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Cited by 5Protein Kinase Regulation and GTPase SignalingFungal and yeast genetics researchGene Regulatory Network Analysis

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Phosphoregulation of the novel hemi-arrestin MAPK scaffold Sms1 prevents untimely mating

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Sieber, Boris, Merlini, Laura, Li, Wanlan, Besomi, Maëlys, Michon, Laetitia, Gordon-Lennox, Sushila, Martin, Sophie G.·2026·Nature Communications
DOI 10.1038/s41467-026-70631-9

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Abstract

Mitogen-activated protein kinases (MAPK) are ancestral kinases that form essential signalling cascades. However, scaffolds that recruit kinases to subcellular locations and promote signal transduction have only been described in a few species. Notably, no scaffold was thought necessary for the MAPK cascade promoting sexual differentiation in fission yeast. Here, we identify the hemi-arrestin protein Sms1 as a novel scaffold of this MAPK cascade. Interactions with PIP2 and the pheromone receptor–coupled Gα subunit target Sms1 to plasma membrane patches, where it assembles the active cascade by binding each MAP kinase. These interactions are essential for signal transduction and local signal interpretation for polarised growth. Phosphorylation, including by the MAPK itself, antagonises Sms1 membrane translocation, establishing a negative feedback that underlies polarity patch turnover and prevents untimely mating attempts. Thus, Sms1 is a MAPK scaffold with canonical functions despite its distinct structural fold, highlighting convergent evolution of MAPK scaffolds across eukaryotes.

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Metadata

Authors
Sieber, B., Merlini, L., Li, W., Besomi, M., Michon, L., Gordon-Lennox, S., & Martin, S. G.
Affiliations
University of Geneva (CH)
Corresponding author
  • Sieber, Boris
  • Martin, Sophie G.
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2026-03-17
Volume
17
Issue
1
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-026-70631-9
OpenAlex
W7138101677
Cited by
5
References
6
Citations by year
2026: 4
FWCI
8.21
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gene Regulatory Network Analysis
Keywords
mitogen-activated protein kinase cascade, pheromone signalling, mating, sexual differentiation, phosphatidylinositol 4,5-bisphosphate, phosphoregulation, membrane translocation, negative feedback, Schizosaccharomyces pombe
MeSH terms
Cell Membrane, Phosphorylation, Schizosaccharomyces, Signal Transduction, Arrestins, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System, Schizosaccharomyces pombe Proteins

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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