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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 requested protein is unambiguously the S. cerevisiae S288c phosphorelay intermediate Ypd1, encoded by YPD1/YDL235C (UniProt Q07688), not a similarly named protein from another organism. Direct yeast literature describes a 167-residue, approximately 19–20-kDa, soluble histidine-containing phosphotransfer (HPt) protein whose experimentally determined all-helical four-helix-bundle structure and exposed phosphoacceptor His64 agree with the supplied YPD1-family, Hpt/PF01627, IPR008207, IPR036641, and IPR045871 annotations. Thus, the database identity, organism, family, and domains are mutually consistent. (xu2001thestructureand pages 38-41, xu2003theyeastypd1sln1 pages 1-2)
Ypd1 is not an ATP-dependent kinase or phosphatase. Its primary function is to act as a mobile phosphate-transfer intermediate and branch point in the Sln1 multistep phosphorelay. It accepts phosphate from the receiver domain of Sln1 and transfers it to either Ssk1 or Skn7. The chemically defined sequence is Sln1-His576 → Sln1-Asp1144 → Ypd1-His64 → response-regulator Asp, a His–Asp–His–Asp relay. Mutation of Ypd1 His64 prevents its phosphorylation and disrupts phosphate transfer, establishing His64 as the essential phosphoacceptor/donor site. (xu2001thestructureand pages 38-41, kennedy2016thebiochemicalcharacterization pages 36-41, kennedy2016thebiochemicalcharacterizationa pages 36-41)
| Context/state | Phosphotransfer event or interaction | Consequence | Evidence type |
|---|---|---|---|
| Basal/normal osmolarity | Active Sln1 relays phosphate through Sln1 His576 → Sln1 Asp1144 → Ypd1 His64 → Ssk1 receiver Asp. | Phosphorylated Ssk1 cannot activate Ssk2/Ssk22, so the HOG MAPK cascade remains off. (kennedy2019roleofthe pages 1-2, kennedy2016thebiochemicalcharacterizationa pages 36-41, dexter2015robustnetworkstructure pages 1-2) | In vivo genetics and signaling assays; in vitro phosphotransfer; biochemical modeling |
| Hyperosmotic stress | Sln1-dependent phosphorelay flux decreases; Ssk1 accumulates in its unphosphorylated signaling-active state. | Unphosphorylated Ssk1 activates Ssk2/Ssk22 → Pbs2 → Hog1, initiating osmoadaptive transcription and glycerol accumulation. (lu2003saccharomycescerevisiaehistidine pages 1-3, porter2005acommondocking pages 1-2, dexter2015robustnetworkstructure pages 1-2) | Genetic and biochemical pathway analysis; phospho-Hog1 assays |
| Skn7 branch | Ypd1 transfers phosphate from Sln1 to the receiver domain of Skn7, a predominantly nuclear response regulator. | Phosphorylated Skn7 regulates outputs associated with cell-wall biosynthesis/stress and cell-cycle control; this branch is distinct from Ssk1-mediated HOG regulation. (kennedy2019roleofthe pages 1-2, lu2003saccharomycescerevisiaehistidine pages 1-3, porter2005acommondocking pages 1-2) | Phosphotransfer, localization, genetic, and transcriptional evidence |
| Cellular localization | Ypd1 was detected in both nucleus and cytosol, placing it between membrane-associated Sln1, cytosolic Ssk1, and nuclear Skn7. | Its distribution permits phosphate delivery to response regulators in both cellular compartments; nucleocytoplasmic shuttling has been proposed from GFP-fusion experiments. (lu2003saccharomycescerevisiaehistidine pages 1-3) | GFP-fusion fluorescence and confocal microscopy |
| Structure and partner recognition | Ypd1 is an all-helical HPt protein with a four-helix-bundle core, solvent-exposed His64, and a largely hydrophobic common docking surface for Sln1-R1, Ssk1-R2, and Skn7-R3. | A shared interface enables branched partner recognition, while peripheral polar/charged contacts contribute specificity; ten surface residues were implicated in contacts with all three receiver domains. (xu2003theyeastypd1sln1 pages 1-2, xu2003theyeastypd1sln1 pages 9-11, porter2005acommondocking pages 6-7) | X-ray crystallography, alanine-scanning mutagenesis, and yeast two-hybrid assays |
| Engineering application—experimental proof-of-concept | A blue-light-responsive LOV–Sln1 hybrid altered Sln1 kinase activity and phosphate transfer to Ypd1. | Light transmitted through the Ypd1-containing relay changed OCH1 expression by about 40% at steady state and produced persistent Hog1 nuclear accumulation, demonstrating optogenetic control of yeast signaling. (bury2018designcharacterizationand pages 7-8, bury2018designcharacterizationand pages 1-2) | In vitro phosphorylation plus engineered in vivo reporter and microscopy assays |
Table: This table summarizes the experimentally supported roles of S. cerevisiae S288c Ypd1 across osmotic states, its Skn7 branch, localization, structural basis of partner recognition, and an optogenetic proof-of-concept.
Verified identifiers: gene YPD1, ordered locus YDL235C, organism Saccharomyces cerevisiae strain S288c, UniProt Q07688. The literature’s “Ypd1,” “Ypd1p,” and “YPD1” refer to this HPt protein when the organism is S. cerevisiae. “Tyrosine phosphatase-dependent protein 1” is a historical alternative name and should not be interpreted as evidence that Ypd1 is itself a tyrosine phosphatase.
The protein is a stand-alone HPt domain, rather than the kinase or output response regulator. HPt proteins transiently carry a high-energy phosphohistidine and mediate phosphotransfer between receiver domains. Ypd1’s four-helix-bundle fold, exposed His64, and response-regulator-binding surface directly support the supplied domain annotation. (kennedy2019roleofthe pages 1-2, xu2003theyeastypd1sln1 pages 1-2)
Reports about Ypd1 homologs in Candida albicans, Cryptococcus neoformans, Aspergillus fumigatus, or other fungi are not direct evidence for S288c Ypd1. For example, C. albicans YPD1 is dispensable and has distinct mutant phenotypes, whereas deletion of S. cerevisiae YPD1 is lethal under ordinary genetic backgrounds. (mavrianos2014twocomponenthistidinephosphotransfer pages 1-2, mavrianos2014twocomponenthistidinephosphotransfer pages 7-7)
Ypd1 catalyzes reversible phosphotransfer involving its N-phosphorylated His64. Its physiological upstream phosphodonor is the phosphorylated receiver domain of Sln1, and its physiological downstream phosphate acceptors are the receiver domains of Ssk1 and Skn7. ATP is used by Sln1 for initial autophosphorylation, not by Ypd1; transfer from phospho-Sln1 to Ypd1 and onward is ATP-independent. (kennedy2019roleofthe pages 1-2, mavrianos2014twocomponenthistidinephosphotransfer pages 1-2)
The direct relay is:
Ypd1 is therefore best classified as a signaling phosphotransfer protein, not an enzyme with a freely diffusible small-molecule substrate. Its effective substrate specificity is protein-partner specificity: Sln1-R1 as donor/acceptor upstream and Ssk1-R2 or Skn7-R3 downstream. In vitro transfer involving bacterial CheY demonstrates some biochemical promiscuity, but this is not known to be physiologically relevant. (xu2001thestructureand pages 38-41, xu2003theyeastypd1sln1 pages 9-11)
Under normal osmolarity, active plasma-membrane Sln1 continuously feeds phosphate through Ypd1 to Ssk1. Phosphorylated Ssk1 does not activate the redundant MAP3Ks Ssk2/Ssk22; consequently Pbs2 and Hog1 remain inactive. Ypd1 thus acts functionally as an upstream negative regulator of basal HOG signaling, although its immediate biochemical action is positive phosphate delivery to Ssk1. (lu2003saccharomycescerevisiaehistidine pages 1-3, dexter2015robustnetworkstructure pages 1-2)
Hyperosmotic stress reduces Sln1-relay output. Ssk1 becomes dephosphorylated, binds/activates Ssk2 and Ssk22, and triggers Ssk2/Ssk22 → Pbs2 → Hog1 signaling. Hog1 then drives transcriptional and metabolic osmoadaptation, including increased glycerol accumulation. HOG activation can occur within approximately one minute of osmotic shock, illustrating the relay’s rapid response. (porter2005acommondocking pages 1-2, dexter2015robustnetworkstructure pages 1-2)
YPD1 deletion or severe depletion removes phosphate delivery to Ssk1 and causes inappropriate HOG activation. The resulting lethality is pathway-based rather than evidence for a constitutive housekeeping reaction: comparative and genetic evidence associates loss of YPD1 or SLN1 with constitutive HOG signaling, and Ypd1 underexpression produces a clear growth defect. (mavrianos2014twocomponenthistidinephosphotransfer pages 7-7, dexter2015robustnetworkstructure pages 7-8)
Ypd1 also transfers phosphate to Skn7, a predominantly nuclear response regulator and transcription factor. This branch contributes to cell-wall biosynthesis/stress responses and cell-cycle-associated regulation. It is mechanistically distinct from the Ssk1-HOG branch: Ypd1 is the common bifurcation component, but Skn7 acts primarily through transcriptional regulation rather than initiating the Ssk2/Ssk22–Pbs2–Hog1 cascade. (lu2003saccharomycescerevisiaehistidine pages 1-3, porter2005acommondocking pages 1-2)
Oxidative-stress regulation involving Skn7 is more nuanced: Skn7 participates in antioxidant responses, but not every oxidative-stress output necessarily requires its Sln1-dependent receiver phosphorylation. Accordingly, Ypd1 should be annotated confidently for Sln1-dependent Skn7 phosphotransfer, but not as the sole conduit for all Skn7 oxidative-stress functions. (kennedy2019roleofthe pages 1-2, mavrianos2014twocomponenthistidinephosphotransfer pages 1-2)
Ypd1 is a soluble intracellular protein detected in both cytosol and nucleus. GFP and tandem-GFP fusion microscopy, including confocal imaging with nuclear DNA staining in a ypd1Δ replacement background, supported nucleocytoplasmic distribution. This localization is mechanistically appropriate: Sln1 is membrane-associated, Ssk1 is cytosolic, and Skn7 is predominantly nuclear. (lu2003saccharomycescerevisiaehistidine pages 1-3)
The influential 2003 interpretation is that Ypd1 shuttles between nucleus and cytoplasm to phosphorylate both Ssk1 and Skn7. No obvious stress-dependent relocalization of Ssk1 or Skn7 was observed. A later engineering study did not detect marked nuclear accumulation of GFP-Ypd1 and questioned whether active shuttling was required. The conservative current annotation is therefore nuclear and cytosolic localization permitting compartment-spanning phosphotransfer; regulated or directional shuttling is plausible but less firmly established than dual-compartment presence. (lu2003saccharomycescerevisiaehistidine pages 1-3, bury2018designcharacterizationand pages 7-8)
X-ray crystallography shows an all-helical HPt fold centered on a four-helix bundle, with His64 solvent-exposed. Structures of the Ypd1–Sln1 receiver-domain complex were solved in two crystal forms at 2.1 and 2.3 Å resolution. The complex positions Ypd1 His64 near Sln1 Asp1144; modeling His64 into its conserved rotamer and adding the required Mg²⁺ yields geometry compatible with direct His–Asp transfer without large backbone rearrangements. (xu2003theyeastypd1sln1 pages 1-2, xu2003theyeastypd1sln1 pages 9-11)
The principal partner-binding region is a largely hydrophobic patch between His64 and helix A, estimated at approximately 690 Ų, surrounded by polar and charged residues. Alanine scanning and yeast two-hybrid experiments identified a common docking region used by Sln1-R1, Ssk1-R2, and Skn7-R3: ten Ypd1 surface residues contributed to interaction with all three domains, while peripheral residues appeared to tune partner specificity. Eight of the ten core residues also contacted Sln1-R1 in the crystal structure. (xu2003theyeastypd1sln1 pages 1-2, porter2005acommondocking pages 6-7)
His64-adjacent residues are important for catalytic geometry. N61 and K67 help stabilize/position the active-site region; K67 and R90 contact Sln1-R1 in the phosphoryl-analog complex. Substitution of conserved Gly68, four residues after His64, with bulky, hydrophobic, or charged residues nearly abolished phosphate acceptance from Sln1-R1 while causing only modest affinity changes. This indicates failure to form a productive transition-state geometry rather than simple loss of binding. (kennedy2019roleofthe pages 1-2)
The common hydrophobic docking site explains how one small HPt protein recognizes three homologous receiver domains, while less-conserved peripheral electrostatic and loop contacts provide discrimination. Only about 11.5% of Ypd1’s surface was buried in the Sln1-R1 complex, consistent with a transient signaling complex, yet the interface showed high shape complementarity. (porter2005acommondocking pages 6-7)
Ypd1 is not merely a passive wire. Mathematical modeling and controlled expression experiments indicate that a relatively large cellular pool of Ypd1 buffers fluctuations in Sln1, Ssk1, and relay flux, preventing accidental HOG activation under normal conditions. Moderate expression perturbations were tolerated, whereas Ypd1 depletion caused inappropriate pathway activation and toxicity. (dexter2015robustnetworkstructure pages 1-2, dexter2015robustnetworkstructure pages 7-8)
The 2015 experiments used inducible single-copy alleles and high-copy 2μ plasmids estimated at 15–50 copies per cell. Massive Ypd1 overexpression did not produce the growth defect seen with strong Sln1 or Ssk1 overexpression; conversely, low Ypd1 expression caused growth defects at 0–5 nM inducer. These findings support an expert interpretation of Ypd1 as an excess intermediate/buffer whose abundance makes HOG repression robust until its free pool is depleted. (dexter2015robustnetworkstructure pages 7-8)
This architecture provides a potential evolutionary advantage over a simple two-component circuit: an intermediate present in excess can absorb component-level fluctuations while still transmitting a rapid environmental signal. That conclusion combines experimental depletion/overexpression data with a biochemically constrained mathematical model and should be regarded as strongly supported systems-level interpretation rather than a separate catalytic function. (dexter2015robustnetworkstructure pages 1-2, dexter2015robustnetworkstructure pages 7-8)
Ypd1 has been exploited as the endogenous relay component in an optogenetic proof of concept. A blue-light-responsive LOV–Sln1 hybrid kinase altered ATP-dependent autophosphorylation and phosphate transfer to Ypd1. In yeast lacking native Sln1, illumination propagated through Ypd1 to alter downstream signaling, decreasing steady-state OCH1 reporter expression by about 40% and producing persistent Hog1 nuclear accumulation. This demonstrates that the Sln1–Ypd1 relay can couple engineered sensory inputs to native transcriptional and MAPK outputs. (bury2018designcharacterizationand pages 1-2)
This remains a laboratory implementation rather than an established industrial Ypd1 product. Its practical value lies in programmable stress signaling, studies of intracellular signal diffusion, and potential control of yeast gene expression. The study also reported up to approximately threefold light-induced Hog1 nuclear enrichment in selected cells, compared with up to fourfold following salt stress. (bury2018designcharacterizationand pages 7-8)
Fungal histidine-kinase/HPt systems are attractive antifungal targets because canonical His–Asp relays are absent from animals. However, most drug-target evidence concerns Ypd1 homologs in pathogenic fungi, not S288c Ypd1 itself. Differences in essentiality—including dispensability of YPD1 in C. albicans—show why results cannot be transferred uncritically across species. (mavrianos2014twocomponenthistidinephosphotransfer pages 1-2, mavrianos2014twocomponenthistidinephosphotransfer pages 7-7)
The search found no 2023–2024 primary study that overturns or substantially revises the direct mechanistic annotation of S288c Ypd1. Recent work has instead extended fungal HPt structural principles and examined broader HOG-network coordination. A July 2024 Communications Biology study analyzed recognition of fungal HPt proteins using receiver domains and HPts from other fungi; its findings support the continuing relevance of low-affinity, geometry-dependent receiver–HPt recognition, but they are comparative evidence, not direct experiments on Q07688. DOI: https://doi.org/10.1038/s42003-024-06459-0.
A 2024 study of yeast MAPK cross-talk confirms the contemporary importance of the Sln1 and Sho1 branches in coordinating osmotic responses, but focuses on downstream MAPK sharing rather than revising Ypd1’s biochemical role. DOI: https://doi.org/10.1091/mbc.e24-06-0270. Consequently, precise foundational studies from 1999–2019 remain the authoritative sources for Ypd1’s catalytic residue, structure, localization, and partner specificity.
High-confidence molecular function: histidine-containing phosphotransfer intermediate in the Sln1 phosphorelay; accepts phosphate on His64 from Sln1-Asp1144 and donates it to Ssk1 or Skn7 receiver domains. This is supported by genetics, mutagenesis, in-vitro transfer, and structural complexes. (kennedy2019roleofthe pages 1-2, kennedy2016thebiochemicalcharacterization pages 36-41, xu2003theyeastypd1sln1 pages 1-2)
High-confidence biological processes: negative control of basal HOG signaling through Ssk1 phosphorylation; activation of osmoadaptation when relay flux falls; Sln1-dependent Skn7 regulation associated with cell-wall and cell-cycle outputs. (lu2003saccharomycescerevisiaehistidine pages 1-3, porter2005acommondocking pages 1-2, dexter2015robustnetworkstructure pages 1-2)
High-confidence localization: cytosol and nucleus. Moderate-confidence refinement: dynamic nucleocytoplasmic shuttling, because dual localization is direct but later imaging did not show conspicuous nuclear accumulation. (lu2003saccharomycescerevisiaehistidine pages 1-3, bury2018designcharacterizationand pages 7-8)
High-confidence structural annotation: soluble four-helix HPt fold with exposed His64 and a shared hydrophobic response-regulator docking surface. (xu2003theyeastypd1sln1 pages 1-2, porter2005acommondocking pages 6-7)
Overall conclusion: Ypd1 is the central mobile phosphohistidine branch point connecting the membrane Sln1 sensor to cytosolic Ssk1/HOG control and nuclear Skn7 regulation. Its essentiality arises primarily from preventing constitutive, toxic HOG activation under non-stress conditions, while its excess cellular pool makes that repression robust to fluctuations. Its dual-compartment distribution and reusable receiver-domain interface are integral to its signaling role rather than secondary pleiotropic features. (mavrianos2014twocomponenthistidinephosphotransfer pages 7-7, lu2003saccharomycescerevisiaehistidine pages 1-3, dexter2015robustnetworkstructure pages 1-2)
References
(xu2001thestructureand pages 38-41): Q Xu. The structure and function of ypd1, a histidine-containing phosphotransfer protein from yeast. Unknown journal, 2001.
(xu2003theyeastypd1sln1 pages 1-2): Qingping Xu, Stace W Porter, and Ann H West. The yeast ypd1/sln1 complex: insights into molecular recognition in two-component signaling systems. Structure, 11 12:1569-81, Dec 2003. URL: https://doi.org/10.1016/j.str.2003.10.016, doi:10.1016/j.str.2003.10.016. This article has 89 citations and is from a domain leading peer-reviewed journal.
(kennedy2016thebiochemicalcharacterization pages 36-41): E Kennedy. The biochemical characterization of two phosphorelay signaling proteins: ypd1 homologs from saccharomyces cerevisiae and cryptococcus neoformans. Unknown journal, 2016.
(kennedy2016thebiochemicalcharacterizationa pages 36-41): E Kennedy. The biochemical characterization of two phosphorelay signaling proteins: ypd1 homologs from saccharomyces cerevisiae and cryptococcus neoformans. Unknown journal, 2016.
(kennedy2019roleofthe pages 1-2): Emily N. Kennedy, Skyler D. Hebdon, Smita K. Menon, Clay A. Foster, Daniel M. Copeland, Qingping Xu, Fabiola Janiak-Spens, and Ann H. West. Role of the highly conserved g68 residue in the yeast phosphorelay protein ypd1: implications for interactions between histidine phosphotransfer (hpt) and response regulator proteins. BMC Biochemistry, Jan 2019. URL: https://doi.org/10.1186/s12858-019-0104-5, doi:10.1186/s12858-019-0104-5. This article has 6 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.
(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.
(porter2005acommondocking pages 1-2): Stace W. Porter and Ann H. West. A common docking site for response regulators on the yeast phosphorelay protein ypd1. Biochimica et biophysica acta, 1748 2:138-45, May 2005. URL: https://doi.org/10.1016/j.bbapap.2004.12.009, doi:10.1016/j.bbapap.2004.12.009. This article has 30 citations.
(xu2003theyeastypd1sln1 pages 9-11): Qingping Xu, Stace W Porter, and Ann H West. The yeast ypd1/sln1 complex: insights into molecular recognition in two-component signaling systems. Structure, 11 12:1569-81, Dec 2003. URL: https://doi.org/10.1016/j.str.2003.10.016, doi:10.1016/j.str.2003.10.016. This article has 89 citations and is from a domain leading peer-reviewed journal.
(porter2005acommondocking pages 6-7): Stace W. Porter and Ann H. West. A common docking site for response regulators on the yeast phosphorelay protein ypd1. Biochimica et biophysica acta, 1748 2:138-45, May 2005. URL: https://doi.org/10.1016/j.bbapap.2004.12.009, doi:10.1016/j.bbapap.2004.12.009. This article has 30 citations.
(bury2018designcharacterizationand pages 7-8): 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.
(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.
(mavrianos2014twocomponenthistidinephosphotransfer pages 1-2): John Mavrianos, Chirayu Desai, and Neeraj Chauhan. Two-component histidine phosphotransfer protein ypd1 is not essential for viability in candida albicans. Apr 2014. URL: https://doi.org/10.1128/ec.00243-13, doi:10.1128/ec.00243-13. This article has 42 citations and is from a peer-reviewed journal.
(mavrianos2014twocomponenthistidinephosphotransfer pages 7-7): John Mavrianos, Chirayu Desai, and Neeraj Chauhan. Two-component histidine phosphotransfer protein ypd1 is not essential for viability in candida albicans. Apr 2014. URL: https://doi.org/10.1128/ec.00243-13, doi:10.1128/ec.00243-13. This article has 42 citations and is from a peer-reviewed journal.
(dexter2015robustnetworkstructure pages 7-8): 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.
(bury2018designcharacterizationand pages 10-10): 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.