The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The supplied identity is internally consistent and matches the literature: SLN1, also called YPD2 and ordered locus YIL147C, encodes the S288c budding-yeast protein Sln1p, a plasma-membrane hybrid sensor histidine kinase. Its architecture—an extracellular region between two transmembrane segments, a cytosolic HAMP/coiled-coil signaling region, a HisKA/HATPase transmitter, and a C-terminal CheY-like receiver—agrees with the domains listed for UniProt P39928. No evidence from a different same-symbol gene was used. Proteins called Sln1 in Candida, Aspergillus, and plant-pathogenic fungi are homologs, not P39928, and their phenotypes cannot automatically be assigned to budding-yeast Sln1.
Sln1’s primary biochemical function is ATP-dependent protein histidine kinase signaling. In a membrane dimer, Sln1 uses ATP to autophosphorylate His576, apparently in trans, and transfers the phosphoryl group to its own receiver Asp1144. Phosphate then passes to Ypd1-His64 and from Ypd1 to either Ssk1-Asp554 or Skn7-Asp427. Thus, Sln1 does not phosphorylate a conventional soluble metabolite; its physiological substrates are residues within an ordered protein phosphorelay. Direct transfer from Sln1-His576 to Ypd1 is not supported—the intervening Sln1-Asp1144 step is required (posas1996yeasthog1map pages 4-6, posas1996yeasthog1map pages 1-2).
Under ordinary osmolarity, active Sln1 keeps Ssk1 phosphorylated and thereby represses the Ssk2/Ssk22–Pbs2–Hog1 MAPK cascade. Hyperosmotic shock inhibits Sln1 activity, allowing dephosphorylated Ssk1 to activate that cascade and promote glycerol-centered osmoadaptation. A parallel Sln1–Ypd1–Skn7 branch controls hypo-osmotic/cell-wall transcription, including OCH1. The strongest mechanistic evidence remains the foundational biochemical and genetic literature; 2023–2024 work chiefly refines the evolutionary classification and broader significance of fungal histidine kinases rather than changing this core model.
Sln1 is a hybrid histidine kinase because one polypeptide contains both the transmitter and first response-regulator receiver. Functional dissection showed that a construct ending near residue 1070 retained the transmitter but lacked the C-terminal receiver, while signaling required receiver Asp1144. Ypd1 interacts with the Sln1 receiver region, consistent with a modular transmitter→receiver→HPt relay rather than direct kinase-to-Ypd1 transfer (posas1996yeasthog1map pages 3-4).
The HAMP/coiled-coil region couples the transmembrane input to the cytosolic kinase. The HATPase module binds ATP and supports phosphoryl transfer to the conserved histidine in the dimerization/histidine-phosphotransfer region. The C-terminal CheY-like domain contains the conserved receiver aspartate. This architecture is characteristic of fungal hybrid histidine kinases, whose added receiver domain distinguishes their multistep relays from many canonical bacterial two-component systems (mina2024structureanddistribution pages 1-2).
Sln1 is an integral plasma-membrane protein functioning as a membrane-bound dimer. Its extracellular N-terminal region lies between two transmembrane helices, whereas its HAMP/transmitter and receiver machinery is cytoplasmic. Consequently, ATP utilization and all phosphotransfer reactions occur on the cytoplasmic side of the membrane (lu2003saccharomycescerevisiaehistidine pages 1-3, xu2001thestructureand pages 35-38, dexter2015robustnetworkstructure pages 1-2).
The downstream topology is compartmentalized. Ssk1 acts in the cytoplasmic HOG cascade, whereas Skn7 is a nuclear transcription factor. Ypd1 is found in both cytosol and nucleus and shuttles between them, providing a physical means to distribute the membrane-generated Sln1 signal to both response regulators (lu2003saccharomycescerevisiaehistidine pages 1-3). Sln1 itself should therefore be annotated primarily to the plasma membrane, not to the nucleus; nuclear signaling is mediated by mobile Ypd1 and nuclear Skn7.
A useful reaction scheme is:
ATP + Sln1-His576 → ADP + Sln1-His576~P
Sln1-His576~P + Sln1-Asp1144 → Sln1-His576 + Sln1-Asp1144~P
Sln1-Asp1144~P + Ypd1-His64 → Sln1-Asp1144 + Ypd1-His64~P
Ypd1 subsequently donates phosphate to Ssk1-Asp554 or Skn7-Asp427. The first step is reported to occur in trans within the Sln1 dimer; the His→Asp step is intramolecular in the standard model (kaserer2009effectofosmolytes pages 43-49).
Direct biochemical support includes incorporation of phosphate from [γ-³²P]ATP by a purified Sln1 transmitter construct. H576Q abolished this autophosphorylation. Approximately half of the radiolabel transferred to the receiver construct within 15 minutes, and transfer required Asp1144. Differential acid/base sensitivity identified phosphohistidine on the transmitter and phosphoaspartate on the receiver. H576Q or D1144N also abolished Ypd1 phosphorylation in vivo, and no direct H576→Ypd1-H64 shortcut was detected (posas1996yeasthog1map pages 4-6).
Accordingly, substrate specificity should be described at two levels:
EC 2.7.13.3, protein histidine kinase, is therefore appropriate. Sln1 should not be annotated as a tyrosine phosphatase despite the historical synonym “tyrosine phosphatase-dependent protein 2”; that name reflects genetic context rather than Sln1’s catalytic chemistry.
At normal osmolarity, Sln1 is active and maintains the relay:
Sln1-H576 → Sln1-D1144 → Ypd1-H64 → Ssk1-D554.
Phosphorylated Ssk1 does not activate the functionally overlapping MAPKKKs Ssk2 and Ssk22. Pbs2 and Hog1 therefore remain relatively inactive. Hyperosmotic stress suppresses Sln1 kinase activity, the supply of phosphoryl groups declines, and unphosphorylated Ssk1 binds and activates Ssk2/Ssk22. These activate Pbs2 and then Hog1, leading to transcriptional and metabolic adaptation, notably glycerol production and accumulation (posas1996yeasthog1map pages 1-2, dexter2015robustnetworkstructure pages 1-2).
The model is supported by several convergent experiments:
Sln1 is thus an unusual stress sensor whose kinase is relatively active in the absence of hyperosmotic stress. Stress is represented as loss of inhibitory phosphorelay output—a release-of-inhibition circuit.
Ypd1 also transfers phosphate to nuclear Skn7 at Asp427. Increased Sln1 activity, associated especially with hypo-osmotic signaling or activating sln1 alleles, promotes Skn7-dependent transcription. Skn7 contains a receiver domain and an HSF-like DNA-binding region, making it a response regulator directly coupled to transcription (li1998theyeasthistidine pages 1-2, li2002theeukaryotictwocomponent pages 1-2).
A particularly well-defined target is OCH1, encoding an α-1,6-mannosyltransferase involved in N-linked glycoprotein maturation and cell-wall integrity. Skn7 binds a repeated response element in the OCH1 promoter. Activating sln1 alleles produced approximately 3–5-fold reporter induction; an isolated OCH1 promoter region gave 3.2-fold activation, and a duplicated response element gave 5.2-fold activation. Substitution of two conserved guanines abolished the response (li1998theyeasthistidine pages 1-2, li2002theeukaryotictwocomponent pages 7-8).
This branch must be distinguished from Skn7’s oxidative-stress role. OCH1/hypo-osmotic signaling requires the phosphoacceptor Asp427, whereas important oxidative-stress functions of Skn7 can be Asp427-independent. Therefore, not every Skn7-regulated oxidative response should be attributed directly to Sln1 phosphotransfer (li2002theeukaryotictwocomponent pages 1-2).
The physiological input is best described as osmotic/turgor or membrane–cell-wall mechanical state, not a chemically defined extracellular ligand. Hyperosmotic shock causes water loss and reduced turgor and inhibits Sln1 kinase activity; hypotonic conditions favor increased pathway phosphorylation. The extracellular domain is functionally important and has been implicated in dimerization and communication with the cell-wall environment, but the precise molecular stimulus and conformational sequence remain incompletely resolved (xu2001thestructureand pages 35-38, kaserer2009effectofosmolytes pages 43-49).
Consequently, “osmosensor” is experimentally justified at the systems level, while statements that Sln1 directly binds a particular osmolyte would be unsupported. The most cautious current model is that extracellular-domain/transmembrane/HAMP conformational coupling reports physical changes associated with turgor, membrane tension, or cell-wall state.
The HOG pathway can activate within roughly one minute of osmotic shock and can follow periodic changes in external osmolyte concentration up to approximately 0.0046 Hz. Such dynamics require both rapid phosphorelay shutdown and robust suppression during unstressed growth (dexter2015robustnetworkstructure pages 1-2).
A combined perturbation/modeling study concluded that the three-component architecture is robust because Ypd1 forms an excess buffering pool. Ypd1 was estimated to be at least fivefold more abundant than Ssk1. Moderate changes in Sln1, Ypd1, or Ssk1 generally did not spuriously activate Hog1, whereas depletion of Ypd1 caused inappropriate HOG activation. Massive Ssk1 overexpression increased phospho-Hog1 (p=0.0224), while Ypd1 overexpression reduced it (p=0.0246) (dexter2015robustnetworkstructure pages 8-11).
This supports an expert interpretation of Ypd1 as more than a passive wire: its abundance buffers fluctuations in sensor and response-regulator levels. The multicomponent relay thereby combines sensitivity to osmotic shutdown with resistance to molecular-expression noise—an advantage not readily available to a direct two-component architecture (dexter2015robustnetworkstructure pages 1-2, dexter2015robustnetworkstructure pages 8-11).
The principal evidence is summarized below.
| Annotation aspect | Best-supported conclusion | Key experimental evidence / quantitative result | Evidence type | Source, date, DOI URL |
|---|---|---|---|---|
| Identity and domain architecture | The target is S. cerevisiae Sln1p, a hybrid sensor histidine kinase containing an extracellular sensor region, two membrane-spanning segments, a cytosolic HAMP/coiled-coil region, histidine-kinase transmitter/HATPase module, and C-terminal CheY-like receiver domain. This agrees with P39928, SLN1/YPD2/YIL147C, rather than a similarly named protein from another organism. | Deletion/mutation and domain-complementation experiments showed that the transmitter and receiver are distinct required modules; residues 1–1070 retain the kinase module but lack the receiver, and receiver Asp1144 is required for signaling. | Direct genetics and domain dissection, supported by curated domain annotation | Posas et al., September 1996, https://doi.org/10.1016/S0092-8674(00)80162-2 (posas1996yeasthog1map pages 3-4, posas1996yeasthog1map pages 1-2) |
| Localization and topology | Sln1p is an integral plasma-membrane, dimeric sensor. Its N-terminal extracellular region lies between two predicted transmembrane helices; the catalytic transmitter and receiver regions face the cytoplasm. Ypd1 subsequently carries the signal through cytoplasm and nucleus. | Sln1p was characterized as a membrane-bound dimer and plasma-membrane kinase; localization studies showed Ypd1 in both cytosol and nucleus, consistent with signaling from membrane Sln1 to cytoplasmic Ssk1 and nuclear Skn7. | Topology prediction, biochemical/genetic characterization, and fluorescence localization | Lu et al., December 2003, https://doi.org/10.1128/EC.2.6.1304-1314.2003 (lu2003saccharomycescerevisiaehistidine pages 1-3, xu2001thestructureand pages 35-38, dexter2015robustnetworkstructure pages 1-2) |
| Catalytic reaction and specificity | Sln1p uses ATP to autophosphorylate His576, apparently in trans within the dimer, and then transfers the phosphoryl group intramolecularly to Asp1144. The receiver transfers it specifically to Ypd1-His64; there is no supported direct His576→Ypd1 shortcut. | A purified GST–Sln1 transmitter incorporated phosphate from [γ-³²P]ATP; H576Q abolished autophosphorylation. About half of the label transferred to the receiver within 15 minutes, dependent on Asp1144. Acid/base sensitivity distinguished phosphohistidine from phosphoaspartate. | Direct in-vitro radiochemical biochemistry and site-directed mutagenesis | Posas et al., September 1996, https://doi.org/10.1016/S0092-8674(00)80162-2 (posas1996yeasthog1map pages 4-6) |
| Ssk1–HOG branch | In normal osmolarity, active Sln1 drives His576→Asp1144→Ypd1-His64→Ssk1-Asp554 phosphotransfer; phosphorylated Ssk1 cannot activate Ssk2/Ssk22, keeping Pbs2–Hog1 off. Hyperosmotic stress inhibits Sln1, allowing dephosphorylated Ssk1 to activate the HOG MAPK cascade and osmoadaptation. | Sln1-dependent phosphorylation fell strongly after 0.4 M NaCl. Mutating Sln1 His576 or Asp1144 abolished Ypd1 phosphorylation. sln1 lethality was suppressed by deleting SSK1, SSK2, PBS2, or HOG1, linking loss of Sln1 to toxic constitutive HOG activation. | Direct biochemical and genetic epistasis evidence | Posas et al., September 1996, https://doi.org/10.1016/S0092-8674(00)80162-2 (posas1996yeasthog1map pages 3-4, posas1996yeasthog1map pages 4-6, posas1996yeasthog1map pages 1-2) |
| Skn7–OCH1 branch | The same Sln1–Ypd1 relay also phosphorylates nuclear Skn7 at Asp427. Phospho-Skn7 activates hypo-osmotic/cell-wall transcription, including OCH1, which encodes an α-1,6-mannosyltransferase required for glycoprotein maturation and cell-wall integrity. This branch is mechanistically distinct from Skn7’s Asp427-independent oxidative-stress function. | Activating sln1 alleles increased Skn7-dependent reporters roughly 3–5-fold; loss of SLN1 reduced one reporter about 10-fold. An OCH1 promoter fragment showed 3.2-fold activation and a duplicated response element 5.2-fold activation; mutation of two conserved guanines abolished the response. | Genetics, reporter assays, EMSA, promoter mutagenesis, and phosphoacceptor mutation | Li et al., December 1998, https://doi.org/10.1093/emboj/17.23.6952; Li et al., February 2002, https://doi.org/10.1091/mbc.01-09-0434 (li1998theyeasthistidine pages 1-2, li2002theeukaryotictwocomponent pages 1-2, li2002theeukaryotictwocomponent pages 7-8) |
| Systems robustness | The three-component relay is robust to moderate variation in Sln1, Ypd1, and Ssk1 abundance because a large excess pool of Ypd1 buffers fluctuations; depletion of Ypd1 causes inappropriate HOG activation. | Ypd1 was estimated to be at least fivefold more abundant than Ssk1. HOG signaling can activate within 1 minute and track osmolyte oscillations up to 0.0046 Hz. Massive Ssk1 overexpression increased phospho-Hog1 (p=0.0224), whereas Ypd1 overexpression lowered it (p=0.0246). | Quantitative perturbation experiments and biochemical mathematical modeling | Dexter et al., March 2015, https://doi.org/10.1186/s12918-015-0158-y (dexter2015robustnetworkstructure pages 1-2, dexter2015robustnetworkstructure pages 8-11) |
| 2024 phylogenomics | Directly relevant to classification, not new mechanistic evidence for P39928: Sln1 is the unique S. cerevisiae representative of fungal group-VI transmembrane osmosensors. Group-VI homolog phenotypes in pathogenic fungi are contextual and must not be assigned to yeast P39928. | A phylogenomic survey analyzed 726 predicted histidine kinases from 91 fungal species, including 42 group-VI proteins. The authors emphasize histidine kinases as prospective antifungal targets because humans lack these signaling systems. | Comparative genomics and phylogenomics; homolog evidence only where explicitly stated | Mina et al., published September 14, 2024, https://doi.org/10.1007/s00294-024-01301-w (mina2024structureanddistribution pages 1-2, mina2024structureanddistribution pages 2-5, mina2024structureanddistribution pages 5-8) |
| Optogenetic application | Sln1’s kinase module has been repurposed as a light-controlled signaling input, demonstrating that its ATP-dependent kinase/Ypd1 interface can drive engineered gene-expression and Hog1-localization responses in living yeast. | A LOV–Sln1 hybrid replaced endogenous Sln1; blue light inhibited kinase autophosphorylation and transfer to Ypd1, reduced steady-state OCH1 expression by about 40% at saturating light, and induced persistent rather than transient Hog1 nuclear accumulation. | Protein engineering, in-vitro kinase assay, reporter expression, and live-cell fluorescence | Bury & Hellingwerf, April 2018, https://doi.org/10.1186/s13568-018-0582-7 (bury2018designcharacterizationand pages 1-2) |
Table: Evidence matrix for the identity, mechanism, localization, pathways, quantitative behavior, evolutionary context, and engineered use of S. cerevisiae Sln1/P39928. Findings from other fungal Sln1-family proteins are explicitly treated as contextual rather than direct evidence for P39928.
Direct 2023–2024 mechanistic studies of S. cerevisiae P39928 are limited; the core phosphorelay model is mature and continues to rest on high-quality biochemical and genetic work from the 1990s–2010s. The most relevant recent authoritative development is the Mina et al. 2024 fungal-histidine-kinase phylogenomics study, received May 24, revised July 2, accepted August 17, and published online September 14, 2024: https://doi.org/10.1007/s00294-024-01301-w (mina2024structureanddistribution pages 1-2).
That study analyzed 726 predicted histidine kinases from 91 fungal species and classified 42 group-VI transmembrane osmosensors. It places S. cerevisiae Sln1 as the well-studied, unique histidine kinase of budding yeast and a representative of group VI. The work reinforces the view that fungal hybrid kinases combine variable sensing regions with conserved HisKA, HATPase, and receiver machinery (mina2024structureanddistribution pages 1-2, mina2024structureanddistribution pages 5-8).
The same survey emphasizes that humans lack two-component histidine-kinase systems, making fungal histidine kinases conceptually attractive antifungal targets. This is an expert translational inference, not evidence that P39928 itself is a clinical drug target: S. cerevisiae is principally a model and industrial organism, and group-VI homolog phenotypes in Candida, Aspergillus, or phytopathogens do not establish identical essentiality or inhibitor sensitivity for Sln1/P39928 (mina2024structureanddistribution pages 2-5, mina2024structureanddistribution pages 5-8).
A 2024 structural paper examined receiver–HPt recognition in several fungal hybrid kinases, including Candida albicans Sln1-related material, but it did not directly determine the structure or mechanism of S. cerevisiae P39928. It is therefore useful as broader family context, not as direct annotation evidence.
Sln1’s modular transmitter and Ypd1 interface have been repurposed in a LOV–Sln1 light-regulated kinase. Blue light inhibited ATP-dependent autophosphorylation and transfer to Ypd1. In cells lacking endogenous Sln1, the construct enabled optical control of downstream signaling, reduced steady-state OCH1 expression by about 40% under saturating illumination, and produced persistent Hog1 nuclear accumulation rather than the transient response characteristic of salt shock. This demonstrates an experimentally implemented route for controlling eukaryotic gene expression through a histidine phosphorelay: Bury and Hellingwerf, published April 2018, https://doi.org/10.1186/s13568-018-0582-7 (bury2018designcharacterizationand pages 1-2).
The HOG system is central to yeast survival under high sugar, salt, desiccation, and related osmotic conditions relevant to fermentation and industrial cultivation. Sln1 is the membrane input governing one major HOG branch. Nevertheless, direct industrial implementation of SLN1 engineering is less established than general HOG-pathway engineering; constitutive manipulation is potentially hazardous because excessive HOG activity impairs growth, while excessive Sln1/Ssk1 expression can also produce fitness defects (dexter2015robustnetworkstructure pages 1-2, dexter2015robustnetworkstructure pages 8-11).
Fungal histidine kinases are absent from humans and regulate stress adaptation and, in pathogenic species, sometimes virulence and antifungal susceptibility. Sln1 supplies a mechanistic model for this target class. However, drug-development conclusions require pathogen-specific validation because fungal kinase repertoires and redundancy differ substantially. The 2024 survey found marked diversity across fungal clades, including 19-class classification schemes and newly recognized groups, underscoring that an inhibitor designed against one group may not generalize (mina2024structureanddistribution pages 1-2, mina2024structureanddistribution pages 2-5).
Plasma-membrane hybrid osmosensing histidine kinase that uses ATP to autophosphorylate His576 and transfers phosphate through its receiver Asp1144 to Ypd1. The Ypd1–Ssk1 branch represses the Ssk2/Ssk22–Pbs2–Hog1 high-osmolarity pathway in unstressed cells; hyperosmotic inhibition of Sln1 releases HOG signaling. A parallel Ypd1–Skn7 branch regulates hypo-osmotic and cell-wall transcription, including OCH1.
This wording captures the experimentally established primary function, reaction, protein-substrate specificity, localization, and pathway role without overassigning broader phenotypes or findings from non-cerevisiae Sln1 homologs.
References
(posas1996yeasthog1map pages 4-6): Francesc Posas, Susannah M Wurgler-Murphy, Tatsuya Maeda, Elizabeth A Witten, Tran Cam Thai, and Haruo Saito. Yeast hog1 map kinase cascade is regulated by a multistep phosphorelay mechanism in the sln1–ypd1–ssk1 “two-component” osmosensor. Cell, 86:865-875, Sep 1996. URL: https://doi.org/10.1016/s0092-8674(00)80162-2, doi:10.1016/s0092-8674(00)80162-2. This article has 1174 citations and is from a highest quality peer-reviewed journal.
(posas1996yeasthog1map pages 1-2): Francesc Posas, Susannah M Wurgler-Murphy, Tatsuya Maeda, Elizabeth A Witten, Tran Cam Thai, and Haruo Saito. Yeast hog1 map kinase cascade is regulated by a multistep phosphorelay mechanism in the sln1–ypd1–ssk1 “two-component” osmosensor. Cell, 86:865-875, Sep 1996. URL: https://doi.org/10.1016/s0092-8674(00)80162-2, doi:10.1016/s0092-8674(00)80162-2. This article has 1174 citations and is from a highest quality peer-reviewed journal.
(xu2001thestructureand pages 35-38): Q Xu. The structure and function of ypd1, a histidine-containing phosphotransfer protein from yeast. Unknown journal, 2001.
(posas1996yeasthog1map pages 3-4): Francesc Posas, Susannah M Wurgler-Murphy, Tatsuya Maeda, Elizabeth A Witten, Tran Cam Thai, and Haruo Saito. Yeast hog1 map kinase cascade is regulated by a multistep phosphorelay mechanism in the sln1–ypd1–ssk1 “two-component” osmosensor. Cell, 86:865-875, Sep 1996. URL: https://doi.org/10.1016/s0092-8674(00)80162-2, doi:10.1016/s0092-8674(00)80162-2. This article has 1174 citations and is from a highest quality peer-reviewed journal.
(mina2024structureanddistribution pages 1-2): Sara Mina, Anaïs Hérivaux, Hajar Yaakoub, Vincent Courdavault, Méline Wéry, and Nicolas Papon. Structure and distribution of sensor histidine kinases in the fungal kingdom. Current genetics, 70 1:17, Sep 2024. URL: https://doi.org/10.1007/s00294-024-01301-w, doi:10.1007/s00294-024-01301-w. This article has 3 citations and is from a peer-reviewed journal.
(lu2003saccharomycescerevisiaehistidine pages 1-3): Jade Mei-Yeh Lu, Robert J. Deschenes, and Jan S. Fassler. Saccharomyces cerevisiae histidine phosphotransferase ypd1p shuttles between the nucleus and cytoplasm for sln1-dependent phosphorylation of ssk1p and skn7p. Eukaryotic Cell, 2:1304-1314, Dec 2003. URL: https://doi.org/10.1128/ec.2.6.1304-1314.2003, doi:10.1128/ec.2.6.1304-1314.2003. This article has 120 citations and is from a peer-reviewed journal.
(dexter2015robustnetworkstructure pages 1-2): Joseph P Dexter, Ping Xu, Jeremy Gunawardena, and Megan N McClean. Robust network structure of the sln1-ypd1-ssk1 three-component phospho-relay prevents unintended activation of the hog mapk pathway in saccharomyces cerevisiae. BMC Systems Biology, Mar 2015. URL: https://doi.org/10.1186/s12918-015-0158-y, doi:10.1186/s12918-015-0158-y. This article has 24 citations and is from a peer-reviewed journal.
(kaserer2009effectofosmolytes pages 43-49): AO Kaserer. Effect of osmolytes on regulating the activities of the ssk1 response regulator from saccharomyces cerevisiae. Unknown journal, 2009.
(li1998theyeasthistidine pages 1-2): Sheng Li, Addison Ault, Cheryl L. Malone, Desmond Raitt, Susan Dean, Leland H. Johnston, Robert J. Deschenes, and Jan S. Fassler. The yeast histidine protein kinase, sln1p, mediates phosphotransfer to two response regulators, ssk1p and skn7p. The EMBO Journal, 17:6952-6962, Dec 1998. URL: https://doi.org/10.1093/emboj/17.23.6952, doi:10.1093/emboj/17.23.6952. This article has 253 citations.
(li2002theeukaryotictwocomponent pages 1-2): Sheng Li, Susan Dean, Zhijian Li, Joe Horecka, Robert J. Deschenes, and Jan S. Fassler. The eukaryotic two-component histidine kinase sln1p regulates och1 via the transcription factor, skn7p. Molecular biology of the cell, 13 2:412-24, Feb 2002. URL: https://doi.org/10.1091/mbc.01-09-0434, doi:10.1091/mbc.01-09-0434. This article has 133 citations and is from a domain leading peer-reviewed journal.
(li2002theeukaryotictwocomponent pages 7-8): Sheng Li, Susan Dean, Zhijian Li, Joe Horecka, Robert J. Deschenes, and Jan S. Fassler. The eukaryotic two-component histidine kinase sln1p regulates och1 via the transcription factor, skn7p. Molecular biology of the cell, 13 2:412-24, Feb 2002. URL: https://doi.org/10.1091/mbc.01-09-0434, doi:10.1091/mbc.01-09-0434. This article has 133 citations and is from a domain leading peer-reviewed journal.
(dexter2015robustnetworkstructure pages 8-11): Joseph P Dexter, Ping Xu, Jeremy Gunawardena, and Megan N McClean. Robust network structure of the sln1-ypd1-ssk1 three-component phospho-relay prevents unintended activation of the hog mapk pathway in saccharomyces cerevisiae. BMC Systems Biology, Mar 2015. URL: https://doi.org/10.1186/s12918-015-0158-y, doi:10.1186/s12918-015-0158-y. This article has 24 citations and is from a peer-reviewed journal.
(mina2024structureanddistribution pages 2-5): Sara Mina, Anaïs Hérivaux, Hajar Yaakoub, Vincent Courdavault, Méline Wéry, and Nicolas Papon. Structure and distribution of sensor histidine kinases in the fungal kingdom. Current genetics, 70 1:17, Sep 2024. URL: https://doi.org/10.1007/s00294-024-01301-w, doi:10.1007/s00294-024-01301-w. This article has 3 citations and is from a peer-reviewed journal.
(mina2024structureanddistribution pages 5-8): Sara Mina, Anaïs Hérivaux, Hajar Yaakoub, Vincent Courdavault, Méline Wéry, and Nicolas Papon. Structure and distribution of sensor histidine kinases in the fungal kingdom. Current genetics, 70 1:17, Sep 2024. URL: https://doi.org/10.1007/s00294-024-01301-w, doi:10.1007/s00294-024-01301-w. This article has 3 citations and is from a peer-reviewed journal.
(bury2018designcharacterizationand pages 1-2): Aleksandra Bury and Klaas J. Hellingwerf. Design, characterization and in vivo functioning of a light-dependent histidine protein kinase in the yeast saccharomyces cerevisiae. AMB Express, Apr 2018. URL: https://doi.org/10.1186/s13568-018-0582-7, doi:10.1186/s13568-018-0582-7. This article has 7 citations and is from a peer-reviewed journal.