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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 the Saccharomyces cerevisiae S288c gene product Pbs2—not a similarly named protein from another organism. The supplied identifiers PBS2/YJL128C, aliases HOG4, SFS4, SSK4, and UniProt P08018 correspond functionally to the protein consistently described in the yeast literature as the central MAP kinase kinase (MAP2K/MAPKK) of the high-osmolarity glycerol (HOG) pathway. Its architecture—an N-terminal regulatory/scaffolding region and a C-terminal eukaryotic protein-kinase domain—also agrees with the supplied STE-family Ser/Thr-kinase and Pfam/InterPro annotations. The retrieved papers generally identify the protein as S. cerevisiae Pbs2 rather than printing the UniProt accession, so accession-level verification rests on concordance with the supplied curated record, locus, organism, aliases, pathway, biochemical activity, and domain organization. No evidence concerning a different organism’s PBS2-like protein was used.
Pbs2 has two inseparable primary functions. It is (1) the MAP2K that directly activates Hog1 and (2) a scaffold that assembles pathway-specific upstream and downstream components. Its best-established catalytic reaction is ATP-dependent phosphorylation of the Hog1 activation-loop residues Thr174 and Tyr176. Pbs2 itself is activated at Ser514 and Thr518, with different upstream branches producing biochemically distinct Pbs2 phosphoforms. (tatebayashi2023twoactivatingphosphorylation pages 1-2, tatebayashi2020osmostressenhancesactivating pages 1-2)
| Aspect | Mechanistic conclusion | Key residues/components | Evidence type | Representative source/date |
|---|---|---|---|---|
| Identity and domain architecture | Pbs2 is the Saccharomyces cerevisiae HOG-pathway MAP kinase kinase (MAP2K), combining an N-terminal regulatory/scaffolding region with a C-terminal protein-kinase domain. This matches PBS2/YJL128C and UniProt P08018. | N-terminal docking regions; C-terminal kinase domain | Sequence/domain annotation supported by interaction mapping and mutagenesis | Tatebayashi et al., July 2003 (tatebayashi2003adockingsite pages 1-2) |
| Catalytic reaction and substrate specificity | Activated Pbs2 transfers phosphate from ATP to both regulatory residues of its direct MAPK substrate Hog1, thereby activating Hog1 during osmotic stress. | Hog1 Thr174 and Tyr176 | Phosphosite analysis, pathway genetics, and biochemical assays | Tatebayashi & Saito, April 2023 (tatebayashi2023twoactivatingphosphorylation pages 1-2) |
| Differential upstream activation | The SHO1-branch MAP3K Ste11 phosphorylates Pbs2 primarily at Thr518, whereas the SLN1-branch MAP3Ks Ssk2/Ssk22 can phosphorylate both Ser514 and Thr518. Diphosphorylated Pbs2 is intrinsically competent to activate Hog1; Thr518-monophosphorylated Pbs2 requires osmostress-enhanced Pbs2–Hog1 reactivity. | Pbs2 Ser514 and Thr518; Ste11; Ssk2; Ssk22 | Phospho-specific immunoblotting, mutant reconstruction, and pathway genetics | Tatebayashi et al., February 2020; Tatebayashi & Saito, April 2023 (tatebayashi2023twoactivatingphosphorylation pages 1-2, tatebayashi2020osmostressenhancesactivating pages 1-2) |
| Scaffolding and docking | Pbs2 is both an enzyme and a pathway scaffold: separate N-terminal regions dock Ssk2/Ssk22, Sho1, and Hog1, increasing signaling efficiency and insulating the HOG cascade from other MAPK pathways. | Ssk2/Ssk22 docking region; Sho1-binding proline-rich motif; HBD-1; Hog1 CD and PBD-2 regions | Interaction assays, docking-site mutations, domain transfer, and osmosensitivity phenotypes | Tatebayashi et al., July 2003; Murakami et al., April 2008 (tatebayashi2003adockingsite pages 1-2, murakami2008twoadjacentdocking pages 1-2, murakami2008twoadjacentdocking pages 11-12) |
| Cellular localization | Wild-type Pbs2 is predominantly cytoplasmic and normally excluded from the nucleus. Osmostress transiently recruits Pbs2 to Sho1-associated polarized cortical sites at bud tips and mother–bud necks; recruitment depends on Sho1 and Cdc42. An N-terminal nuclear-export signal maintains cytoplasmic enrichment. | Sho1 SH3 domain; Pbs2 Pro96 region; Cdc42; N-terminal nuclear-export signal; Pbs2(K389M) reporter | GFP microscopy, deletion/mutant analysis, and localization scoring after osmotic shock | Reiser et al., September 2000; Saito & Tatebayashi, September 2004 (reiser2000polarizedlocalizationof pages 1-2, saito2004regulationofthe pages 4-4, reiser2000polarizedlocalizationof pages 7-7) |
| PP2C-mediated downregulation | Ptc1–Ptc4 reverse activating phosphorylation of Pbs2. Ptc1 predominantly controls Thr518, whereas all four phosphatases act redundantly on Ser514; Nbp2 helps recruit Ptc1 to Pbs2. | Ptc1, Ptc2, Ptc3, Ptc4; Nbp2; Pbs2 Ser514 and Thr518 | Phos-tag electrophoresis, phospho-specific antibodies, immunoprecipitation, and combinatorial phosphatase deletions | Tatebayashi & Saito, April 2023 (tatebayashi2023twoactivatingphosphorylation pages 7-8, tatebayashi2023twoactivatingphosphorylation pages 1-2, tatebayashi2023twoactivatingphosphorylation pages 8-9) |
| Hog1-to-Pbs2 positive feedback | Activated Hog1 phosphorylates Pbs2 at Ser248. Modeling and mutant validation support an affinity/catalytic feedback mechanism that can shift Hog1 phosphorylation from distributive toward processive behavior, improving response sensitivity and robustness. | Pbs2 Ser248; Pbs2-S248A; Pbs2-S248E; Hog1 | ODE modeling, in-vivo phosphosignaling measurements, in-vitro kinase assays, and binding analysis | Mosbacher et al., May 2023 (mosbacher2023positivefeedbackinduces pages 10-11) |
| Glycerol-assimilation application | Disrupting PBS2 increased glycerol assimilation, consistent with reduced HOG-pathway output improving glycerol use under the tested conditions. The engineering effect is context-dependent and may trade metabolic performance against stress tolerance. | PBS2 deletion; HOG1 deletion; SSK2/SSK22/STE11 triple disruption; STL1; RIM15; CYB2 | Adaptive laboratory evolution, genome resequencing, targeted gene disruption, growth assays, and lactic-acid production demonstration | Sone et al., July 2023 (sone2023lossoffunction pages 1-2) |
| Telomerase-associated oxidative stress | In telomerase-deficient yeast, Hog1 activation and control of elevated reactive oxygen species require the canonical upstream MAP2K Pbs2. The response is separable from Mec1 checkpoint signaling, although effects of Hog1 loss on senescence are complicated by pre-existing telomere and viability defects. | Pbs2; Hog1 Thr174/Tyr176; Mec1; reactive oxygen species | Gene deletion, phospho-Hog1 analysis, ROS measurements, and replicative-senescence experiments | Zeinoun et al., October 2023 preprint; peer-reviewed June 2024 report (zeinoun2023hog1actsin pages 1-6) |
Table: Concise evidence map for the verified S. cerevisiae Pbs2 MAP2K, covering catalytic specificity, regulation, scaffolding, localization, recent mechanistic findings, and biotechnology applications.
Pbs2 belongs to the eukaryotic protein-kinase superfamily and is specifically a MAP2K in the HOG pathway. Literature mapping divides it functionally into an N-terminal noncatalytic interaction region and a catalytic kinase domain. The N terminus contains separable docking determinants for Ssk2/Ssk22, Sho1, and Hog1, as well as a nuclear-export determinant; this experimentally observed modular organization is consistent with the supplied PBS2_N and Pkinase domain annotations. (tatebayashi2003adockingsite pages 1-2, murakami2008twoadjacentdocking pages 11-12, tatebayashi2003adockingsite pages 6-7)
This identification is not merely symbol based. The relevant studies explicitly concern budding yeast S. cerevisiae, place Pbs2 between the MAP3Ks Ste11/Ssk2/Ssk22 and Hog1, and describe the same kinase/scaffold architecture and osmoregulatory function. Therefore, the literature matches P08018 rather than an unrelated PBS2 symbol in another taxon. (tatebayashi2003adockingsite pages 1-2, tatebayashi2023twoactivatingphosphorylation pages 1-2)
Pbs2 catalyzes transfer of phosphate from ATP to the activation loop of the MAPK Hog1:
ATP + Hog1 → ADP + Hog1-pThr174/pTyr176.
Thus, despite belonging to a kinase family commonly labeled Ser/Thr kinases, Pbs2 is functionally a dual-specificity MAP2K, because its physiological substrate is phosphorylated on both threonine and tyrosine. The strongly supported direct physiological substrate is Hog1; the retrieved evidence does not establish a broad alternative substrate repertoire comparable to that of downstream MAPKs. (tatebayashi2023twoactivatingphosphorylation pages 1-2, zeinoun2023hog1actsin pages 1-6)
Substrate recognition is reinforced by docking rather than catalytic-site specificity alone. Pbs2’s N-terminal HBD-1 region engages two adjacent Hog1 surfaces, the common-docking domain and PBD-2. Mutation of both Hog1 regions abolishes detectable Pbs2 association and produces severe osmosensitivity, while HBD-1 is required for optimal Hog1 activation after osmotic stress. (murakami2008twoadjacentdocking pages 1-2, murakami2008twoadjacentdocking pages 11-12, murakami2008twoadjacentdocking pages 10-11)
The two upstream HOG branches converge on Pbs2 but do not activate it identically:
This explains how Pbs2 helps preserve signaling specificity. Basal Ste11 activity alone is insufficient to drive inappropriate Hog1 activation, reducing crosstalk from other Ste11-dependent yeast MAPK pathways. In an upstream-signaling mutant, weak Hog1 phosphorylation was observed only at approximately 0.8–1.6 M NaCl; it disappeared upon PBS2 deletion and increased with constitutively active Ste11, directly tying the response to Pbs2. (tatebayashi2020osmostressenhancesactivating pages 1-2)
Pbs2 is the obligatory convergence point of two osmosensing systems:
The Pbs2 N-terminal Ssk2/Ssk22 docking region constitutively binds the MAP3K kinase domains. Mutating it weakens interaction and Hog1 activation; transferring it to another MAP2K, Ste7, permits Ssk2/Ssk22-dependent phosphorylation of Ste7. This domain-transfer result is unusually strong evidence that the site encodes pathway specificity rather than merely increasing nonspecific collision frequency. (tatebayashi2003adockingsite pages 1-2)
Pbs2 is consequently best understood as a catalytic scaffold. It brings upstream MAP3Ks, membrane-associated Sho1, and downstream Hog1 into productive arrangements while helping insulate HOG signaling from mating and filamentation MAPK cascades. (tatebayashi2003adockingsite pages 1-2, murakami2008twoadjacentdocking pages 10-11)
Wild-type Pbs2–GFP is predominantly cytoplasmic and visibly excluded from the nucleus before and after osmotic stress. An N-terminal nuclear-export signal maintains this distribution: deleting residues 4–18 causes nuclear accumulation, whereas additional sequence changes reveal a C-terminal nuclear-import capacity. Pbs2 therefore may shuttle, but unlike activated Hog1, wild-type Pbs2 does not show prominent stress-induced nuclear accumulation. (saito2004regulationofthe pages 4-4, tatebayashi2003adockingsite pages 6-7)
A transient membrane-proximal signaling pool is revealed particularly clearly with kinase-inactive Pbs2(K389M)–GFP. After 0.4 M NaCl, it accumulates within roughly 5–15 minutes at polarized cortical sites—growing bud tips and mother–bud necks—where Sho1 is concentrated. Recruitment depends on the Sho1 SH3 domain, the Pbs2 proline-rich interaction determinant around Pro96, and Cdc42. It is reduced to fewer than 5% of cells in sho1Δ, versus about 20% in the reported cdc42-1 condition; more than 200 cells were scored per experiment. (reiser2000polarizedlocalizationof pages 1-2, reiser2000polarizedlocalizationof pages 7-7, reiser2000polarizedlocalizationof pages 2-3)
Upstream components Ste11, Ste20, and Ste50 are not required to establish the initial Sho1–Pbs2 localization interaction. Instead, impaired kinase activation prolongs cortical accumulation, supporting a model in which Pbs2 is recruited to a polarized plasma-membrane complex, activated there, and then released into the cytoplasm to activate Hog1. The conspicuous localization of inactive Pbs2 probably represents trapping of a normally short-lived intermediate rather than the steady-state distribution of active wild-type protein. (reiser2000polarizedlocalizationof pages 6-7, reiser2000polarizedlocalizationof pages 5-6)
A 2023 Journal of Biological Chemistry study established that four PP2C phosphatases directly regulate Pbs2’s activation-loop sites. Ptc1 predominantly controls Thr518, whereas Ptc1–Ptc4 act redundantly on Ser514. Nbp2 recruits Ptc1 to Pbs2, providing interaction specificity for dephosphorylation. These conclusions were based on phospho-specific antibodies, Pbs2 immunoprecipitation, Phos-tag electrophoresis, and combinatorial phosphatase deletions. One reported normalized comparison for Thr518 phosphorylation was 27.4 versus 501, illustrating the large accumulation possible when relevant negative regulation is removed, although these assay-normalized units should not be interpreted as an absolute enzymatic rate. Published April 2023: https://doi.org/10.1016/j.jbc.2023.104569. (tatebayashi2023twoactivatingphosphorylation pages 7-8, tatebayashi2023twoactivatingphosphorylation pages 1-2, tatebayashi2023twoactivatingphosphorylation pages 8-9)
Mosbacher and colleagues combined ODE modeling, cellular phosphosignaling measurements, mutagenesis, kinase assays, and binding experiments to argue that Hog1 activation can switch from predominantly distributive toward more processive behavior. Activated Hog1 phosphorylates Pbs2 at Ser248; S248A and S248E substitutions produced behavior consistent with disrupted and constitutive affinity feedback, respectively, and S248E increased Hog1 affinity in vitro. The proposed mixed mechanism increases sensitivity and robustness rather than treating distributive and processive phosphorylation as mutually exclusive fixed modes. Published May 2023: https://doi.org/10.1038/s41467-023-37430-y. (mosbacher2023positivefeedbackinduces pages 10-11)
A representative in-vitro experiment used 0.5 μg GST-Hog1, 0.25 μg kinase-impaired Pbs2 constructs, 50 μM ATP, and a 15-minute incubation at 30 °C; cellular validation used 0.4 M NaCl. These are assay conditions, not physiological concentrations, but they provide reproducible quantitative context for the mechanistic inference. (mosbacher2023positivefeedbackinduces pages 10-11)
A study published in peer-reviewed form in June 2024 found that telomerase inactivation increases reactive oxygen species and activates Hog1 through canonical Pbs2. This response persists independently of Mec1 checkpoint signaling and helps counter oxidative stress. Interpretation requires caution: accelerated senescence after HOG1 deletion may partly reflect shorter telomeres and reduced viability already present before telomerase inactivation. DOI: https://doi.org/10.1038/s42003-024-06464-3; the retrieved full-text evidence was the October 2023 preprint, https://doi.org/10.1101/2023.10.04.560866. (zeinoun2023hog1actsin pages 1-6)
This finding broadens the experimentally observed circumstances in which the Pbs2–Hog1 module operates, but it does not displace osmoregulation as Pbs2’s primary annotated function.
The HOG pathway is relevant to food, brewing, biofuel, and chemical fermentation because industrial yeast experiences fluctuating osmolarity, temperature, ethanol, oxygen, pH, and nutrient availability. Pbs2 is therefore a potential engineering control point for balancing stress resistance against carbon flux. However, because it is the obligatory MAP2K for Hog1, complete PBS2 disruption can compromise environmental robustness; pathway tuning is generally more defensible than assuming deletion will improve every production process.
A 2023 engineering study found that PBS2 disruption increased glycerol assimilation, consistent with HOG-pathway attenuation redirecting physiology under the tested conditions. Individual deletion of SSK2, SSK22, or STE11 did not reproduce the effect, while triple deletion only partially improved assimilation, reinforcing Pbs2’s status as the common convergence node. An HOG1/CYB2 double disruptant was also used to produce L-lactic acid from glycerol. Published July 2023: https://doi.org/10.1007/s11274-023-03696-z. (sone2023lossoffunction pages 1-2)
The effect was context dependent: HOG1 loss did not further improve an already high-assimilation STL1-overexpressing, rim15Δ strain. The available excerpt did not provide titers, yield, productivity, or fold-change values, so the study supports proof of principle rather than a quantitatively benchmarked industrial process. (sone2023lossoffunction pages 1-2)
Recommended primary annotation: Pbs2 is a cytoplasmic, stress-recruited dual-specificity MAP kinase kinase and catalytic scaffold of the S. cerevisiae HOG pathway. It receives signals from Ste11 or Ssk2/Ssk22, is activated through Ser514/Thr518 phosphorylation, and directly phosphorylates Hog1 at Thr174/Tyr176. Its N-terminal docking modules assemble pathway components and enforce specificity; its kinase domain executes signal transmission. It acts transiently at Sho1-associated polarized cortical sites and predominantly in the cytoplasm, while activated Hog1 carries much of the downstream nuclear response. (tatebayashi2003adockingsite pages 1-2, tatebayashi2023twoactivatingphosphorylation pages 1-2, reiser2000polarizedlocalizationof pages 1-2, saito2004regulationofthe pages 4-4)
Confidence: High for the HOG-pathway MAP2K reaction, Hog1 substrate, activation sites, scaffold role, and predominantly cytoplasmic localization. Moderate for broader nonosmotic roles, because these can be stress- and context-specific. The 2023 feedback and phosphatase studies refine rather than overturn the canonical model: Pbs2 is not a passive middle kinase but a dynamically regulated specificity hub whose phosphorylation state, docking interactions, localization, feedback, and dephosphorylation jointly determine Hog1 signaling.
References
(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.
(tatebayashi2020osmostressenhancesactivating pages 1-2): Kazuo Tatebayashi, Katsuyoshi Yamamoto, Taichiro Tomida, Akiko Nishimura, Tomomi Takayama, Masaaki Oyama, Hiroko Kozuka‐Hata, Satomi Adachi‐Akahane, Yuji Tokunaga, and Haruo Saito. Osmostress enhances activating phosphorylation of hog1 map kinase by mono‐phosphorylated pbs2 map2k. The EMBO Journal, Feb 2020. URL: https://doi.org/10.15252/embj.2019103444, doi:10.15252/embj.2019103444. This article has 74 citations.
(tatebayashi2003adockingsite pages 1-2): K. Tatebayashi, M. Takekawa, and H. Saito. A docking site determining specificity of pbs2 mapkk for ssk2/ssk22 mapkkks in the yeast hog pathway. The EMBO Journal, 22:3624-3634, Jul 2003. URL: https://doi.org/10.1093/emboj/cdg353, doi:10.1093/emboj/cdg353. This article has 142 citations.
(murakami2008twoadjacentdocking pages 1-2): Yulia Murakami, Kazuo Tatebayashi, and Haruo Saito. Two adjacent docking sites in the yeast hog1 mitogen-activated protein (map) kinase differentially interact with the pbs2 map kinase kinase and the ptp2 protein tyrosine phosphatase. Apr 2008. URL: https://doi.org/10.1128/mcb.01817-07, doi:10.1128/mcb.01817-07. This article has 72 citations and is from a domain leading peer-reviewed journal.
(murakami2008twoadjacentdocking pages 11-12): Yulia Murakami, Kazuo Tatebayashi, and Haruo Saito. Two adjacent docking sites in the yeast hog1 mitogen-activated protein (map) kinase differentially interact with the pbs2 map kinase kinase and the ptp2 protein tyrosine phosphatase. Apr 2008. URL: https://doi.org/10.1128/mcb.01817-07, doi:10.1128/mcb.01817-07. This article has 72 citations and is from a domain leading peer-reviewed journal.
(reiser2000polarizedlocalizationof pages 1-2): Vladimír Reiser, Suhal M. Salah, and Gustav Ammerer. Polarized localization of yeast pbs2 depends on osmostress, the membrane protein sho1 and cdc42. Nature Cell Biology, 2:620-627, Sep 2000. URL: https://doi.org/10.1038/35023568, doi:10.1038/35023568. This article has 193 citations and is from a highest quality peer-reviewed journal.
(saito2004regulationofthe pages 4-4): H. Saito and K. Tatebayashi. Regulation of the osmoregulatory hog mapk cascade in yeast. Journal of biochemistry, 136 3:267-72, Sep 2004. URL: https://doi.org/10.1093/jb/mvh135, doi:10.1093/jb/mvh135. This article has 327 citations and is from a peer-reviewed journal.
(reiser2000polarizedlocalizationof pages 7-7): Vladimír Reiser, Suhal M. Salah, and Gustav Ammerer. Polarized localization of yeast pbs2 depends on osmostress, the membrane protein sho1 and cdc42. Nature Cell Biology, 2:620-627, Sep 2000. URL: https://doi.org/10.1038/35023568, doi:10.1038/35023568. This article has 193 citations and is from a highest quality peer-reviewed journal.
(tatebayashi2023twoactivatingphosphorylation pages 7-8): 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.
(tatebayashi2023twoactivatingphosphorylation pages 8-9): 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.
(mosbacher2023positivefeedbackinduces pages 10-11): Maximilian Mosbacher, Sung Sik Lee, Matthias Peter, and Manfred Claassen. Positive feedback induces switch between distributive and processive phosphorylation of hog1. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-37430-y, doi:10.1038/s41467-023-37430-y. This article has 15 citations and is from a highest quality peer-reviewed journal.
(sone2023lossoffunction pages 1-2): Masato Sone, Kantawat Navanopparatsakul, Shunsuke Takahashi, Chikara Furusawa, and Takashi Hirasawa. Loss of function of hog1 improves glycerol assimilation in saccharomyces cerevisiae. World Journal of Microbiology & Biotechnology, Jul 2023. URL: https://doi.org/10.1007/s11274-023-03696-z, doi:10.1007/s11274-023-03696-z. This article has 8 citations and is from a peer-reviewed journal.
(zeinoun2023hog1actsin pages 1-6): Bechara Zeinoun, Maria Teresa Teixeira, and Aurélia Barascu. Hog1 acts in a mec1-independent manner to counteract oxidative stress following telomerase inactivation. BioRxiv, Oct 2023. URL: https://doi.org/10.1101/2023.10.04.560866, doi:10.1101/2023.10.04.560866. This article has 0 citations.
(tatebayashi2003adockingsite pages 6-7): K. Tatebayashi, M. Takekawa, and H. Saito. A docking site determining specificity of pbs2 mapkk for ssk2/ssk22 mapkkks in the yeast hog pathway. The EMBO Journal, 22:3624-3634, Jul 2003. URL: https://doi.org/10.1093/emboj/cdg353, doi:10.1093/emboj/cdg353. This article has 142 citations.
(murakami2008twoadjacentdocking pages 10-11): Yulia Murakami, Kazuo Tatebayashi, and Haruo Saito. Two adjacent docking sites in the yeast hog1 mitogen-activated protein (map) kinase differentially interact with the pbs2 map kinase kinase and the ptp2 protein tyrosine phosphatase. Apr 2008. URL: https://doi.org/10.1128/mcb.01817-07, doi:10.1128/mcb.01817-07. This article has 72 citations and is from a domain leading peer-reviewed journal.
(reiser2000polarizedlocalizationof pages 2-3): Vladimír Reiser, Suhal M. Salah, and Gustav Ammerer. Polarized localization of yeast pbs2 depends on osmostress, the membrane protein sho1 and cdc42. Nature Cell Biology, 2:620-627, Sep 2000. URL: https://doi.org/10.1038/35023568, doi:10.1038/35023568. This article has 193 citations and is from a highest quality peer-reviewed journal.
(reiser2000polarizedlocalizationof pages 6-7): Vladimír Reiser, Suhal M. Salah, and Gustav Ammerer. Polarized localization of yeast pbs2 depends on osmostress, the membrane protein sho1 and cdc42. Nature Cell Biology, 2:620-627, Sep 2000. URL: https://doi.org/10.1038/35023568, doi:10.1038/35023568. This article has 193 citations and is from a highest quality peer-reviewed journal.
(reiser2000polarizedlocalizationof pages 5-6): Vladimír Reiser, Suhal M. Salah, and Gustav Ammerer. Polarized localization of yeast pbs2 depends on osmostress, the membrane protein sho1 and cdc42. Nature Cell Biology, 2:620-627, Sep 2000. URL: https://doi.org/10.1038/35023568, doi:10.1038/35023568. This article has 193 citations and is from a highest quality peer-reviewed journal.