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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 identity is verified. SSK1/YLR006C, UniProt Q07084, in Saccharomyces cerevisiae strain S288c is the cytoplasmic response regulator of the Sln1–Ypd1–Ssk1 phosphorelay, not an identically named protein from Candida or another fungus. Its C-terminal CheY-like receiver domain contains the phospho-acceptor Asp554, matching the supplied Response_reg/PF00072, Sig_transdc_resp-reg_receiver, and CheY-like annotations. Literature concerning other fungal SSK1 homologs was excluded from the protein-specific conclusions below. (saito2012responsetohyperosmotic pages 4-5, posas1996yeasthog1map pages 1-2, branscum2015structuralandmutagenesis pages 89-94)
Ssk1 is not an enzyme, transporter, or structural protein. Its primary function is that of a phosphorylation-controlled signaling adaptor or molecular switch. Under normal osmotic conditions, Ssk1 is phosphorylated and inactive. Hyperosmotic stress interrupts phosphate delivery, producing unphosphorylated Ssk1, which binds and activates the MAP kinase kinase kinases Ssk2 and Ssk22. These activate Pbs2 and then Hog1, initiating osmoadaptation. Ssk1 therefore couples a fungal His–Asp phosphorelay to a eukaryotic MAPK cascade. (posas1998activationofthe pages 1-2, posas1996yeasthog1map pages 1-2, nadal2022thehogpathway pages 3-4)
| Annotation aspect | Best-supported conclusion | Evidence type / key experiment | Representative source |
|---|---|---|---|
| Identity and domain | Ssk1 (Q07084; YLR006C) of S. cerevisiae S288c is a nonenzymatic two-component response regulator with a C-terminal CheY-like receiver (Response_reg/PF00072) domain. Its phospho-acceptor is Asp554. | Organism-specific genetics, phosphotransfer mapping, receiver-domain mutagenesis, and structural analysis. Literature on Candida or other fungal SSK1 homologs is not evidence for this protein. (saito2012responsetohyperosmotic pages 4-5, posas1996yeasthog1map pages 1-2, branscum2015structuralandmutagenesis pages 89-94) | Posas et al., 1996, DOI; Saito & Posas, 2012, DOI |
| Normal-osmolarity phosphorelay | At normal turgor, active Sln1 maintains Ssk1 phosphorylated through Sln1-His576 → Sln1-Asp1144 → Ypd1-His64 → Ssk1-Asp554. Ssk1-P is inactive toward the downstream MAP3Ks and suppresses inappropriate HOG signaling. | Phosphorelay mutants, biochemical phosphotransfer, and genetic suppression of constitutive pathway activation. (saito2012responsetohyperosmotic pages 4-5, posas1996yeasthog1map pages 1-2, horie2008phosphorylatedssk1prevents pages 2-2) | Posas et al., 1996, DOI; Horie et al., 2008, DOI |
| Hyperosmotic activation | Increased external osmolarity lowers turgor and inhibits Sln1 kinase activity. Phosphate input to Ssk1 falls, allowing unphosphorylated Ssk1 (Ssk1-OH) to accumulate as the signaling-active species. Thus, Ssk1 operates through an unusual dephosphorylation-activates logic. | Hyperosmotic stimulation, phosphorelay-disrupting alleles, and pathway epistasis. (posas1996yeasthog1map pages 1-2, horie2008phosphorylatedssk1prevents pages 1-2, nadal2022thehogpathway pages 3-4) | Posas et al., 1996, DOI; de Nadal & Posas, 2022, DOI |
| Direct MAP3K activation and output | Ssk1-OH binds the N-terminal regulatory region of Ssk2 and, by established pathway annotation, its paralog Ssk22. Binding induces latent MAP3K activity, followed by Ssk2 autophosphorylation; the resulting cascade is Ssk2/Ssk22 → Pbs2 → Hog1. Ssk1 is therefore a phosphorylation-controlled signaling adaptor/switch, not an enzyme. | Direct binding assays, in-vitro restoration of Ssk2 activity by Ssk1, autophosphorylation assays, activation-loop mutagenesis, and genetic epistasis. (posas1998activationofthe pages 1-2, posas1996yeasthog1map pages 1-2, horie2008phosphorylatedssk1prevents pages 1-2) | Posas & Saito, 1998, DOI; Horie et al., 2008, DOI |
| Phosphorylated Ssk1 as inhibitor | Ssk1 is predominantly dimeric. Ssk1-OH homodimers activate Ssk2 efficiently, whereas Ssk1-P can associate with and inhibit Ssk1-OH, buffering spontaneous activation caused by phosphoaspartate hydrolysis. | Overexpression and dominant-inhibition experiments with phosphorylation-defective and Ssk2-binding-defective Ssk1 variants. (horie2008phosphorylatedssk1prevents pages 1-2, horie2008phosphorylatedssk1prevents pages 11-12) | Horie et al., 2008, DOI |
| Cellular localization | Ssk1 acts principally in the cytoplasm, consistent with its interaction with cytoplasmic Ypd1 and Ssk2/Ssk22. Ssk1 was distinguished experimentally from nuclear Skn7, and no stress-dependent Ssk1 relocalization was detected. | Fluorescence/localization analysis and compartment-specific investigation of Ypd1 shuttling between cytoplasm and nucleus. (lu2003saccharomycescerevisiaehistidine pages 1-3) | Lu et al., 2003, DOI |
| Turnover and feedback | Signaling-active, unphosphorylated Ssk1 is preferentially removed by a Ubc7/Qri8-dependent ubiquitin–proteasome pathway. Loss of UBC7 impairs Ssk1 degradation and delays Hog1 dephosphorylation, providing negative feedback after adaptation. | Protein-stability assays, ubiquitin-pathway mutants, and Hog1 phosphorylation kinetics. (sato2003phosphorelayregulateddegradationof pages 1-2) | Sato et al., 2003, DOI |
| Quantitative phosphotransfer | Ypd1 transfers phosphate to Ssk1 at approximately 160 s⁻¹, compared with about 1.4 s⁻¹ for transfer to Skn7, supporting rapid constitutive Ssk1 phosphorylation under normal osmolarity. | In-vitro phosphotransfer kinetics. (saito2012responsetohyperosmotic pages 4-5) | Saito & Posas, 2012, DOI |
| Quantitative phospho-state stability | Ssk1-P has an approximately 13-min dephosphorylation half-life without Ypd1 but approximately 42 h in vitro with Ypd1, indicating that Ypd1 both transfers phosphate and strongly stabilizes the phosphorylated state. | Purified-protein phosphoaspartate decay assays with and without Ypd1. (horie2008phosphorylatedssk1prevents pages 11-12) | Horie et al., 2008, DOI |
| Quantitative Ypd1 recognition | Ypd1 has approximately 1,000-fold higher affinity for the Ssk1 receiver domain than for the Sln1 receiver domain, despite use of a common Ypd1 surface; Ssk1 substitutions E510G, N512T, I514T, and I518T disrupt interaction in vivo. | Receiver-domain structural comparison, interaction mutagenesis, and binding analysis. (branscum2015structuralandmutagenesis pages 89-94) | Branscum, 2015, structural and mutagenesis study |
| 2023 downstream refinement | Ssk1's core annotation was unchanged. The Sln1–Ypd1–Ssk1 branch was used as established context to show that Ssk2/Ssk22 phosphorylate both Ser514 and Thr518 of Pbs2, whereas Sho1-branch MAP3K Ste11 phosphorylates only Thr518; Ptc1–Ptc4 then differentially dephosphorylate Pbs2. | Site-specific Pbs2 phosphorylation and phosphatase experiments. (tatebayashi2023twoactivatingphosphorylation pages 1-2) | Tatebayashi & Saito, 2023, DOI |
| 2024 branch-level refinement | Recent work refines branch behavior rather than changing Ssk1's molecular function. SSK1 deletion was used to perturb the Sln1 branch: branch-specific effects were observed on Hog1 activation amplitude/duration, nuclear trafficking, transcription, and Sho1/Kss1-mediated cross-talk during salt and pheromone signaling. | SSK1/SHO1 deletions; Hog1-mRuby2 nuclear imaging; CRE-LacZ assays over 0–550 mM KCl; RNA-seq including 350 mM KCl, with three independent experiments. (zhang2024sharedandredundant pages 1-2, zhang2024sharedandredundant pages 4-5) | Zhang et al., 2024, DOI |
Table: Compact evidence map for S. cerevisiae Ssk1/Q07084, covering identity, phosphorelay logic, MAPK activation, localization, turnover, quantitative biochemistry, and recent pathway refinements. It separates direct Ssk1 evidence from 2023–2024 studies that retain the established annotation while refining downstream and branch-level behavior.
The evidence is internally consistent with the supplied identity:
The receiver domain has the expected response-regulator α/β topology. Structural work on the isolated Ssk1 receiver region identified Asp554 at the active site, a flexible approximately 20-residue loop, and a disordered approximately 50-residue C-terminal tail. Ypd1-contact substitutions E510G, N512T, I514T, and I518T disrupted interaction in vivo, supporting a specific phosphotransfer interface rather than nonspecific association. (branscum2015structuralandmutagenesis pages 89-94)
This domain agreement is important because SSK1 homologs occur in other fungi and may control additional stress or virulence phenotypes. Those homologs are evolutionarily informative but are not interchangeable evidence for Q07084. The conclusions here derive from experiments explicitly performed in S. cerevisiae.
At normal osmolarity and turgor, the transmembrane hybrid histidine kinase Sln1 is active. Phosphate flows through the sequence:
Sln1-His576 → Sln1-Asp1144 → Ypd1-His64 → Ssk1-Asp554.
Phosphorylated Ssk1, conventionally denoted Ssk1-P, is inactive toward the downstream MAP3Ks. Increased extracellular osmolarity reduces turgor and inhibits Sln1 kinase activity. Continued phosphoaspartate hydrolysis without replenishment then increases unphosphorylated Ssk1, or Ssk1-OH, which is the active signaling species. Ssk1 consequently exhibits an unusual dephosphorylation-activates response-regulator logic. (saito2012responsetohyperosmotic pages 4-5, posas1996yeasthog1map pages 1-2, horie2008phosphorylatedssk1prevents pages 1-2)
Biochemical kinetics support this model. Ypd1 transfers phosphate to Ssk1 at approximately 160 s⁻¹, compared with approximately 1.4 s⁻¹ for the alternative response regulator Skn7. This rapid transfer helps keep Ssk1 phosphorylated under nonstress conditions. In vitro, Ssk1-P had an approximately 13-minute dephosphorylation half-life without Ypd1 but approximately 42 hours in the presence of Ypd1, indicating that Ypd1 both transfers phosphate and strongly stabilizes Ssk1-P. (saito2012responsetohyperosmotic pages 4-5, horie2008phosphorylatedssk1prevents pages 11-12)
Unphosphorylated Ssk1 directly binds the N-terminal regulatory region of Ssk2; pathway genetics and established annotation extend this activation to the paralogous MAP3K Ssk22. Biochemical reconstitution showed that Ssk1 promotes rapid Ssk2 autophosphorylation. The favored mechanism has two stages: Ssk1 binding relieves N-terminal autoinhibition and initiates latent kinase activity; Ssk2 then autophosphorylates and remains catalytically active without continued dependence on Ssk1. Thr1460 in the Ssk2 activation loop is important for this process. (posas1998activationofthe pages 1-2)
Ssk1 itself does not catalyze phosphorylation of Ssk2. It is better annotated as a phosphorylation-state-dependent MAP3K activator/adaptor whose molecular specificity is for the regulatory regions of Ssk2/Ssk22.
Ssk1 also appears to buffer basal signaling. It is predominantly dimeric: Ssk1-OH homodimers efficiently activate Ssk2, whereas phosphorylated Ssk1 can associate with and inhibit Ssk1-OH. This provides a mechanism for preventing small amounts of spontaneously dephosphorylated Ssk1 from activating Hog1 in unstressed cells. Mutations that prevent Ssk1 phosphorylation cause constitutive pathway activation, while overexpressed wild-type Ssk1 or an Ssk2-binding-defective variant can inhibit constitutively active Ssk1 mutants. (horie2008phosphorylatedssk1prevents pages 1-2, horie2008phosphorylatedssk1prevents pages 11-12, horie2008phosphorylatedssk1prevents pages 2-2)
Ssk1 functions specifically in the Sln1 branch of the high-osmolarity glycerol pathway:
Sln1 → Ypd1 → Ssk1 → Ssk2/Ssk22 → Pbs2 → Hog1.
The separate Sho1 branch uses membrane-associated Hkr1/Msb2–Sho1/Opy2 machinery and Ste11, rather than Ssk1, before converging on Pbs2. Thus, Ssk1 is neither a component of the Sho1 branch nor a general downstream MAPK protein. (nadal2022thehogpathway pages 3-4, tatebayashi2023twoactivatingphosphorylation pages 1-2)
Foundational epistasis established this ordering. Loss of SLN1 or YPD1 causes excessive HOG signaling, while deletion of SSK1 or downstream SSK2, PBS2, or HOG1 suppresses relevant constitutive-activation phenotypes. Conversely, activated N-terminally truncated Ssk2/Ssk22 bypass upstream control and are toxic because they drive the cascade constitutively. (posas1996yeasthog1map pages 1-2, horie2008phosphorylatedssk1prevents pages 2-2)
Activated Hog1 controls the wider adaptive program, including glycerol synthesis and retention, transcriptional and translational reprogramming, and temporary cell-cycle arrest. These are downstream consequences of Ssk1 signaling rather than direct biochemical activities of Ssk1 itself. The authoritative 2022 review retains Ssk1's established annotation as the Sln1-branch response regulator upstream of Ssk2/Ssk22. (nadal2022thehogpathway pages 3-4)
The best-supported site of Ssk1 action is the cytoplasm. Localization studies distinguished cytoplasmic Ssk1 from the more nuclear response regulator Skn7 and proposed that Ypd1 shuttles between nucleus and cytoplasm to phosphorylate the two targets in their respective compartments. No stress-dependent relocalization of Ssk1 was detected. Its cytoplasmic assignment also agrees with its physical and functional interactions with Ypd1 and Ssk2/Ssk22. (lu2003saccharomycescerevisiaehistidine pages 1-3)
Ssk1 should therefore not be annotated as a plasma-membrane osmosensor. Sln1 performs transmembrane sensing; Ssk1 receives the intracellular phosphorelay state and activates the cytoplasmic MAPK module.
Ssk1 abundance is regulated as well as its phosphorylation state. Unphosphorylated, signaling-active Ssk1 is preferentially degraded through a Ubc7/Qri8-dependent ubiquitin–proteasome pathway. Loss of UBC7 impairs Ssk1 degradation and delays Hog1 dephosphorylation, indicating that Ssk1 turnover contributes to pathway shutoff after osmoadaptation. (sato2003phosphorelayregulateddegradationof pages 1-2)
This creates layered negative regulation: rapid phosphorylation maintains inactivity before stress; phosphorylated Ssk1 inhibits residual active Ssk1; and proteasomal turnover removes unphosphorylated Ssk1 during adaptation. The Sln1–Ypd1–Ssk1 network is also robust to fluctuations in component abundance, consistent with the need to avoid inappropriate Hog1 activation under normal growth conditions.
No 2023–2024 study retrieved here overturns or materially revises the core molecular annotation of Ssk1. Recent work instead uses the established SSK1 branch to resolve downstream chemistry and branch-specific signaling behavior.
Tatebayashi and Saito, published April 2023, showed that Ssk2/Ssk22 can phosphorylate both Ser514 and Thr518 in the activation loop of Pbs2, whereas the Sho1-branch MAP3K Ste11 phosphorylates only Thr518. Ptc1–Ptc4 then differentially dephosphorylate Pbs2, with Ptc1 preferentially acting on Thr518 and using Nbp2 for recruitment. This refines the biochemical consequences of signaling through the Ssk1-controlled branch but does not change Ssk1's placement or direct function. DOI: https://doi.org/10.1016/j.jbc.2023.104569. (tatebayashi2023twoactivatingphosphorylation pages 1-2)
Zhang and colleagues, published October 2024, compared SSK1 and SHO1 deletion strains using MAPK phosphorylation, Hog1 nuclear trafficking, reporter assays, and transcriptomics. Their results indicate complementary branch effects on Hog1 activation amplitude and duration and show that loss of Sln1-branch signaling can release Sho1/Kss1-dependent cross-talk toward the mating pathway. Experiments included CRE-LacZ responses over 0–550 mM KCl, RNA sequencing at 350 mM KCl, and Hog1-mRuby2 nuclear imaging. The study used SSK1 deletion as a branch-selective perturbation; it did not identify a new catalytic activity or localization for Ssk1. DOI: https://doi.org/10.1091/mbc.e24-06-0270. (zhang2024sharedandredundant pages 1-2, zhang2024sharedandredundant pages 4-5)
These modern data caution against describing the Sln1/Ssk1 and Sho1 branches as merely interchangeable. They converge on Pbs2-Hog1 but differ in downstream phosphorylation potential, signal kinetics, transcriptional output, and cross-pathway insulation.
Ssk1 itself is primarily a research-system component rather than a currently deployed industrial reagent or therapeutic target. Its established applications are nevertheless substantial:
A concise functional annotation supported by the literature is:
Ssk1 is a cytoplasmic, CheY-like response regulator in the S. cerevisiae Sln1–Ypd1 osmosensing phosphorelay. At normal osmolarity, phosphorylation of Asp554 keeps Ssk1 inactive. Hyperosmotic inhibition of Sln1 causes unphosphorylated Ssk1 to accumulate and bind the regulatory regions of Ssk2/Ssk22, promoting MAP3K activation and signaling through Pbs2 to Hog1. Phosphorylated-Ssk1-mediated inhibition and ubiquitin–proteasome-dependent turnover constrain basal and prolonged signaling.
Confidence is high for identity, Asp554 phosphorylation, phosphorelay direction, cytoplasmic action, direct Ssk2 activation, and downstream Pbs2-Hog1 signaling because these are supported by convergent genetics, biochemistry, mutagenesis, structural evidence, localization studies, and authoritative reviews. The strongest qualification concerns treating Ssk2 and Ssk22 as completely equivalent: they are commonly described as redundant in osmostress signaling, but stimulus-specific work and recent branch analyses indicate that apparent redundancy should not be interpreted as identical behavior in every context. (posas1998activationofthe pages 1-2, horie2008phosphorylatedssk1prevents pages 11-12, nadal2022thehogpathway pages 3-4, tatebayashi2023twoactivatingphosphorylation pages 1-2)
References
(saito2012responsetohyperosmotic pages 4-5): Haruo Saito and Francesc Posas. Response to hyperosmotic stress. Genetics, 192:289-318, Oct 2012. URL: https://doi.org/10.1534/genetics.112.140863, doi:10.1534/genetics.112.140863. This article has 656 citations and is from a domain leading 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.
(branscum2015structuralandmutagenesis pages 89-94): K Branscum. Structural and mutagenesis studies of the yeast phosphorelay signaling proteins ypd1 and ssk1. Unknown journal, 2015.
(posas1998activationofthe pages 1-2): F. Posas and H. Saito. Activation of the yeast ssk2 map kinase kinase kinase by the ssk1 two‐component response regulator. The EMBO Journal, 17:1385-1394, Mar 1998. URL: https://doi.org/10.1093/emboj/17.5.1385, doi:10.1093/emboj/17.5.1385. This article has 407 citations.
(nadal2022thehogpathway pages 3-4): Eulàlia de Nadal and Francesc Posas. The hog pathway and the regulation of osmoadaptive responses in yeast. FEMS Yeast Research, Mar 2022. URL: https://doi.org/10.1093/femsyr/foac013, doi:10.1093/femsyr/foac013. This article has 155 citations and is from a peer-reviewed journal.
(horie2008phosphorylatedssk1prevents pages 2-2): Tetsuro Horie, Kazuo Tatebayashi, Rika Yamada, and Haruo Saito. Phosphorylated ssk1 prevents unphosphorylated ssk1 from activating the ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway. Sep 2008. URL: https://doi.org/10.1128/mcb.00589-08, doi:10.1128/mcb.00589-08. This article has 64 citations and is from a domain leading peer-reviewed journal.
(horie2008phosphorylatedssk1prevents pages 1-2): Tetsuro Horie, Kazuo Tatebayashi, Rika Yamada, and Haruo Saito. Phosphorylated ssk1 prevents unphosphorylated ssk1 from activating the ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway. Sep 2008. URL: https://doi.org/10.1128/mcb.00589-08, doi:10.1128/mcb.00589-08. This article has 64 citations and is from a domain leading peer-reviewed journal.
(horie2008phosphorylatedssk1prevents pages 11-12): Tetsuro Horie, Kazuo Tatebayashi, Rika Yamada, and Haruo Saito. Phosphorylated ssk1 prevents unphosphorylated ssk1 from activating the ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway. Sep 2008. URL: https://doi.org/10.1128/mcb.00589-08, doi:10.1128/mcb.00589-08. This article has 64 citations and is from a domain leading 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.
(sato2003phosphorelayregulateddegradationof pages 1-2): Naoto Sato, Hiroyuki Kawahara, Akio Toh-e, and Tatsuya Maeda. Phosphorelay-regulated degradation of the yeast ssk1p response regulator by the ubiquitin-proteasome system. Molecular and Cellular Biology, 23:6662-6671, Sep 2003. URL: https://doi.org/10.1128/mcb.23.18.6662-6671.2003, doi:10.1128/mcb.23.18.6662-6671.2003. This article has 62 citations and is from a domain leading peer-reviewed journal.
(tatebayashi2023twoactivatingphosphorylation pages 1-2): Kazuo Tatebayashi and Haruo Saito. Two activating phosphorylation sites of pbs2 map2k in the yeast hog pathway are differentially dephosphorylated by four pp2c phosphatases ptc1–ptc4. Journal of Biological Chemistry, 299:104569, Apr 2023. URL: https://doi.org/10.1016/j.jbc.2023.104569, doi:10.1016/j.jbc.2023.104569. This article has 23 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.
(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.