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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 target is correctly identified. FUS3/DAC2 (YBL016W; UniProt P16892) in Saccharomyces cerevisiae S288c is the mating-response mitogen-activated protein kinase Fus3, a CMGC-family Ser/Thr protein kinase. Its primary function is to convert pheromone-receptor activation into coordinated phosphorylation of nuclear, cytoplasmic, and cortical proteins. This drives mating-gene transcription, G1 arrest, polarized growth and partner-directed chemotropism while suppressing inappropriate filamentous-growth signaling. The literature’s placement of Fus3 downstream of Ste11 and Ste7, activation through its conserved TEY loop, and use of MAPK docking interactions agree with the supplied protein-kinase/MAPK domain annotations. No results concerning same-named or homologous proteins in other organisms were used to assign function to P16892. (kusari2004aconservedprotein pages 1-2, schwartz2005signalingspecificityin pages 26-31, zhang2024sharedandredundant pages 1-2)
| Annotation dimension | Best-supported conclusion | Key experiment / quantitative datum | Evidence strength | Source / date / DOI URL |
|---|---|---|---|---|
| Identity and family | FUS3/P16892 is the Saccharomyces cerevisiae mating-pathway MAP kinase, consistent with locus YBL016W and a CMGC Ser/Thr protein-kinase/MAPK domain. It functions in the Ste11–Ste7–Fus3 module assembled by Ste5. | Genetic, biochemical, and pathway studies consistently identify Fus3 as the mating-specific MAPK downstream of Ste7; conserved MAPK docking-region mutations impair activation and mating. | Very strong | Kusari et al., January 2004, 10.1083/jcb.200310021 (kusari2004aconservedprotein pages 1-2); Zhang et al., July 31, 2024 online, 10.1091/mbc.E24-06-0270 (zhang2024sharedandredundant pages 1-2) |
| Catalytic activation | Ste7 activates Fus3 by dual phosphorylation of the canonical TEY activation loop at Thr180 and Tyr182; activated Fus3 transfers phosphate from ATP to Ser/Thr residues in protein substrates. | The nonphosphorylatable Fus3-T180A/Y182A-GFP reporter fails to show phosphorylation-dependent nuclear retention; pathway studies place Ste7 directly upstream of Fus3. | Very strong | Blackwell et al., October 26, 2007, 10.1186/1471-2121-8-44 (blackwell2007thepheromoneinducednuclear pages 1-2); Schwartz and Madhani, 2005 evidence summary (schwartz2005signalingspecificityin pages 26-31) |
| Ste7 recognition | Fus3 forms a specific, high-affinity complex with its MAP2K Ste7; docking contributes substantially to efficient activation and pathway specificity. | Interaction of Fus3 and Ste7 was reconstituted without other yeast proteins, with an estimated Kd of approximately 5 nM; conserved CD/7m docking-site mutations reduce Ste7-dependent phosphorylation in vivo. | Very strong | Bardwell et al., July 1996, 10.1128/MCB.16.7.3637 (bardwell1996signalinginthe pages 1-2); Kusari et al., January 2004, 10.1083/jcb.200310021 (kusari2004aconservedprotein pages 1-2) |
| Far1 and cell-cycle arrest | Fus3 phosphorylates Far1, coupling pheromone detection to inhibition of G1 cyclin–CDK activity and mating-associated G1 arrest; Far1 also connects signaling to polarity machinery. | Genetic and biochemical pathway studies identify Far1 as a Fus3-selective effector whose activation is required for efficient arrest and mating-projection formation. | Strong | Bardwell et al., July 1996, 10.1128/MCB.16.7.3637 (bardwell1996signalinginthe pages 1-2); Maleri, 2007, 10.17615/3rme-ma38 (peter2007ste7variantsthat pages 125-129, peter2007ste7variantsthat pages 38-44) |
| Ste12, Dig1, and Dig2 | Nuclear Fus3 regulates mating-gene transcription through Ste12 and the Ste12-associated repressors Dig1/Dig2. These proteins are signaling targets or partners and retention factors for active Fus3. | Loss of DIG1 or DIG2 reduces pheromone-induced Fus3-GFP nuclear accumulation; Ste12 overexpression increases accumulation of wild-type but not Fus3-T180A/Y182A-GFP. | Strong | Blackwell et al., October 26, 2007, 10.1186/1471-2121-8-44 (blackwell2007thepheromoneinducednuclear pages 1-2); Kusari et al., January 2004, 10.1083/jcb.200310021 (kusari2004aconservedprotein pages 1-2) |
| Tec1 and pathway insulation | Fus3 phosphorylates the filamentation transcription factor Tec1, triggering SCF–Cdc4-dependent ubiquitylation and degradation. This prevents pheromone-activated shared components from erroneously inducing filamentous-growth genes. | Tec1 destruction requires phosphorylation at T273 and T276; high-affinity Cdc4 binding requires both phosphates, and both sites are important for pheromone-induced proteolysis in vivo. | Very strong | Bao et al., January 2010, 10.1128/EC.00250-09 (bao2010multisitephosphorylationof pages 1-2) |
| Subcellular localization | Fus3 is present in both cytoplasm and nucleus in proliferating cells, with slight basal nuclear enrichment. Pheromone increases nuclear accumulation, while Ste5 and Gpa1 interactions position signaling at the plasma membrane, cell cortex, and mating projection. | Fus3-GFP nuclear-to-cytoplasmic fluorescence ratios typically range from 1.6 to 2.0; Dig1/Dig2 and phosphorylation promote nuclear retention, whereas Msg5 phosphatase antagonizes it. | Strong | Blackwell et al., October 26, 2007, 10.1186/1471-2121-8-44 (blackwell2007thepheromoneinducednuclear pages 1-2); Gpa1/Ste5 localization evidence (sharmeen2020molecularroleofa pages 38-42) |
| Signaling dynamics | Fus3 activation is sustained and strongly scaffold-dependent rather than simply mirroring the faster, graded Kss1 response. Stimulus dose changes activation kinetics, and supersensitive mutants respond rapidly at lower pheromone concentrations. | A Fus3-specific kinase-translocation reporter showed rapid, sustained activation at 3 micromolar pheromone but slower activation at 0.3 micromolar in wild type; in bar1Δ and gpa1-G302S cells, both doses produced a sharp increase within 10 minutes. | Strong | Shellhammer et al., August 2019, 10.1002/yea.3395 (shellhammer2019quantitativeanalysisof pages 17-19, shellhammer2019quantitativeanalysisof pages 20-22) |
| Morphogenesis and gradient tracking | Fus3 has specialized spatial functions not fully replaceable by Kss1: its interaction with Gα/Gpa1 is needed for accurate pheromone-gradient tracking, morphogenesis, and reduced cell-to-cell fate variability. | Mutational analysis separating Fus3 catalytic state and Gpa1 binding showed that inactive Fus3 can inhibit chemotropism, whereas Gpa1-bound active Fus3 supports gradient tracking and robust fate selection. | Strong | Errede et al., July 15, 2015 online, 10.1091/mbc.E15-03-0176 (errede2015pheromoneinducedmorphogenesisand pages 1-2) |
| 2024 pathway crosstalk | Recent work reinforces Fus3 as the insulated mating-specific MAPK: during concurrent osmotic and pheromone signaling, cross-pathway communication is mediated principally by Sho1 and shared MAPK Kss1 rather than by osmotic activation of Fus3. | Phos-tag immunoblotting, live-cell translocation imaging, reporters, and RNA-seq were applied after 350 mM KCl, with transcriptomes sampled at 15 minutes. Salt-induced mating-gene expression in an ssk1Δ background depended on Kss1; osmotic pressure did not activate Fus3. | Strong and recent | Zhang et al., received June 25 and published online July 31, 2024, 10.1091/mbc.E24-06-0270 (zhang2024sharedandredundant pages 2-4, zhang2024sharedandredundant pages 1-2) |
| Synthetic rewiring | Fus3 can be redirected to non-native targets when kinase and substrate carry compatible docking modules and the engineered substrate contains a phosphorylatable motif that recruits a downstream effector, such as ubiquitin-dependent degradation machinery. | Engineered docking interactions plus phosphorylation-activated degrons enabled Fus3 to control degradation of novel targets and predictably reshape yeast responses to mating pheromone. | Strong proof of concept | Groves et al., August 15, 2016, 10.7554/eLife.15200 (groves2016rewiringmapkinases pages 1-2) |
Table: Compact evidence table for S. cerevisiae FUS3/P16892 covering identity, activation, substrates, localization, signaling dynamics, recent pathway-crosstalk research, and synthetic rewiring. Findings from Fus3-like proteins in other organisms are excluded.
The evidence consistently identifies budding-yeast Fus3 as the mating-pathway MAPK in the Ste11–Ste7–Fus3 three-tier kinase module. Ste5 binds the three tiers and organizes Fus3 activation in response to mating pheromone. This agrees with the supplied identifiers FUS3/DAC2, YBL016W and P16892 and with the annotated kinase-like, protein-kinase, MAPK and MAPK-signature domains. (kusari2004aconservedprotein pages 1-2, zhang2024sharedandredundant pages 1-2)
Fus3 is closely related functionally to Kss1, but they should not be treated as interchangeable. Both can be activated during pheromone signaling, whereas Fus3 is specialized for mating, and Kss1 has a major role in filamentous growth and certain shared-pathway responses. Ste5-dependent activation, Fus3-specific substrates and spatial interactions provide specificity despite overlap between the two MAPKs. (peter2007ste7variantsthat pages 125-129, shellhammer2019quantitativeanalysisof pages 20-22, errede2015pheromoneinducedmorphogenesisand pages 1-2)
Fus3 is an ATP-dependent protein Ser/Thr kinase. Its generic reaction is:
ATP + protein Ser/Thr–OH → ADP + protein Ser/Thr–O-phosphate.
As for other MAPKs, the local Ser/Thr-Pro phosphoacceptor motif is only part of specificity. Productive phosphorylation also depends heavily on docking interactions, scaffold-mediated colocalization and cellular compartment. Fus3’s conserved CD/7m docking region binds regulators and substrates including Ste7, Ste5 and Dig proteins; mutations in that region disrupt partner binding, reduce Ste7-dependent phosphorylation and impair pheromone response and mating. (kusari2004aconservedprotein pages 1-2)
The MAP2K Ste7 activates Fus3 through dual phosphorylation of Thr180 and Tyr182 in the TEY activation loop. A T180A/Y182A Fus3 reporter lacks phosphorylation-dependent nuclear retention, providing functional confirmation of these residues. Ste7 and Fus3 also form a highly specific complex in vitro and in extracts, with an estimated dissociation constant of approximately 5 nM; Hog1, Mpk1 and mammalian ERK2 did not detectably substitute in that binding assay. (bardwell1996signalinginthe pages 1-2, blackwell2007thepheromoneinducednuclear pages 1-2)
This strong interaction is not simply constitutive catalysis: docking and subsequent rearrangement or dissociation help coordinate productive phosphorylation. Ste5 adds a second specificity layer by assembling Ste11, Ste7 and Fus3 at the pheromone-responsive cortex. (kusari2004aconservedprotein pages 1-2, bardwell1996signalinginthe pages 1-2)
The pathway can be summarized as follows:
Fus3 therefore is not merely a transcriptional kinase. It is the central signaling integrator that synchronizes cell-cycle withdrawal with preparation of the mating projection and orientation toward a compatible partner.
Far1 is a particularly important Fus3 effector and is more selective for Fus3 than for Kss1. Fus3-dependent phosphorylation of Far1 couples pheromone signaling to inhibition of G1 cyclin–CDK activity, allowing arrest before mating. Far1 also links receptor signaling to Cdc42 polarity machinery, helping coordinate arrest with projection formation. (peter2007ste7variantsthat pages 125-129, bardwell1996signalinginthe pages 1-2, peter2007ste7variantsthat pages 38-44)
Fus3 regulates the Ste12 transcriptional system and its repressors Dig1 and Dig2. These interactions relieve repression and promote expression of pheromone-responsive genes. The conserved Fus3 docking surface binds Dig1 and Dig2, while mutations that disturb these interactions produce mating-response defects. (kusari2004aconservedprotein pages 1-2)
The proteins also act as nuclear tethers. Deleting DIG1 or DIG2 reduces pheromone-induced accumulation of Fus3-GFP in the nucleus, and Ste12 overexpression causes hyperaccumulation of wild-type Fus3-GFP but not nonphosphorylatable Fus3-T180A/Y182A-GFP. Thus, substrate/partner binding and localization are mechanistically coupled. (blackwell2007thepheromoneinducednuclear pages 1-2)
One of the clearest demonstrations of Fus3 specificity is phosphorylation of Tec1, the transcription factor driving filamentous-growth genes. Fus3-dependent phosphorylation marks Tec1 for SCF–Cdc4-mediated ubiquitylation and proteolysis, preventing pheromone-activated shared components from triggering the wrong developmental program. (peter2007ste7variantsthat pages 182-186, bao2010multisitephosphorylationof pages 1-2)
Tec1 destruction requires a biphosphorylated degron involving T273 and T276. Both phosphates are needed for high-affinity binding to recombinant Cdc4, and both sites and Cdc4’s conserved basic pocket are important for pheromone-induced Tec1 degradation in vivo. Active Fus3 can phosphorylate several Tec1 sites in vitro; the evidence is strongest that Fus3 initiates the Tec1 phosphodegron pathway, although the detailed division of labor in generating both degron phosphates has historically required careful interpretation. (bao2010multisitephosphorylationof pages 1-2)
Bni1, Gβ and Ste5 have been implicated as cortical Fus3 targets that influence polarized growth and feedback. The evidence summarized here is less definitive than for Far1 or Tec1, so these are best regarded as supported pathway targets rather than the sole determinants of Fus3 output. Fus3–Gpa1 binding itself is especially important: perturbing it impairs morphogenesis and gradient tracking even when broader pathway activation remains possible. (sharmeen2020molecularroleofa pages 38-42, blackwell2007thepheromoneinducednuclear pages 1-2, errede2015pheromoneinducedmorphogenesisand pages 1-2)
Nuclear Fus3 activates the Ste12-centered transcriptional response, inducing genes required for pheromone communication, adhesion, polarized growth and cell fusion. This output depends on both catalytic activity and interactions with transcriptional regulators. (kusari2004aconservedprotein pages 1-2, blackwell2007thepheromoneinducednuclear pages 1-2)
Through Far1, Fus3 imposes G1 arrest so mating cells do not enter another mitotic cycle while preparing for fusion. Loss of Fus3 can be partly compensated by Kss1 for some transcriptional outputs, but efficient arrest and mating exhibit stronger Fus3 dependence. (peter2007ste7variantsthat pages 125-129, bardwell1996signalinginthe pages 1-2)
Fus3 helps generate the shmoo and orient growth up a pheromone gradient. Errede and colleagues showed that Fus3’s interaction with Gα/Gpa1 has state-dependent effects: inactive Gpa1-bound Fus3 can inhibit chemotropic transition, whereas catalytically active Gpa1-bound Fus3 is required for accurate gradient tracking and suppresses cell-to-cell variability between mating and chemotropic fates. This demonstrates that Fus3 specificity is encoded not only by catalytic preference but also by interaction state and location. The study was published online July 15, 2015; DOI: https://doi.org/10.1091/mbc.E15-03-0176. (errede2015pheromoneinducedmorphogenesisand pages 1-2)
Fus3 suppresses filamentous-growth output through Tec1 degradation. This negative branch is biologically important because the mating and filamentation pathways share Ste11, Ste7, Ste12 and, under some conditions, Kss1. Thus, Fus3 simultaneously promotes the desired mating program and eliminates a key transcription factor for the competing program. (peter2007ste7variantsthat pages 182-186, bao2010multisitephosphorylationof pages 1-2)
Fus3 is intracellular and dynamically partitioned rather than confined to one organelle.
Quantitative Fus3-GFP imaging found nuclear-to-cytoplasmic fluorescence ratios generally around 1.6–2.0. Although numerically modest, these shifts correlate with pheromone responsiveness: resistant cells show lower ratios, hypersensitive cells higher ratios, and nuclear enrichment declines during adaptation and cell-cycle re-entry. FRAP/FLIP evidence did not support major pheromone-regulated changes in active nuclear import or export, favoring altered binding to cytoplasmic and nuclear tethers as the principal mechanism. Blackwell et al. was published October 26, 2007; DOI: https://doi.org/10.1186/1471-2121-8-44. (blackwell2007thepheromoneinducednuclear pages 1-2)
Fus3 and Kss1 encode different temporal and dose-response properties. Fus3 activation tends to rise at a relatively constant rate and has a steeper, more switch-like dose response, whereas Kss1 activation is faster, transient and more graded. Disrupting Fus3–Ste5 binding makes Fus3 signaling more Kss1-like and compromises polarized expansion toward pheromone gradients, supporting an expert model in which the scaffold specifies dynamics as well as pathway membership. (shellhammer2019quantitativeanalysisof pages 20-22)
A Fus3-specific kinase-translocation reporter measured activity in single cells under microfluidic stimulation. In wild-type cells, 3 μM pheromone produced rapid, sustained activation, while 0.3 μM produced a slower increase. In supersensitive bar1Δ and gpa1-G302S strains, both doses caused a sharp increase within approximately 10 minutes, indicating saturation at 0.3 μM. The reporter preferentially measured Fus3 rather than Kss1 and was fast and reversible, although it reports substrate phosphorylation rather than endogenous Fus3 localization. Shellhammer et al. was published in August 2019; DOI: https://doi.org/10.1002/yea.3395. (shellhammer2019quantitativeanalysisof pages 17-19)
Methodologically, conventional phospho-p44/42 antibodies can detect both mono- and dually phosphorylated Fus3. Because monophosphorylated Fus3 may inhibit downstream signaling, Phos-tag separation is preferable when the exact activation state matters. GFP transcriptional reporters also introduce maturation delays of up to approximately 45 minutes, whereas enzymatic or translocation reporters can provide different dynamic ranges and temporal resolution. (shellhammer2019quantitativeanalysisof pages 19-20)
The strongest directly relevant 2024 study did not overturn the established Fus3 annotation; instead, it refined understanding of pathway insulation during simultaneous environmental inputs. Zhang et al. combined Phos-tag immunoblotting, live-cell MAPK translocation, reporter assays and RNA sequencing to examine concurrent salt and pheromone stimulation. The study was received June 25, accepted July 25 and published online July 31, 2024; DOI: https://doi.org/10.1091/mbc.E24-06-0270. (zhang2024sharedandredundant pages 2-4, zhang2024sharedandredundant pages 1-2)
The authors found that osmotic pressure and pheromone converge principally through Kss1, not Fus3. Fus3 remained the pheromone-specific MAPK, while the Sho1 branch of the HOG pathway activated Kss1 and could partially induce mating-associated transcripts when Sln1 signaling was absent. The transcriptomic experiment used 350 mM KCl and a 15-minute sampling point; differentially expressed genes were defined using log2 fold change greater than 1 and adjusted P below 0.05. In the relevant ssk1Δ condition, 48 salt-induced genes were enriched for mating-related processes, and five of 881 salt-induced transcripts were among the ten genes most strongly induced by pheromone. (zhang2024sharedandredundant pages 2-4)
This recent result strengthens a network-level interpretation: specificity is not created by an absolutely isolated linear chain. It emerges from scaffolds, MAPK-specific docking, transcription-factor destruction, localization and differential use of Kss1. Fus3 is insulated from osmotic activation even though Ste11 and other machinery are shared. (zhang2024sharedandredundant pages 1-2)
No 2023–2024 primary study found in this search provided a more authoritative revision of Fus3’s catalytic reaction, activation-loop residues or principal substrates. Some recent papers use “Fus3” for homologous kinases in other fungi; those were excluded because they do not concern P16892/YBL016W.
The Fus3 pathway is widely implemented as an experimental model for GPCR-to-MAPK signaling. Current tools include phospho-immunoblotting, Phos-tag electrophoresis, FRET, Fus3-specific kinase-translocation reporters, flow/imaging cytometry and microfluidic pheromone gradients. These permit measurements of activation state, spatial gradients, transcription, morphology, cell-cycle progression and chemotropic accuracy at population and single-cell scales. (shellhammer2019quantitativeanalysisof pages 19-20, shellhammer2019quantitativeanalysisof pages 17-19, shellhammer2019quantitativeanalysisof pages 20-22)
Groves et al. demonstrated that Fus3 can be retargeted to engineered proteins when two conditions are supplied: a compatible kinase–substrate docking interaction and a phosphorylatable motif that recruits a downstream effector. Coupling such motifs to phosphodegrons allowed Fus3 to induce degradation of non-native targets and predictably reshape the response to mating pheromone. This establishes Fus3 as a modular input-processing element for synthetic protein-degradation circuits rather than merely a natural mating kinase. The work was published August 15, 2016; DOI: https://doi.org/10.7554/eLife.15200. (groves2016rewiringmapkinases pages 1-2)
Fus3 itself is not a clinical target or deployed industrial product. Its practical value lies in providing a genetically tractable system for studying conserved MAPK principles—scaffold control, docking specificity, signal dynamics, crosstalk and synthetic rewiring. Extrapolation to mammalian ERK systems is conceptually useful but must not be mistaken for direct evidence about therapeutic efficacy. (kusari2004aconservedprotein pages 1-2, groves2016rewiringmapkinases pages 1-2)
Highest-confidence conclusions are that Fus3 is the S288c mating MAPK; Ste7 activates it at T180/Y182; it uses MAPK docking interactions; it regulates Far1 and the Ste12/Dig transcriptional system; it promotes Tec1 destruction; and it acts dynamically at the cortex, cytoplasm and nucleus. These conclusions are supported by complementary biochemical reconstitution, site-directed mutagenesis, genetics, microscopy and quantitative signaling assays. (kusari2004aconservedprotein pages 1-2, bardwell1996signalinginthe pages 1-2, bao2010multisitephosphorylationof pages 1-2, blackwell2007thepheromoneinducednuclear pages 1-2)
Important qualification: lists of Fus3 substrates vary with the criterion used. Direct in-vitro phosphorylation, docking, genetic dependence and physiological necessity are not equivalent. Far1 and Tec1 are especially well-supported functional substrates; Ste12 and Dig1/Dig2 are firmly established pathway partners/targets, but individual phosphorylation events can have overlapping or context-dependent effects. Proposed cortical targets should therefore be interpreted in conjunction with localization and mutant phenotypes rather than from motif presence alone.
Current expert interpretation: Fus3 specificity is an emergent systems property. Catalytic motif recognition contributes, but Ste5 scaffolding, high-affinity Ste7 docking, Gpa1-mediated positioning, nuclear tethering, signal kinetics and destruction of Tec1 together explain why shared upstream components generate a mating response rather than filamentation. The 2024 cross-stimulation study reinforces this view by showing that residual HOG–mating crosstalk is routed through Kss1 while Fus3 remains insulated as the mating-specific MAPK. (kusari2004aconservedprotein pages 1-2, shellhammer2019quantitativeanalysisof pages 20-22, zhang2024sharedandredundant pages 1-2, bao2010multisitephosphorylationof pages 1-2)
FUS3 encodes an intracellular, pheromone-activated MAP kinase that is scaffold-activated at the cell cortex and functions in the nucleus, cytoplasm and mating projection. It phosphorylates selected proteins through a combination of Ser/Thr-Pro motif recognition, docking interactions and spatial colocalization. Its principal pathway role is to coordinate Ste12-dependent mating transcription, Far1-mediated G1 arrest, polarized morphogenesis and gradient tracking, while maintaining developmental specificity by triggering Tec1 degradation and thereby suppressing filamentous-growth transcription.
References
(kusari2004aconservedprotein pages 1-2): Anasua B. Kusari, Douglas M. Molina, Walid Sabbagh, Chang S. Lau, and Lee Bardwell. A conserved protein interaction network involving the yeast map kinases fus3 and kss1. The Journal of Cell Biology, 164:267-277, Jan 2004. URL: https://doi.org/10.1083/jcb.200310021, doi:10.1083/jcb.200310021. This article has 93 citations.
(schwartz2005signalingspecificityin pages 26-31): MA Schwartz. Signaling specificity in saccharomyces cerevisiae mating and filamentous growth mapk pathways. Unknown journal, 2005.
(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.
(blackwell2007thepheromoneinducednuclear pages 1-2): Ernest Blackwell, Hye-Jin N Kim, and David E Stone. The pheromone-induced nuclear accumulation of the fus3 mapk in yeast depends on its phosphorylation state and on dig1 and dig2. BMC Cell Biology, 8:44-44, Oct 2007. URL: https://doi.org/10.1186/1471-2121-8-44, doi:10.1186/1471-2121-8-44. This article has 35 citations.
(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.
(peter2007ste7variantsthat pages 125-129): 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.
(peter2007ste7variantsthat pages 38-44): 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.
(bao2010multisitephosphorylationof pages 1-2): Marie Z. Bao, Teresa R. Shock, and Hiten D. Madhani. Multisite phosphorylation of the saccharomyces cerevisiae filamentous growth regulator tec1 is required for its recognition by the e3 ubiquitin ligase adaptor cdc4 and its subsequent destruction in vivo. Eukaryotic Cell, 9:31-36, Jan 2010. URL: https://doi.org/10.1128/ec.00250-09, doi:10.1128/ec.00250-09. This article has 31 citations and is from a peer-reviewed journal.
(sharmeen2020molecularroleofa pages 38-42): N Sharmeen. Molecular role of the ste50 adaptor protein in regulating mating-pheromone signaling specificity in «saccharomyces cerevisiae». Unknown journal, 2020.
(shellhammer2019quantitativeanalysisof pages 17-19): James P. Shellhammer, Amy E. Pomeroy, Yang Li, Lorena Dujmusic, Timothy C. Elston, Nan Hao, and Henrik G. Dohlman. Quantitative analysis of the yeast pheromone pathway. Yeast, 36:495-518, Aug 2019. URL: https://doi.org/10.1002/yea.3395, doi:10.1002/yea.3395. This article has 33 citations and is from a peer-reviewed journal.
(shellhammer2019quantitativeanalysisof pages 20-22): James P. Shellhammer, Amy E. Pomeroy, Yang Li, Lorena Dujmusic, Timothy C. Elston, Nan Hao, and Henrik G. Dohlman. Quantitative analysis of the yeast pheromone pathway. Yeast, 36:495-518, Aug 2019. URL: https://doi.org/10.1002/yea.3395, doi:10.1002/yea.3395. This article has 33 citations and is from a peer-reviewed journal.
(errede2015pheromoneinducedmorphogenesisand pages 1-2): Beverly Errede, Lior Vered, Eintou Ford, Matthew I. Pena, and Timothy C. Elston. Pheromone-induced morphogenesis and gradient tracking are dependent on the mapk fus3 binding to gα. Molecular Biology of the Cell, 26:3343-3358, Sep 2015. URL: https://doi.org/10.1091/mbc.e15-03-0176, doi:10.1091/mbc.e15-03-0176. This article has 38 citations and is from a domain leading peer-reviewed journal.
(zhang2024sharedandredundant pages 2-4): 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.
(groves2016rewiringmapkinases pages 1-2): Benjamin Groves, Arjun Khakhar, Cory M Nadel, Richard G Gardner, and Georg Seelig. Rewiring map kinases in saccharomyces cerevisiae to regulate novel targets through ubiquitination. eLife, Aug 2016. URL: https://doi.org/10.7554/elife.15200, doi:10.7554/elife.15200. This article has 13 citations and is from a domain leading peer-reviewed journal.
(peter2007ste7variantsthat pages 182-186): 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.
(shellhammer2019quantitativeanalysisof pages 19-20): James P. Shellhammer, Amy E. Pomeroy, Yang Li, Lorena Dujmusic, Timothy C. Elston, Nan Hao, and Henrik G. Dohlman. Quantitative analysis of the yeast pheromone pathway. Yeast, 36:495-518, Aug 2019. URL: https://doi.org/10.1002/yea.3395, doi:10.1002/yea.3395. This article has 33 citations and is from a peer-reviewed journal.