidine kinase monitors changes in turgor pressures...
- Janiak Spens F, Sparling D, West A. Novel role for an HPt domain in stabilizing the phosphorylated state of a response regulator domain. J Bacteriol. 2000;182:6673-8 pubmed..In Saccharomyces cerevisiae, the YPD1 protein facilitates phosphoryl transfer from a hybrid sensor kinase, SLN1, to two distinct response regulator proteins, SSK1 and SKN7...
- Santos B, Snyder M. Sbe2p and sbe22p, two homologous Golgi proteins involved in yeast cell wall formation. Mol Biol Cell. 2000;11:435-52 pubmed..Thus, we suggest a model in which Sbe2p and Sbe22p are involved in the transport of cell wall components from the Golgi apparatus to the cell surface periphery in a pathway independent of Chs5p. ..
- Mizuno T, Masuda Y, Irie K. The Saccharomyces cerevisiae AMPK, Snf1, Negatively Regulates the Hog1 MAPK Pathway in ER Stress Response. PLoS Genet. 2015;11:e1005491 pubmed publisher..Thus, Snf1 plays pleiotropic roles in ER stress response by negatively regulating the Hog1 MAPK pathway and the UPR pathway. ..
- Hiramoto F, Nomura N, Furumai T, Igarashi Y, Oki T. Pradimicin resistance of yeast is caused by a mutation of the putative N-glycosylation sites of osmosensor protein Sln1. Biosci Biotechnol Biochem. 2005;69:238-41 pubmed..In this study, the involvement of a membrane-spanning osomosensor, Sln1, which is located upstream of Ypd1, was investigated...
- Horie T, Tatebayashi K, Yamada R, Saito H. Phosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway. Mol Cell Biol. 2008;28:5172-83 pubmed publisher..Ssk1 (Ssk1-OH) is the active form and that Ssk1 phosphorylated (Ssk1 approximately P) at Asp554 by the Sln1-Ypd1-Ssk1 multistep phosphorelay mechanism is the inactive form...
- Janiak Spens F, Sparling J, Gurfinkel M, West A. Differential stabilities of phosphorylated response regulator domains reflect functional roles of the yeast osmoregulatory SLN1 and SSK1 proteins. J Bacteriol. 1999;181:411-7 pubmedOsmoregulation in Saccharomyces cerevisiae involves a multistep phosphorelay system requiring three proteins, SLN1, YPD1, and SSK1, that are related to bacterial two-component signaling proteins, in particular, those involved in ..
- Dexter J, Xu P, Gunawardena J, McClean M. Robust network structure of the Sln1-Ypd1-Ssk1 three-component phospho-relay prevents unintended activation of the HOG MAPK pathway in Saccharomyces cerevisiae. BMC Syst Biol. 2015;9:17 pubmed publisher..Under normal growth conditions, however, a three-component phospho-relay consisting of the histidine kinase Sln1, the transfer protein Ypd1, and the response regulator Ssk1 represses HOG pathway activity by phosphorylation of ..
- Janiak Spens F, Cook P, West A. Kinetic analysis of YPD1-dependent phosphotransfer reactions in the yeast osmoregulatory phosphorelay system. Biochemistry. 2005;44:377-86 pubmed..HPt) protein YPD1 transfers phosphoryl groups between the three different response regulator domains of SLN1, SSK1, and SKN7 (designated R1, R2, and R3, respectively)...
- Ostrander D, Gorman J. The extracellular domain of the Saccharomyces cerevisiae Sln1p membrane osmolarity sensor is necessary for kinase activity. J Bacteriol. 1999;181:2527-34 pubmedThe function of the extracellular domain (ECD) of Sln1p, a plasma membrane two-transmembrane domain (TMD) sensor of the high-osmolarity glycerol (HOG) response pathway, has been studied in the yeast Saccharomyces cerevisiae...
- Mollapour M, Shepherd A, Piper P. Presence of the Fps1p aquaglyceroporin channel is essential for Hog1p activation, but suppresses Slt2(Mpk1)p activation, with acetic acid stress of yeast. Microbiology. 2009;155:3304-11 pubmed publisher..Lack of Fps1p therefore exerts opposing effects on the activation of Hog1p and Slt2p in yeast exposed to acetic acid stress. ..
- Li S, Ault A, Malone C, Raitt D, Dean S, Johnston L, et al. The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two response regulators, Ssk1p and Skn7p. EMBO J. 1998;17:6952-62 pubmed..Phosphorylation of Sln1p inhibits the HOG1 MAP kinase osmosensing pathway via a phosphorelay mechanism including Ypd1p and the response ..
- Warmka J, Hanneman J, Lee J, Amin D, Ota I. Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1. Mol Cell Biol. 2001;21:51-60 pubmed..Consistent with its role as a negative regulator of Hog1, which accumulates in the nucleus upon activation, Ptc1 was found in both the nucleus and the cytoplasm. Thus, one function of Ptc1 is to inactivate Hog1. ..
- Singh K. The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion. Free Radic Biol Med. 2000;29:1043-50 pubmed..This study demonstrates that primary sensors of osmotic stress, the Sln1p-Ssk1p two-component proteins, are involved in sensing oxidative stress specifically induced by hydrogen peroxide ..
- Fassler J, Gray W, Malone C, Tao W, Lin H, Deschenes R. Activated alleles of yeast SLN1 increase Mcm1-dependent reporter gene expression and diminish signaling through the Hog1 osmosensing pathway. J Biol Chem. 1997;272:13365-71 pubmed..Phosphorylation of Sln1p leads to inhibition of the Hog1 mitogen-activated protein kinase osmosensing pathway...
- Xu Q, Porter S, West A. The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems. Structure. 2003;11:1569-81 pubmed..protein intermediate required for phosphoryl group transfer from a membrane-bound sensor histidine kinase (SLN1) to two distinct response regulator proteins (SSK1 and SKN7)...
- Lu J, Deschenes R, Fassler J. Role for the Ran binding protein, Mog1p, in Saccharomyces cerevisiae SLN1-SKN7 signal transduction. Eukaryot Cell. 2004;3:1544-56 pubmedYeast Sln1p is an osmotic stress sensor with histidine kinase activity...
- Lu J, Deschenes R, Fassler J. Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles between the nucleus and cytoplasm for SLN1-dependent phosphorylation of Ssk1p and Skn7p. Eukaryot Cell. 2003;2:1304-14 pubmedb>Sln1p is a plasma membrane-localized two-component histidine kinase that functions as an osmotic stress sensor in Saccharomyces cerevisiae...
- Zhao X, Copeland D, Soares A, West A. Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog. J Mol Biol. 2008;375:1141-51 pubmedThe crystal structure of the yeast SLN1 response regulator (RR) domain bound to both a phosphoryl analog [beryllium fluoride (BeF(3)(-))] and Mg(2+), in complex with its downstream phosphorelay signaling partner YPD1, has been determined ..
- Stojanovski K, Ferrar T, Benisty H, Uschner F, Delgado J, Jimenez J, et al. Interaction Dynamics Determine Signaling and Output Pathway Responses. Cell Rep. 2017;19:136-149 pubmed publisher..We created mutant pairs of the Sln1-Ypd1 complex interface that caused major compensating changes in the association (kon) and dissociation (..