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A deep origin of the RAF–SnRK2–PP2C functional module with distinctive ancestral features

ABSTRACT: The SNF1-related protein kinase 2 (SnRK2) pathway is central to abiotic stress signaling in land plants; however, its evolutionary origin and ancestral functions remain poorly understood. Here, we identify and characterize a functional SnRK2 signaling module in the unicellular green alga Chlamydomonas reinhardtii. We demonstrate that the algal isoform SnRK2.7 is essential for osmotic stress tolerance, providing a pre- abscisic acid (ABA) model system for characterizing SnRK2 signaling. Functional analysis reveals that SnRK2.7 exhibits key regulatory elements conserved in land plant SnRK2s, but also displays lineage-specific features: it is required for general cellular viability in algae and localizes to the contractile vacuole—an osmoregulatory organelle lost during streptophyte evolution. Notably, SnRK2.7 phosphorylates PP2C3, a clade A protein phosphatase, revealing an ancestral regulatory logic distinct from that in angiosperms, where PP2Cs functions upstream, dephosphorylating SnRK2 proteins. Together with MAPKKK3, a B1/B3-RAF kinase, these proteins form an evolutionarily ancient SnRK2 signaling module. Our findings reveal that a sophisticated SnRK2 pathway predates both the evolution of ABA signaling and plant terrestrialization, implying key regulatory innovations that emerged during chlorophyte-streptophyte divergence.

INSTRUMENT(S):

ORGANISM(S): Chlamydomonas Reinhardtii

SUBMITTER: GKN JK

LAB HEAD: Xiaobo Li

PROVIDER: PXD072844 | Pride | 2026-07-02

REPOSITORIES: Pride

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			Action	DRS
	MS2200647_C2_flag.raw	Raw
	MS2200647_C7_flag.raw	Raw
	MS2200647_C8_flag.raw	Raw
	MS2200647_WT_flag.raw	Raw
	MS2200647_flag_LFQ_nn.msf	Msf

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A RAF–SnRK2–PP2C functional module regulates cell survival in the chlorophyte Chlamydomonas reinhardtii

Project description:The SNF1-related protein kinase 2 (SnRK2) pathway is a central regulator of abiotic stress signaling in land plants; however, its evolutionary origins and functional conservation across the green lineage remain poorly understood. Land plants evolved from streptophyte algae, whereas the chlorophyte algae, including the widely studied model Chlamydomonas reinhardtii, represent an older lineage that diverged from streptophytes over one billion years ago. Here, we identify and characterize a functional SnRK2 signaling module in Chlamydomonas reinhardtii. We show that the isoform SnRK2.7 is required for osmotic stress tolerance and general cellular viability, thus offering an alternative model for dissecting SnRK2 functions in algae. SnRK2.7 localizes to the contractile vacuole, an osmoregulatory organelle lost during streptophyte evolution, revealing a lineage-specific functional adaptation. Together with MAPKKK3, a B1/B3-RAF kinase, and the clade A protein phosphatase PP2C3, these components constitute a SnRK2 signaling module in Chlamydomonas reinhardtii. Our findings demonstrate the presence of a functional SnRK2 pathway in a chlorophyte alga, indicating that core components were established early in the green lineage. This work provides a foundation for comparative studies across green plants and underscores the need for broader taxonomic sampling to reconstruct the ancestral signaling networks underlying stress adaptation.

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The C-terminal domains SnRK2-box and ABA-box have a role in sugarcane SnRK2s auto-activation and activity

Project description:Resistance to drought stress is fundamental to plant survival and development. Abscisic acid (ABA) is one of the major hormones involved in different types of abiotic and biotic stress responses. ABA intracellular signaling has been extensively explored in Arabidopsis thaliana and occurs via a phosphorylation cascade mediated by three related protein kinases, denominated SnRK2s (SNF1-related protein kinases). However, the role of ABA signaling and the biochemistry of SnRK2 in crop plants remains underexplored. Considering the importance of the ABA hormone in abiotic stress tolerance, here we investigated the regulatory mechanism of sugarcane SnRK2s - known as SAPKs (Stress/ABA-activated Protein Kinases). The crystal structure of ScSAPK10 revealed the characteristic SnRK2 family architecture, in which the regulatory SnRK2-box interacts with the kinase domain αC helix. To study sugarcane SnRK2 regulation, we produced a series of mutants for the protein regulatory domains SnRK2-box and ABA-box. Surprisingly, mutations in the SnRK2-box did not drastically affect sugarcane SnRK2 activity, in contrast to previous observations for the homologous proteins in Arabidopsis. Also, we found that the ABA-box might have a role in SnRK2 activation in the absence of PP2C phosphatase. Taken together, our results demonstrate that both C-terminal domains of sugarcane SnRK2 proteins play a role in protein activation and activity.

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