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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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 gene symbol KDX1 corresponds to the Saccharomyces cerevisiae gene MLP1 (Mpk1-Like Protein kinase 1), with the systematic name YKL161C. The protein is also designated as "Kinase Dead X-talker protein 1" (UniProt: P36005). It belongs to the protein kinase superfamily and contains MAP kinase-like domains (IPR050117, IPR000719), consistent with its identity as a pseudokinase paralog of the Slt2/Mpk1 MAPK in the cell wall integrity (CWI) signaling pathway (levin2011regulationofcell pages 15-16).
KDX1/MLP1 encodes a pseudokinase — a protein that adopts a kinase-like fold but is catalytically inactive. Despite its annotation as a serine/threonine protein kinase (EC 2.7.11.1), extensive biochemical studies have failed to detect protein kinase activity for Mlp1 (levin2011regulationofcell pages 15-16). The protein lacks several residues recognized as critical for protein kinase catalytic function. Most notably, the conserved Thr residue within the canonical MAPK dual phosphorylation site (Thr-X-Tyr) of the activation loop is replaced by a Lys residue in Mlp1, rendering it unable to undergo the dual phosphorylation required for typical MAPK catalytic activation (levin2011regulationofcell pages 15-16).
Rather than functioning as a kinase, Mlp1 serves as a noncatalytic transcriptional regulator in the CWI signaling pathway, where it is redundant with Mpk1/Slt2 specifically for noncatalytic transcriptional functions (levin2011regulationofcell pages 15-16, levin2011regulationofcell pages 16-18). It does not phosphorylate substrates; instead, it regulates gene expression through direct protein-protein interactions at gene promoters and coding regions.
Despite lacking kinase activity, Mlp1 requires activation through phosphorylation to carry out its signaling functions. It is phosphorylated by the upstream MAP kinase kinases (MAPKKs) Mkk1 and Mkk2 of the CWI pathway (levin2011regulationofcell pages 16-18, levin2011regulationofcell pages 8-9). However, unlike canonical MAPKs that require dual phosphorylation of both Thr and Tyr residues in their activation loop, Mlp1 is activated by single phosphorylation at Tyr192 (levin2011regulationofcell pages 16-18). This phosphorylation induces an active conformation that is essential for its downstream signaling functions, even though the protein itself does not catalyze phosphotransfer reactions. Like other MAPKs, Mlp1 associates with its targets and regulators through a canonical D (docking) motif (levin2011regulationofcell pages 8-9).
The CWI pathway is a MAPK cascade in S. cerevisiae that responds to cell wall damage and other stresses threatening cell integrity. The canonical cascade proceeds from cell surface sensors through Rho1 GTPase → Pkc1 → Bck1 (MAPKKK) → Mkk1/Mkk2 (MAPKKs) → Slt2/Mpk1 (MAPK). Mlp1 functions at the level of the MAPK as a pseudokinase paralog of Slt2/Mpk1, receiving the same upstream activating signal from Mkk1/Mkk2 (levin2011regulationofcell pages 15-16, heinisch2018proteinkinasec pages 9-13).
The CWI pathway controls gene expression through two principal transcription factors: Rlm1 and SBF (Swi4/Swi6). While Rlm1 is activated by direct catalytic phosphorylation by Mpk1, the activation of SBF occurs through a remarkable noncatalytic mechanism that both Mpk1 and Mlp1 carry out redundantly (levin2011regulationofcell pages 16-18, levin2011regulationofcell pages 15-16).
This noncatalytic mechanism involves two essential steps:
Step 1 — Transcription Initiation: Activated Mlp1 (or Mpk1) binds to a D motif on the Swi4 subunit of SBF that is adjacent to the C-terminal Swi6-binding site. This binding relieves the auto-inhibitory intramolecular association within Swi4, allowing it to bind DNA at SBF-binding sites (SCB elements) in the promoters of cell wall stress-activated genes (levin2011regulationofcell pages 16-18). Although Mlp1/Mpk1 substitutes for Swi6 in enabling Swi4 DNA binding, Swi6 must subsequently be recruited to the Mlp1–Swi4 complex to form a functional trimeric complex on the promoter. This trimeric Mlp1–Swi4–Swi6 complex is required for recruitment of RNA polymerase II (Pol II) to the promoter (levin2011regulationofcell pages 16-18).
Step 2 — Antitermination/Transcription Elongation: After the initiation complex is assembled, Mlp1/Mpk1 moves from the promoter to the coding region of the gene through a "hand-off" from Swi4 to the Paf1 complex (Paf1C), which is associated with the elongating RNA Pol II (levin2011regulationofcell pages 18-19, levin2011regulationofcell pages 16-18). The interaction between Mpk1/Mlp1 and the Paf1 subunit of Paf1C occurs via a D motif in Paf1. This interaction is critical because it blocks recruitment of the Sen1–Nrd1–Nab3 termination complex to the elongating polymerase, thereby overcoming transcriptional attenuation that would otherwise lead to premature termination (levin2011regulationofcell pages 18-19). Under non-inducing conditions, a single Nab3-binding site within the FKS2 promoter-proximal region mediates transcriptional attenuation, minimizing FKS2 expression in the absence of stress (levin2011regulationofcell pages 18-19).
Importantly, this mechanism does not require kinase catalytic activity — a mutation in the ATP-binding site of Mpk1 (mpk1-K54R) does not impair FKS2 transcription, and FKS2 expression was actually slightly enhanced in this catalytically inactive mutant (levin2011regulationofcell pages 18-19). However, the active phosphorylated conformation is required: a mutation blocking activation loop phosphorylation (mpk1-TA/YF) abolished transcription (levin2011regulationofcell pages 16-18).
Genes under the control of this noncatalytic SBF-dependent pathway branch include FKS2 (encoding β-1,3-glucan synthase, critical for cell wall biosynthesis), CHA1, YLR042C, and YKR013W, though this is likely not a complete list (levin2011regulationofcell pages 16-18).
The MLP1 gene is itself a transcriptional target of the CWI pathway, creating a biologically significant positive feedback loop. Mpk1 catalytically phosphorylates and activates the Rlm1 transcription factor at two residues (Ser427 and Thr439) within its activation domain (levin2011regulationofcell pages 15-16). Activated Rlm1 then directly induces MLP1 expression by binding to at least two functional Rlm1-binding sites (BOX1 and BOX2) in the MLP1 promoter (sanz2012chromatinremodelingby pages 5-7, sanz2012chromatinremodelingby pages 9-10). This transcriptional activation requires coordination between Rlm1 and the SWI/SNF chromatin remodeling complex: upon cell wall stress, Slt2 activates Rlm1, which recruits SWI/SNF to the MLP1 promoter, leading to nucleosome displacement and histone H3 eviction that expose the Rlm1-binding sites (sanz2012chromatinremodelingby pages 9-10, sanz2012chromatinremodelingby pages 7-8). Additionally, the SAGA complex cooperates with SWI/SNF for full gene expression at CWI-responsive genes (sanz2012chromatinremodelingby pages 5-7).
Because MLP1 encodes a protein that then reinforces the noncatalytic transcriptional branch of the pathway, this creates a feedback loop that selectively amplifies the SBF-dependent transcriptional output (levin2011regulationofcell pages 15-16). MLP1 is one of the most strongly induced genes in the CWI pathway: in response to cell wall damage, MLP1 transcript levels increase approximately 4.2-fold at 2 hours, 9.4-fold at 4 hours, and up to 24.4-fold upon zymolyase treatment (garcia2004theglobaltranscriptional pages 3-4). At the protein level, Mlp1 levels increase by approximately ~100-fold during cell wall stress (levin2011regulationofcell pages 15-16).
The robustness of MLP1 induction has made the MLP1 promoter a widely used reporter system for CWI pathway activation. Fusions of the MLP1 promoter Rlm1-binding elements to minimal promoter-lacZ constructs create functional reporters that are strongly induced by cell wall stress agents (sanz2012chromatinremodelingby pages 5-7, sellersmoya2021clotrimazoleinducedoxidativestress pages 10-12).
The site of Mlp1 function is primarily nuclear, at the chromatin of cell wall stress-responsive gene promoters and coding regions. Chromatin immunoprecipitation (ChIP) experiments have demonstrated that activated Mlp1 (like Mpk1) forms complexes with Swi4 at SBF-binding sites in the promoters of target genes, then moves to coding regions during transcription elongation (levin2011regulationofcell pages 16-18). By analogy with Mpk1 — which is predominantly nuclear under non-stress conditions but can relocalize to the cytoplasm and to sites of polarized cell growth upon stress (levin2005cellwallintegrity pages 13-14, levin2005cellwallintegrity pages 2-3) — Mlp1 likely also shuttles between nuclear and cytoplasmic compartments. Activated Mlp1 can also mediate Swi6 recruitment to the nucleus through a noncatalytic mechanism, further supporting its nuclear function during stress-induced transcription (levin2011regulationofcell pages 18-19).
In addition, MLP1 mRNA itself is subject to post-transcriptional regulation: during cell wall stress, MLP1 mRNA becomes concentrated in cytoplasmic P-bodies (processing bodies) that colocalize with the decapping factor Dcp2, suggesting regulated mRNA turnover or storage as part of the stress response (garcia2019signallingthroughthe pages 7-8).
Beyond the classical cell wall stress response to agents such as Congo red, Calcofluor white, and zymolyase, Mlp1/MLP1 induction has been documented in response to clotrimazole (an imidazole antifungal). Even minimal induction of the MLP1 promoter by clotrimazole is sufficient to activate an Integrity Pathway Activation Circuit (IPAC) that amplifies CWI pathway signals and renders cells hypersensitive to CWI-activating agents (sellersmoya2021clotrimazoleinducedoxidativestress pages 10-12). This highlights MLP1 as a functional amplifier of CWI stress signaling circuitry beyond classical cell wall-damaging agents.
The noncatalytic transcriptional mechanism carried out by Mpk1/Mlp1 is evolutionarily conserved. Both noncatalytic functions of Mpk1/Mlp1 — transcription initiation at SBF-dependent promoters and antitermination via the Paf1C — are complemented by human ERK5 MAPK, and the MAPK–Paf1 interaction is conserved between yeast Mpk1 and human ERK5/Paf1 (levin2011regulationofcell pages 18-19). This conservation underscores the fundamental biological importance of noncatalytic MAPK signaling mechanisms.
The following table provides a consolidated overview of the key properties and evidence for KDX1/MLP1:
| Property | Summary | Evidence |
|---|---|---|
| Gene / protein identity | KDX1 in the prompt matches the budding yeast gene MLP1 / KDX1 / YKL161C encoding Mpk1-like protein kinase 1, a kinase-dead MAPK-like protein in Saccharomyces cerevisiae S288c. It is described as a paralog of Slt2/Mpk1 in the cell wall integrity (CWI) pathway. | (levin2011regulationofcell pages 15-16, levin2011regulationofcell pages 8-9) |
| Organism | Saccharomyces cerevisiae (baker’s yeast), strain background S288c in the cited reviews and functional studies. | (levin2011regulationofcell pages 15-16) |
| Primary function | Mlp1 is not a catalytically active MAP kinase; instead, it acts as a pseudokinase transcriptional regulator that functions redundantly with Mpk1 for the noncatalytic branch of CWI signaling, especially activation of SBF (Swi4/Swi6)-dependent cell wall stress genes. | (levin2011regulationofcell pages 15-16, levin2011regulationofcell pages 16-18, levin2011regulationofcell pages 8-9) |
| Enzymatic activity / substrate specificity | Despite UniProt kinase annotation, the literature indicates no demonstrable protein kinase catalytic activity for Mlp1; therefore, no bona fide catalytic substrate specificity has been established. Its biologically supported role is signaling by protein interaction rather than phosphotransfer. | (levin2011regulationofcell pages 8-9, levin2011regulationofcell pages 15-16) |
| Pseudokinase-defining features | Mlp1 lacks several residues critical for kinase catalysis, and the canonical MAPK activation-loop Thr-X-Tyr motif is altered: the Thr is replaced by Lys. These changes explain why it is considered a pseudokinase / “kinase-dead” paralog rather than a true MAPK. | (levin2011regulationofcell pages 15-16) |
| Activation mechanism | Mlp1 is activated downstream of the CWI MAPKKs Mkk1/Mkk2. Unlike canonical MAPKs, it is activated by single phosphorylation at Tyr192, not by dual Thr/Tyr phosphorylation. Its signaling output requires the phosphorylated active conformation, even though it lacks catalytic activity. | (levin2011regulationofcell pages 16-18) |
| Relationship to Slt2/Mpk1 | Mlp1 is a pseudokinase paralog of Slt2/Mpk1. It is largely redundant with Mpk1 for noncatalytic transcriptional functions, while Mpk1 additionally has catalytic functions such as phosphorylation of other substrates. Mlp1 therefore expands or reinforces the transcriptional arm of the CWI pathway rather than replacing all Slt2 functions. | (levin2011regulationofcell pages 15-16, levin2011regulationofcell pages 16-18, heinisch2018proteinkinasec pages 9-13) |
| Key interaction: Swi4 | Activated Mlp1 binds Swi4 at SBF-regulated promoters through MAPK docking interactions, relieving Swi4 autoinhibition and allowing promoter occupancy at cell wall stress genes such as FKS2. | (levin2011regulationofcell pages 16-18) |
| Key interaction: Swi6 | Mlp1 participates with Swi4 and Swi6 in a trimeric promoter complex needed for SBF-mediated transcription. Swi6 is required for productive transcriptional activation and RNA Pol II recruitment. | (levin2011regulationofcell pages 16-18) |
| Key interaction: Paf1 / Paf1C | After promoter recruitment, Mpk1/Mlp1 move into coding regions and engage the Paf1 complex (Paf1C) to support transcription elongation and prevent premature Sen1-Nrd1-Nab3-dependent termination. This is a core part of the noncatalytic mechanism driving FKS2 expression. | (levin2011regulationofcell pages 16-18, levin2011regulationofcell pages 18-19) |
| Key interaction: Mkk1/Mkk2 | The upstream MAPKKs Mkk1/Mkk2 are the activating kinases for both Mpk1 and Mlp1 in the CWI cascade; for Mlp1 the relevant documented activating event is Tyr192 phosphorylation. | (levin2011regulationofcell pages 16-18) |
| Key interaction: Rlm1 | Rlm1 is primarily an upstream transcription factor relative to MLP1 gene expression: Mpk1 activates Rlm1, and Rlm1 directly induces MLP1 transcription. Earlier transcriptomic work also noted MLP1 among SLT2-pathway genes and reported interaction context with Rlm1. | (garcia2004theglobaltranscriptional pages 3-4, sanz2012chromatinremodelingby pages 5-7, sanz2012chromatinremodelingby pages 9-10, levin2011regulationofcell pages 15-16) |
| Major regulated / associated target genes | Best-characterized SBF/CWI targets supported for Mpk1/Mlp1 noncatalytic control include FKS2, and reported pathway-branch genes include CHA1, YLR042C, and YKR013W. MLP1 itself is also a strongly induced Rlm1 target gene in cell wall stress. | (levin2011regulationofcell pages 16-18, levin2011regulationofcell pages 15-16) |
| Subcellular localization / site of action | Direct evidence places Mlp1 at promoters and coding regions of stress-induced genes during transcription. By analogy with the coupled Mpk1 system, the relevant functional compartment is largely nuclear chromatin-associated transcription complexes, though Mpk1 itself also shuttles between nucleus and cytoplasm under stress. | (levin2011regulationofcell pages 16-18, levin2005cellwallintegrity pages 13-14, levin2005cellwallintegrity pages 2-3, levin2011regulationofcell pages 18-19) |
| Biological pathway | Mlp1 functions in the cell wall integrity (CWI) MAPK pathway, especially the transcriptional response to cell wall damage and related stresses. It contributes to expression of genes needed for cell wall remodeling, integrity maintenance, and stress adaptation. | (levin2011regulationofcell pages 15-16, heinisch2018proteinkinasec pages 9-13) |
| Positive-feedback role in CWI signaling | MLP1 is induced by Rlm1, which is activated by Mpk1. Because Mlp1 then reinforces the noncatalytic transcriptional branch of the pathway, this creates a positive feedback loop that selectively amplifies CWI transcriptional output. | (levin2011regulationofcell pages 15-16) |
| Induction magnitude during cell wall stress | MLP1 is one of the most strongly induced CWI-pathway genes. Reported induction after transient cell wall damage reached about 4.2-fold at 2 h, 9.4-fold at 4 h, and 24.4-fold after zymolyase treatment in one transcriptomic study; review literature further notes that Mlp1 protein levels increase ~100-fold under cell wall stress. | (garcia2004theglobaltranscriptional pages 3-4, levin2011regulationofcell pages 15-16) |
| Promoter architecture / reporter use | The MLP1 promoter contains at least two functional Rlm1-binding sites and is stress responsive in reporter assays. Because of its robust induction, it has been used as a readout of CWI pathway activation. | (sanz2012chromatinremodelingby pages 5-7, sanz2012chromatinremodelingby pages 9-10, sanz2012chromatinremodelingby pages 7-8) |
| Recent / applied context | In newer work, low-level MLP1 induction was sufficient to engage an Integrity Pathway Activation Circuit (IPAC) that amplifies signaling in response to clotrimazole, highlighting MLP1 as a practical amplifier/readout of CWI stress circuitry beyond classic wall-damaging agents. | (sellersmoya2021clotrimazoleinducedoxidativestress pages 10-12) |
| Evolutionary perspective | The unusual noncatalytic transcriptional mechanism carried out by Mpk1/Mlp1 is functionally conserved enough that yeast studies found complementation by human ERK5, and the MAPK–Paf1 interaction is evolutionarily conserved. | (levin2011regulationofcell pages 18-19) |
Table: This table summarizes the verified identity, molecular function, pseudokinase features, pathway role, interactions, localization, and stress-inducible regulation of yeast KDX1/MLP1 (YKL161C). It is useful as a compact evidence map for the gene’s primary annotation in the cell wall integrity pathway.
In summary, KDX1/MLP1 (YKL161C) encodes a pseudokinase in Saccharomyces cerevisiae that, despite its kinase-like domain architecture, functions exclusively through noncatalytic mechanisms in the cell wall integrity MAPK signaling pathway. Activated by single tyrosine phosphorylation via the MAPKKs Mkk1/Mkk2, Mlp1 acts redundantly with the catalytically active MAPK Slt2/Mpk1 to drive SBF-dependent transcription of cell wall stress genes through a two-step mechanism involving transcription initiation (via interaction with Swi4/Swi6) and antitermination (via interaction with the Paf1 complex). Its expression is strongly induced by cell wall stress through an Rlm1-dependent transcriptional mechanism requiring SWI/SNF-mediated chromatin remodeling, establishing a positive feedback loop that selectively amplifies the noncatalytic transcriptional branch of the CWI pathway. KDX1/MLP1 thus represents a paradigmatic example of a pseudokinase with a precisely defined biological role: it functions as a stress-inducible transcriptional cofactor that amplifies cell wall integrity signaling output.
References
(levin2011regulationofcell pages 15-16): David E Levin. Regulation of cell wall biogenesis in saccharomyces cerevisiae: the cell wall integrity signaling pathway. Genetics, 189:1145-1175, Dec 2011. URL: https://doi.org/10.1534/genetics.111.128264, doi:10.1534/genetics.111.128264. This article has 1081 citations and is from a domain leading peer-reviewed journal.
(levin2011regulationofcell pages 16-18): David E Levin. Regulation of cell wall biogenesis in saccharomyces cerevisiae: the cell wall integrity signaling pathway. Genetics, 189:1145-1175, Dec 2011. URL: https://doi.org/10.1534/genetics.111.128264, doi:10.1534/genetics.111.128264. This article has 1081 citations and is from a domain leading peer-reviewed journal.
(levin2011regulationofcell pages 8-9): David E Levin. Regulation of cell wall biogenesis in saccharomyces cerevisiae: the cell wall integrity signaling pathway. Genetics, 189:1145-1175, Dec 2011. URL: https://doi.org/10.1534/genetics.111.128264, doi:10.1534/genetics.111.128264. This article has 1081 citations and is from a domain leading peer-reviewed journal.
(heinisch2018proteinkinasec pages 9-13): Jürgen J Heinisch and Rosaura Rodicio. Protein kinase c in fungi-more than just cell wall integrity. FEMS microbiology reviews, Oct 2018. URL: https://doi.org/10.1093/femsre/fux051, doi:10.1093/femsre/fux051. This article has 112 citations and is from a domain leading peer-reviewed journal.
(levin2011regulationofcell pages 18-19): David E Levin. Regulation of cell wall biogenesis in saccharomyces cerevisiae: the cell wall integrity signaling pathway. Genetics, 189:1145-1175, Dec 2011. URL: https://doi.org/10.1534/genetics.111.128264, doi:10.1534/genetics.111.128264. This article has 1081 citations and is from a domain leading peer-reviewed journal.
(sanz2012chromatinremodelingby pages 5-7): A. Belén Sanz, Raúl García, Jose Manuel Rodríguez-Peña, Sonia Díez-Muñiz, César Nombela, Craig L. Peterson, and Javier Arroyo. Chromatin remodeling by the swi/snf complex is essential for transcription mediated by the yeast cell wall integrity mapk pathway. Molecular Biology of the Cell, 23:2805-2817, Jul 2012. URL: https://doi.org/10.1091/mbc.e12-04-0278, doi:10.1091/mbc.e12-04-0278. This article has 88 citations and is from a domain leading peer-reviewed journal.
(sanz2012chromatinremodelingby pages 9-10): A. Belén Sanz, Raúl García, Jose Manuel Rodríguez-Peña, Sonia Díez-Muñiz, César Nombela, Craig L. Peterson, and Javier Arroyo. Chromatin remodeling by the swi/snf complex is essential for transcription mediated by the yeast cell wall integrity mapk pathway. Molecular Biology of the Cell, 23:2805-2817, Jul 2012. URL: https://doi.org/10.1091/mbc.e12-04-0278, doi:10.1091/mbc.e12-04-0278. This article has 88 citations and is from a domain leading peer-reviewed journal.
(sanz2012chromatinremodelingby pages 7-8): A. Belén Sanz, Raúl García, Jose Manuel Rodríguez-Peña, Sonia Díez-Muñiz, César Nombela, Craig L. Peterson, and Javier Arroyo. Chromatin remodeling by the swi/snf complex is essential for transcription mediated by the yeast cell wall integrity mapk pathway. Molecular Biology of the Cell, 23:2805-2817, Jul 2012. URL: https://doi.org/10.1091/mbc.e12-04-0278, doi:10.1091/mbc.e12-04-0278. This article has 88 citations and is from a domain leading peer-reviewed journal.
(garcia2004theglobaltranscriptional pages 3-4): Raúl García, Clara Bermejo, Cecilia Grau, Rosa Pérez, Jose Manuel Rodríguez-Peña, Jean Francois, César Nombela, and Javier Arroyo. The global transcriptional response to transient cell wall damage in saccharomyces cerevisiae and its regulation by the cell integrity signaling pathway*. Journal of Biological Chemistry, 279:15183-15195, Apr 2004. URL: https://doi.org/10.1074/jbc.m312954200, doi:10.1074/jbc.m312954200. This article has 418 citations and is from a domain leading peer-reviewed journal.
(sellersmoya2021clotrimazoleinducedoxidativestress pages 10-12): Ángela Sellers-Moya, Marcos Nuévalos, María Molina, and Humberto Martín. Clotrimazole-induced oxidative stress triggers novel yeast pkc1-independent cell wall integrity mapk pathway circuitry. Journal of Fungi, 7:647, Aug 2021. URL: https://doi.org/10.3390/jof7080647, doi:10.3390/jof7080647. This article has 26 citations.
(levin2005cellwallintegrity pages 13-14): David E. Levin. Cell wall integrity signaling in saccharomyces cerevisiae. Microbiology and Molecular Biology Reviews, 69:262-291, Jun 2005. URL: https://doi.org/10.1128/mmbr.69.2.262-291.2005, doi:10.1128/mmbr.69.2.262-291.2005. This article has 1478 citations and is from a domain leading peer-reviewed journal.
(levin2005cellwallintegrity pages 2-3): David E. Levin. Cell wall integrity signaling in saccharomyces cerevisiae. Microbiology and Molecular Biology Reviews, 69:262-291, Jun 2005. URL: https://doi.org/10.1128/mmbr.69.2.262-291.2005, doi:10.1128/mmbr.69.2.262-291.2005. This article has 1478 citations and is from a domain leading peer-reviewed journal.
(garcia2019signallingthroughthe pages 7-8): Raúl García, Verónica Pulido, Sara Orellana-Muñoz, César Nombela, Carlos R. Vázquez de Aldana, José M. Rodríguez-Peña, and Javier Arroyo. Signalling through the yeast mapk cell wall integrity pathway controls p-body assembly upon cell wall stress. Scientific Reports, Feb 2019. URL: https://doi.org/10.1038/s41598-019-40112-9, doi:10.1038/s41598-019-40112-9. This article has 40 citations and is from a peer-reviewed journal.