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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 correctly identified as Ste7, encoded by STE7/YDL159W in Saccharomyces cerevisiae S288c, UniProt P06784. The literature consistently identifies this protein as the central MAP kinase kinase (MAP2K/MEK) shared by the mating and filamentous/invasive-growth signaling pathways. This agrees with the supplied protein-kinase, ATP-binding, serine/threonine-kinase active-site, and Byr1-like catalytic-domain annotations. Papers about Ste7-like proteins in other fungi were excluded from the functional annotation.
Ste7 is best described as an ATP-dependent, dual-specificity MAPKK that is activated by the MAPKKK Ste11 and activates the MAPKs Fus3 and Kss1 through phosphorylation of their activation-loop threonine and tyrosine. In mating signaling, Ste7 functions in a Ste5-organized complex recruited to the plasma membrane and preferentially activates Fus3. In filamentous/invasive growth, it preferentially activates Kss1 and is much less dependent on Ste5. Thus, Ste7 is not simply a generic kinase relay: docking, scaffold-dependent localization, and allosteric substrate control determine which developmental program it activates. (maleri2004persistentactivationby pages 1-2, bardwell1996signalinginthe pages 1-2, good2009theste5scaffold pages 1-2)
| Annotation dimension | Best-supported conclusion | Key quantitative/detail | Evidence type and source/year |
|---|---|---|---|
| Identity | STE7 is the S. cerevisiae S288c locus YDL159W, encoding Ste7/P06784; literature identifies Ste7 as the MAPK kinase in the mating and filamentous-growth cascades. | Identifiers: STE7, YDL159W, UniProt P06784. | Supplied UniProt identity and pathway biochemistry; Bardwell et al., 1996 (bardwell1996signalinginthe pages 1-2) |
| Enzyme class and reaction | Ste7 is an ATP-dependent dual-specificity MAPK kinase (MAP2K/MEK) that phosphorylates threonine and tyrosine in target-MAPK activation loops. | ATP + MAPK → ADP + doubly phosphorylated MAPK; EC 2.7.12.2. | Genetic and biochemical evidence; Gartner et al., 1992; Bardwell et al., 1996 (bardwell1996signalinginthe pages 1-2, gartner1992signaltransductionin pages 1-2, gartner1992signaltransductionin pages 8-10) |
| Upstream activator | The MAPKKK Ste11 phosphorylates and activates Ste7, placing Ste7 in the middle tier of the Ste11→Ste7→MAPK cascade. | Reconstituted kinase-cascade evidence; activated Ste11 increases downstream MAPK phosphorylation. | In-vitro reconstitution and pathway biochemistry; Neiman and Herskowitz, 1994; Bardwell et al., 1996 (peter2007ste7variantsthat pages 120-125, bardwell1996signalinginthe pages 1-2) |
| Downstream substrates | The validated Ste7 substrates are the MAPKs Fus3 and Kss1; Ste7-dependent dual activation-loop phosphorylation activates them. | Fus3 sites: Thr180 and Tyr182; analogous threonine/tyrosine activation-loop phosphorylation activates Kss1. Mutation of either Fus3 site abolishes function in vivo. | Site-directed mutagenesis, phosphoanalysis, and genetics; Gartner et al., 1992 (gartner1992signaltransductionin pages 1-2, gartner1992signaltransductionin pages 8-10) |
| Substrate docking | Ste7 forms specific, high-affinity complexes with Fus3 and Kss1 through docking interactions outside its catalytic active site. | Approximate Kᴅ ≈ 5 nM for either MAPK; binding persists without Ste5 or Ste11. | Purified-protein binding and yeast-extract experiments; Bardwell et al., 1996 (bardwell1996signalinginthe pages 1-2) |
| Ste5-dependent spatial control | During pheromone signaling, Ste5 binds Ste11, Ste7, and Fus3 and is recruited through Gβ/Ste4 to the plasma membrane, spatially assembling the mating cascade. | Membrane recruitment places Ste7 between Ste11 and Fus3 at the signaling site. | Interaction, genetic, and reconstitution studies; Good et al., 2009 (good2009theste5scaffold pages 1-2) |
| Ste5-dependent catalytic specificity | Fus3 is intrinsically a poor Ste7 substrate, whereas Kss1 is efficient. The Ste5 minimal-scaffold/VWA domain acts as a substrate-specific cocatalyst that unlocks Fus3 for Ste7 phosphorylation. | Ste5-ms increases Ste7→Fus3 kcat by about 5,000-fold with little effect on Kₘ; Ste5-ms–Ste7 Kᴅ ≈ 75 nM; Ste7→Kss1 kinetics are largely unaffected. | Quantitative kinetics, binding, mutagenesis, and 1.6-Å structure; Good et al., 2009 (good2009theste5scaffold pages 1-2, good2009theste5scaffold pages 4-6) |
| Biological pathway outputs | In mating, scaffolded Ste7 primarily activates Fus3, supporting mating transcription, G1 arrest, shmoo growth, and cell fusion. In invasive or filamentous growth, Ste7 primarily activates Kss1 in a largely Ste5-independent branch. | Constitutively active Ste7 promotes Kss1-dependent invasive growth but does not reproduce Fus3-dependent mating. | Genetics, reporters, phosphorylation assays, and reconstitution; Maleri et al., 2004; Good et al., 2009 (maleri2004persistentactivationby pages 1-2, peter2007ste7variantsthat pages 82-86, good2009theste5scaffold pages 1-2) |
| Ubiquitin regulation | Pheromone induces Ste7 polyubiquitination. Ubp3 regulates this modification and limits pathway output; UBP3 deletion causes polyubiquitinated Ste7 accumulation and potentiated signaling. | Estimated abundance is about 2,000 Ste7 molecules per cell, versus about 5,000 each for Fus3 and Kss1; 15 UBP-disruption mutants were screened. | Mutant screen, immunoblotting, reporters, and cell-cycle assays; Wang and Dohlman, 2002; later SCF-Cdc4 analysis, 2013 (wang2002pheromonedependentubiquitinationof pages 1-2, wang2002pheromonedependentubiquitinationof pages 5-6) |
| 2023 chaperone development | Circuit-level, not direct Ste7 characterization: Ssa1/Ssa2 Hsp70 chaperones support Ste5 abundance, integrity, and localization; their loss reduces Fus3/Kss1 activation, linking scaffold proteostasis to the Ste7-containing module. | Single, double, and triple SSA-family mutants could still mate, indicating compensatory folding mechanisms. | Co-immunoprecipitation, microscopy, immunoblotting, and mating phenotypes; Farley et al., 18 October 2023 (farley2023effectsofhsp70 pages 1-2, farley2023effectsofhsp70 pages 7-8) |
| 2024 cross-talk development | Circuit-level, not direct Ste7 characterization: Sho1-mediated cross-talk operates through Kss1, which drives a transcriptional program distinct from Hog1 and Fus3. Ste7 remained pathway context rather than the principal manipulated variable. | RNA-seq threshold: absolute log₂ fold change of at least 1 and adjusted P no greater than 0.05; experiments used up to 550 mM KCl. | MAPK activation, live-cell translocation, and transcriptomics; Zhang et al., 1 October 2024 (zhang2024sharedandredundant pages 4-5, zhang2024sharedandredundant pages 1-2) |
| 2024 engineering application | Circuit-level application, not direct Ste7 characterization: an engineered yeast sender–receiver platform uses α-factor signaling through the native mating MAPK circuit as a molecular-communication and biosensor testbed. | About one output event per 2 h, RNA responses in less than 3 min, repeated 10 μM α-factor pulses, and 1:1 sender-to-receiver cocultures. | Engineered-cell experiments and mathematical modeling; Ntetsikas et al., January 2024 (ntetsikas2024engineeringyeastcells pages 1-2, ntetsikas2024engineeringyeastcells pages 13-15) |
Table: Evidence matrix for the verified S288c protein Ste7/P06784, integrating catalytic mechanism, pathway position, localization, regulation, quantitative biochemical data, and recent circuit-level developments. The 2023–2024 studies are distinguished from direct characterization of Ste7 itself.
The supplied record—STE7, ordered locus YDL159W, UniProt P06784, organism S. cerevisiae strain S288c—is internally consistent with the retrieved literature. An independent S. cerevisiae study explicitly lists STE7/YDL159W as a kinase in pheromone-induced signaling, while mechanistic studies identify yeast Ste7 as the MAPKK upstream of Fus3 and Kss1. Accordingly, the target is not the unrelated STE7/Ste7-like proteins described in Schizosaccharomyces, Candida, or filamentous fungi.
The UniProt description “serine/threonine-protein kinase” reflects Ste7’s membership in the protein-kinase superfamily, but its experimentally important biochemical classification is more specific: it is a dual-specificity MAPK kinase, because it installs both phosphothreonine and phosphotyrosine on MAPK activation loops. The catalytic-domain annotations supplied by the user—Byr1-like catalytic domain, kinase-like fold, protein-kinase ATP-binding region, and serine/threonine-kinase active site—are therefore fully compatible with its literature-defined MAP2K function. (bardwell1996signalinginthe pages 1-2, wang2002pheromonedependentubiquitinationof pages 1-2, gartner1992signaltransductionin pages 1-2)
Ste7 catalyzes phosphotransfer from ATP to protein hydroxyl groups:
ATP + MAPK → ADP + doubly phosphorylated MAPK.
Its validated physiological MAPK substrates are Fus3 and Kss1. Pheromone treatment rapidly induces threonine and tyrosine phosphorylation of both MAPKs. For Fus3, the experimentally defined activation sites are Thr180 and Tyr182; substitution of either residue caused complete loss of function in vivo. Catalytically inactive Fus3 was still phosphorylated, excluding MAPK autophosphorylation as the principal activation mechanism. Fus3 phosphorylation required STE7 and STE11 genetically, and subsequent biochemical work placed Ste7 directly between Ste11 and Fus3/Kss1. (bardwell1996signalinginthe pages 1-2, gartner1992signaltransductionin pages 1-2, gartner1992signaltransductionin pages 8-10)
Ste7 is therefore a dual-specificity kinase in terms of its substrate reaction, notwithstanding its sequence-level grouping with serine/threonine kinases. This is characteristic of MAP2Ks: Ste7 recognizes folded MAPKs and modifies the two activation-loop residues rather than functioning as a broadly promiscuous peptide kinase.
Ste7 binds Fus3 and Kss1 specifically and with high affinity—approximately 5 nM dissociation constant for either MAPK. The interaction occurs outside the catalytic active site and persists in extracts lacking Ste5 and Ste11, showing that direct MAPKK–MAPK docking does not require the scaffold or upstream kinase. Other yeast MAPKs, including Hog1 and Mpk1, did not detectably bind under the reported conditions. Mutations disrupting the Ste7 docking region reduced signaling, and biochemical experiments indicate that complex dissociation is needed to permit productive reciprocal phosphorylation. (bardwell1996signalinginthe pages 1-2)
This evidence supports a restricted primary substrate set: Fus3 and Kss1 are the established direct physiological substrates. Broader phenotypes should not be interpreted as evidence that Ste7 directly phosphorylates every downstream effector; most transcriptional and morphological effects are mediated through these MAPKs.
The core kinase relationship is:
Ste20 → Ste11 (MAPKKK) → Ste7 (MAPKK) → Fus3 and/or Kss1 (MAPKs).
Reconstitution and pathway studies establish Ste11 as the kinase immediately upstream of Ste7. Ste11 phosphorylation activates Ste7; active Ste7 then phosphorylates Fus3 or Kss1. Fus3 and Kss1 can subsequently phosphorylate Ste7 at regulatory sites, creating feedback rather than a strictly one-way linear relay. (maleri2004persistentactivationby pages 1-2, peter2007ste7variantsthat pages 120-125, bardwell1996signalinginthe pages 1-2)
Pheromone binding to Ste2 or Ste3 activates the heterotrimeric G-protein system, releasing Ste4–Ste18 (Gβγ). Gβγ recruits Ste5 and associated signaling components to the plasma membrane, where membrane-associated Ste20 activates Ste11. Ste5 binds Ste11, Ste7, and Fus3, organizing the Ste11→Ste7→Fus3 module. Activated Fus3 then controls mating transcription, G1 arrest, polarized “shmoo” growth, and cell fusion through downstream regulators such as Ste12 and Far1. (good2009theste5scaffold pages 1-2, wang2002pheromonedependentubiquitinationof pages 1-2, farley2023effectsofhsp70 pages 1-2)
Ste7 and Ste11 are also shared with the filamentous/invasive-growth pathway. Under poor nutrient conditions and other appropriate inputs, Ste7 principally activates Kss1, leading through Ste12/Tec1-regulated transcription to invasive growth in haploids and pseudohyphal growth in diploids. Unlike efficient Fus3 activation, Kss1 activation is substantially less dependent on Ste5. Constitutively active Ste7 preferentially produced Kss1 phosphorylation and invasive-growth transcription but failed to reproduce Fus3-dependent mating, experimentally demonstrating that Ste7 activity alone is insufficient to specify the mating fate. (maleri2004persistentactivationby pages 1-2, peter2007ste7variantsthat pages 82-86, good2009theste5scaffold pages 1-2)
Ste7 is not a membrane-spanning or secreted protein. Its most functionally important localization is transient recruitment to the cytoplasmic face of the plasma membrane as part of the Ste5 signaling complex during pheromone stimulation. Ste5 binds Ste7 and the other mating-cascade kinases and is recruited to membrane-associated Gβγ/Ste4. This colocalizes Ste7 with its upstream activator Ste11 and downstream substrate Fus3 at the site of receptor activation. (good2010theroleof pages 184-189, good2009theste5scaffold pages 1-2)
Available evidence supports a dynamic cytosolic/scaffold-associated kinase rather than an enzyme resident in one organelle. In the mating pathway, the plasma membrane is the key activation site; downstream Fus3 and Kss1 transmit the signal to nuclear and cytoplasmic effectors. For invasive-growth signaling, Ste7→Kss1 transmission can occur without the same strict Ste5-dependent membrane organization. Therefore, database labels such as “cytoplasmic” are not wrong but are mechanistically incomplete: stimulus-dependent scaffold recruitment is the important localization principle.
A major mechanistic insight is that Ste5 is more than a passive tether. Purified Fus3 is intrinsically a poor Ste7 substrate, whereas Kss1 is intrinsically efficient. A roughly 200-residue Ste5 minimal-scaffold domain, residues 593–786, binds Ste7 with a reported KD of approximately 75 nM and increases the kcat of Ste7-mediated Fus3 phosphorylation by about 5,000-fold, with little effect on KM. It has essentially no effect on Ste7-mediated Kss1 phosphorylation. (good2009theste5scaffold pages 1-2, good2009theste5scaffold pages 4-6)
The Ste5 domain consequently acts as a substrate-specific cocatalyst: it allosterically “unlocks” Fus3 so Ste7 can phosphorylate it efficiently. The structure of this Ste5 domain was solved at 1.6 Å resolution and displays a VWA-like fold. Direct Ste7–MAPK docking remains necessary, but simple physical proximity is insufficient to explain Fus3 activation. This is the strongest mechanistic explanation for why pheromone-activated, scaffold-bound Ste7 selects Fus3, whereas Ste7 used in the filamentation circuit readily activates Kss1. (good2009theste5scaffold pages 4-6)
Activated Fus3 and Kss1 phosphorylate Ste7 at regulatory sites, including multiple N-terminal sites and a site C-terminal to the catalytic domain. These events produce the characteristic hyperphosphorylated Ste7 forms seen after pathway activation and contribute to feedback control and pathway-specific behavior. Constitutively active Ste7 experiments distinguish this feedback phosphorylation from the Ste11-dependent activation-loop phosphorylation needed to turn on Ste7’s catalytic domain. (peter2007ste7variantsthat pages 95-101, maleri2004persistentactivationby pages 1-2)
Pheromone stimulation induces Ste7 polyubiquitination. A screen of 15 ubiquitin-specific protease disruption mutants identified Ubp3 as a selective regulator of the pheromone pathway. In ubp3Δ cells, polyubiquitinated Ste7 and free polyubiquitin chains accumulated, while MAPK activity, pheromone-induced transcription, and cell-cycle arrest were enhanced. Epistasis placed the effect downstream of Ste4 and Ste11 but upstream of Ste12, consistent with direct regulation at the Ste7/MAPK tier. (wang2002pheromonedependentubiquitinationof pages 1-2, wang2002pheromonedependentubiquitinationof pages 5-6)
Later work implicated SCF/Cdc4-mediated ubiquitination and a feedback circuit involving Fus3 and Ubp3 in maintaining signal strength and preventing inappropriate Kss1 activation. Thus ubiquitination is not merely bulk protein disposal: it helps determine mating-versus-invasive-growth specificity. (maleri2004persistentactivationby pages 1-2)
A useful abundance estimate from quantitative immunoblotting is approximately 2,000 Ste7 molecules per cell, compared with approximately 5,000 molecules each of Fus3 and Kss1. This lower abundance makes Ste7 a potentially limiting and sensitive regulatory node. (wang2002pheromonedependentubiquitinationof pages 5-6)
Loss of STE7 interrupts signal flow to both Fus3 and Kss1. In the mating program, this prevents normal pheromone-induced MAPK activation and consequently disrupts transcription, G1 arrest, polarized morphogenesis, and efficient mating. In the filamentation program, loss of Ste7 prevents normal Kss1 activation and invasive/pseudohyphal differentiation. These are pathway-proximal consequences and are more informative for annotation than broad secondary phenotypes.
Conversely, constitutively active Ste7 does not simply activate both outputs equally. Persistent Ste7 activity preferentially supports Kss1-mediated invasive growth and fails to support normal Fus3-dependent mating, emphasizing that signal duration, scaffolding, and substrate conformation—not kinase activity alone—determine fate. (maleri2004persistentactivationby pages 1-2, peter2007ste7variantsthat pages 82-86)
Direct molecular characterization of Ste7 itself is mature; the decisive catalytic, docking, and scaffold-mechanism experiments are foundational studies from 1992–2009. Recent work has instead examined how the Ste7-containing circuit is maintained, coordinated with other pathways, and engineered. These studies should not be misrepresented as discovering new direct Ste7 substrates.
Farley and colleagues reported that the Hsp70 chaperones Ssa1 and Ssa2 support Ste5 abundance, integrity, and localization. Loss of Ssa1/Ssa2 reduced Fus3 and Kss1 activation, FUS1 expression, and shmoo morphogenesis. Ste7 was part of the Ste5-bound kinase module rather than the directly manipulated protein. The work extends the model by showing that scaffold proteostasis controls efficient transmission through the Ste11–Ste7–MAPK cascade. Interestingly, various SSA single, double, and triple mutants retained some mating capability, indicating compensation within the chaperone network. Published 18 October 2023 in PLOS ONE; DOI/URL: https://doi.org/10.1371/journal.pone.0289339. (farley2023effectsofhsp70 pages 1-2, farley2023effectsofhsp70 pages 7-8)
Zhang and colleagues examined mating–HOG pathway cross-talk under pheromone and osmotic stress. The work confirmed the Ste5-directed Ste11–Ste7–Fus3 circuit as the mating module but principally manipulated HOG branches and Kss1. Sho1-mediated cross-talk depended on Kss1, and Kss1 initiated a transcriptional program distinct from those of Fus3 and Hog1. RNA-seq significance criteria included |log2 fold change| ≥1 and adjusted P≤0.05, and osmotic-response experiments used KCl concentrations up to 550 mM. Published 1 October 2024 in Molecular Biology of the Cell; DOI/URL: https://doi.org/10.1091/mbc.e24-06-0270. (zhang2024sharedandredundant pages 4-5, zhang2024sharedandredundant pages 1-2)
These results reinforce the current expert view that shared enzymes do not inevitably cause indiscriminate cross-talk: scaffolds, branch architecture, MAPK identity, localization, and transcriptional decoding jointly insulate outputs.
Ste7 itself is not a clinical target or commercial enzyme. Its principal application is as a mechanistically defined component of a model eukaryotic signaling system.
A 2024 engineered-yeast molecular-communication testbed used α-factor-secreting sender cells and mating-responsive receiver cells. Signal transmission necessarily traverses the native mating circuit containing Ste11, Ste7, and Fus3/Kss1, although STE7 was not directly engineered in the reported implementation. The system demonstrated repeated output events at approximately one event per two hours, while RNA fluctuations indicated responses in less than three minutes. Experiments included repeated 10 μM α-factor pulses and 1:1 sender-to-receiver cocultures. The authors propose this platform for yeast biosensors and interfaces to bio-nano communication networks. Published January 2024; DOI/URL: https://doi.org/10.48550/arXiv.2401.13712. (ntetsikas2024engineeringyeastcells pages 1-2, ntetsikas2024engineeringyeastcells pages 13-15)
Because Ste7 is a limiting, shared MAPKK with well-defined docking and scaffold interactions, it is a useful control point for engineering pathway gain, specificity, or cross-talk. In practice, however, altering Ste5 recruitment, MAPK docking, pheromone degradation, or transcriptional output may offer more selective control than simply overexpressing or constitutively activating STE7; persistent active Ste7 biases cells toward Kss1/invasive-growth signaling rather than faithfully reproducing mating. (maleri2004persistentactivationby pages 1-2, good2009theste5scaffold pages 4-6)
The Ste5–Ste11–Ste7–Fus3 system is an authoritative model for understanding mammalian scaffold-regulated RAF–MEK–ERK signaling. The most transferable principle is that scaffolds can control enzyme specificity allosterically, not only through colocalization. Extrapolation to human kinases should nevertheless remain conceptual: Ste7/P06784 is a yeast protein, and the cited experiments do not establish it as a human disease target.
The highest-confidence annotations are:
The principal uncertainty is not Ste7’s core function, which is well established, but the complete state-resolved map of its regulatory modifications and complexes in living cells. Recent studies increasingly treat Ste7 as part of an integrated signaling network rather than revisiting its basic enzymology. Consequently, older primary biochemical studies remain the authoritative sources for catalytic mechanism, while 2023–2024 publications chiefly update network context and applications.
References
(maleri2004persistentactivationby pages 1-2): Seth Maleri, Qingyuan Ge, Elizabeth A. Hackett, Yuqi Wang, Henrik G. Dohlman, and Beverly Errede. Persistent activation by constitutive ste7 promotes kss1-mediated invasive growth but fails to support fus3-dependent mating in yeast. Molecular and Cellular Biology, 24:9221-9238, Oct 2004. URL: https://doi.org/10.1128/mcb.24.20.9221-9238.2004, doi:10.1128/mcb.24.20.9221-9238.2004. This article has 84 citations and is from a domain leading peer-reviewed journal.
(bardwell1996signalinginthe pages 1-2): Lee Bardwell, Jeanette G. Cook, Ernie C. Chang, Bradley R. Cairns, and Jeremy Thorner. Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (map) kinases kss1 and fus3 with the upstream map kinase kinase ste7. Molecular and Cellular Biology, 16:3637-3650, Jul 1996. URL: https://doi.org/10.1128/mcb.16.7.3637, doi:10.1128/mcb.16.7.3637. This article has 217 citations and is from a domain leading peer-reviewed journal.
(good2009theste5scaffold pages 1-2): Matthew Good, Grace Tang, Julie Singleton, Attila Reményi, and Wendell A. Lim. The ste5 scaffold directs mating signaling by catalytically unlocking the fus3 map kinase for activation. Cell, 136:1085-1097, Mar 2009. URL: https://doi.org/10.1016/j.cell.2009.01.049, doi:10.1016/j.cell.2009.01.049. This article has 265 citations and is from a highest quality peer-reviewed journal.
(gartner1992signaltransductionin pages 1-2): A. Gartner, K. Nasmyth, and G. Ammerer. Signal transduction in saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of fus3 and kss1. Genes & development, 6 7:1280-92, Jul 1992. URL: https://doi.org/10.1101/gad.6.7.1280, doi:10.1101/gad.6.7.1280. This article has 375 citations and is from a highest quality peer-reviewed journal.
(gartner1992signaltransductionin pages 8-10): A. Gartner, K. Nasmyth, and G. Ammerer. Signal transduction in saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of fus3 and kss1. Genes & development, 6 7:1280-92, Jul 1992. URL: https://doi.org/10.1101/gad.6.7.1280, doi:10.1101/gad.6.7.1280. This article has 375 citations and is from a highest quality peer-reviewed journal.
(peter2007ste7variantsthat pages 120-125): Seth Peter Maleri. Ste7 variants that promote pathway specificity in s. cerevisiae. Text, 2007. URL: https://doi.org/10.17615/3rme-ma38, doi:10.17615/3rme-ma38. This article has 0 citations and is from a peer-reviewed journal.
(good2009theste5scaffold pages 4-6): Matthew Good, Grace Tang, Julie Singleton, Attila Reményi, and Wendell A. Lim. The ste5 scaffold directs mating signaling by catalytically unlocking the fus3 map kinase for activation. Cell, 136:1085-1097, Mar 2009. URL: https://doi.org/10.1016/j.cell.2009.01.049, doi:10.1016/j.cell.2009.01.049. This article has 265 citations and is from a highest quality peer-reviewed journal.
(peter2007ste7variantsthat pages 82-86): Seth Peter Maleri. Ste7 variants that promote pathway specificity in s. cerevisiae. Text, 2007. URL: https://doi.org/10.17615/3rme-ma38, doi:10.17615/3rme-ma38. This article has 0 citations and is from a peer-reviewed journal.
(wang2002pheromonedependentubiquitinationof pages 1-2): Yuqi Wang and Henrik G. Dohlman. Pheromone-dependent ubiquitination of the mitogen-activated protein kinase kinase ste7*. The Journal of Biological Chemistry, 277:15766-15772, May 2002. URL: https://doi.org/10.1074/jbc.m111733200, doi:10.1074/jbc.m111733200. This article has 59 citations.
(wang2002pheromonedependentubiquitinationof pages 5-6): Yuqi Wang and Henrik G. Dohlman. Pheromone-dependent ubiquitination of the mitogen-activated protein kinase kinase ste7*. The Journal of Biological Chemistry, 277:15766-15772, May 2002. URL: https://doi.org/10.1074/jbc.m111733200, doi:10.1074/jbc.m111733200. This article has 59 citations.
(farley2023effectsofhsp70 pages 1-2): Francis W. Farley, Ryan R. McCully, Paul B. Maslo, Lu Yu, Mark A. Sheff, Homayoun Sadeghi, and Elaine A. Elion. Effects of hsp70 chaperones ssa1 and ssa2 on ste5 scaffold and the mating mitogen-activated protein kinase (mapk) pathway in saccharomyces cerevisiae. PLOS ONE, 18:e0289339, Oct 2023. URL: https://doi.org/10.1371/journal.pone.0289339, doi:10.1371/journal.pone.0289339. This article has 2 citations and is from a peer-reviewed journal.
(farley2023effectsofhsp70 pages 7-8): Francis W. Farley, Ryan R. McCully, Paul B. Maslo, Lu Yu, Mark A. Sheff, Homayoun Sadeghi, and Elaine A. Elion. Effects of hsp70 chaperones ssa1 and ssa2 on ste5 scaffold and the mating mitogen-activated protein kinase (mapk) pathway in saccharomyces cerevisiae. PLOS ONE, 18:e0289339, Oct 2023. URL: https://doi.org/10.1371/journal.pone.0289339, doi:10.1371/journal.pone.0289339. This article has 2 citations and is from a peer-reviewed journal.
(zhang2024sharedandredundant pages 4-5): Shu Zhang, Hao Wang, Emily L. Sipko, Shuang Li, Timothy A. Daugird, Wesley R. Legant, and Henrik G. Dohlman. Shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Molecular Biology of the Cell, Oct 2024. URL: https://doi.org/10.1091/mbc.e24-06-0270, doi:10.1091/mbc.e24-06-0270. This article has 6 citations and is from a domain leading peer-reviewed journal.
(zhang2024sharedandredundant pages 1-2): Shu Zhang, Hao Wang, Emily L. Sipko, Shuang Li, Timothy A. Daugird, Wesley R. Legant, and Henrik G. Dohlman. Shared and redundant proteins coordinate signal cross-talk between mapk pathways in yeast. Molecular Biology of the Cell, Oct 2024. URL: https://doi.org/10.1091/mbc.e24-06-0270, doi:10.1091/mbc.e24-06-0270. This article has 6 citations and is from a domain leading peer-reviewed journal.
(ntetsikas2024engineeringyeastcells pages 1-2): Nikolaos Ntetsikas, Styliana Kyriakoudi, Antonis Kirmizis, Bige Deniz Unluturk, Andreas Pitsillides, Ian F. Akyildiz, and Marios Lestas. Engineering yeast cells to facilitate information exchange. IEEE Transactions on Molecular, Biological and Multi-Scale Communications, 10:2-20, Jan 2024. URL: https://doi.org/10.48550/arxiv.2401.13712, doi:10.48550/arxiv.2401.13712. This article has 9 citations.
(ntetsikas2024engineeringyeastcells pages 13-15): Nikolaos Ntetsikas, Styliana Kyriakoudi, Antonis Kirmizis, Bige Deniz Unluturk, Andreas Pitsillides, Ian F. Akyildiz, and Marios Lestas. Engineering yeast cells to facilitate information exchange. IEEE Transactions on Molecular, Biological and Multi-Scale Communications, 10:2-20, Jan 2024. URL: https://doi.org/10.48550/arxiv.2401.13712, doi:10.48550/arxiv.2401.13712. This article has 9 citations.
(good2010theroleof pages 184-189): MC Good. The role of docking and scaffolding interactions in the spatiotemporal control of map kinase signaling. Unknown journal, 2010.
(peter2007ste7variantsthat pages 95-101): Seth Peter Maleri. Ste7 variants that promote pathway specificity in s. cerevisiae. Text, 2007. URL: https://doi.org/10.17615/3rme-ma38, doi:10.17615/3rme-ma38. This article has 0 citations and is from a peer-reviewed journal.