Function
KIN10 is the catalytic subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex. This complex plays a pivotal role in cellular energy homeostasis. It responds to diverse stimuli including darkness, sugar fluctuations, and stress conditions. This response leads to the activation of energy-producing pathways and the inhibition of energy-consuming processes. KIN10 is believed to be involved in signal transduction cascades that regulate gene expression and carbohydrate metabolism in higher plants. The SnRK complex is also thought to participate in regulating fatty acid synthesis by phosphorylating acetyl-CoA carboxylase, and in nitrogen assimilation by phosphorylating nitrate reductase.
In vitro studies have shown that KIN10 exhibits kinase activity towards sucrose phosphate synthase. This activity is inhibited by PRL1. KIN10 may be a subunit of a SCF ubiquitin ligase complex, potentially involved in proteasomal ubiquitination. It has been observed to phosphorylate GRIK1/SNAK2 and GRIK2/SNAK1 in vitro.
KIN10 cooperates with FUS3 to regulate developmental phase transitions and lateral organ development, acting as positive regulators of abscisic acid (ABA) signaling during germination. It phosphorylates FUS3 within the embryo. KIN10 negatively modulates MYC2 accumulation through protein phosphorylation. It also phosphorylates the AL2 protein of geminiviruses (CaLCuV, TGMV, ToMoV), leading to a delay in viral DNA accumulation and symptom appearance during infection.
KIN10 regulates bZIP63 activity to alter metabolism in response to starvation through protein phosphorylation. Under sugar deprivation conditions, KIN10 antagonizes the IDD8 function in flowering time control by phosphorylating it. KIN10 plays a crucial role in the control of cell proliferation through inhibiting KRP6 activity by phosphorylation. During submergence, KIN10 phosphorylates PTP1, leading to the release of the MPK6 signaling pathway inhibition. KIN10 triggers its own SUMO-mediated proteasomal degradation, establishing a negative feedback loop that attenuates SnRK1 signaling and prevents excessive activation of stress responses.
KIN10 phosphorylates RAPTOR1B and HMGR1S in vitro. Its kinase activity is sensitive to redox changes. KIN10 acts upstream of TOR in the regulation of autophagy. It is essential for the activation of autophagy by various abiotic stresses. KIN10 is involved in the positive regulation of autophagy, potentially by affecting the phosphorylation of ATG1 proteins. It negatively modulates WRI1 accumulation through protein phosphorylation. KIN10 modulates leaf senescence progression by negatively regulating EIN3 accumulation through phosphorylation. Under extended darkness, the C/S1-bZIP-SnRK1 complex interacts with histone acetylation machinery to remodel chromatin and facilitate transcription. The BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to upregulate its transcription. Finally, KIN10 phosphorylates and downregulates IPK2b in vitro. It is involved in the regulation of sucrose-induced hypocotyl elongation under light/dark cycles.