PROTEIN PHOSPHATASE 2A B′η drives spliceosome subunit dephosphorylation to mediate alternative splicing following heat stress
Seung Hee Jo, Hyun Ji Park, Haemyeong Jung, Ga Seul Lee, Jeong Hee Moon, Hyun‐Soon Kim, Hyo‐Jun Lee, Choonkyun Jung, Hye Sun Cho
Abstract
Dephosphorylation of spliceosome components is an essential regulatory step for intron removal from pre-mRNA, thereby controlling gene expression. However, the specific phosphatase responsible for this dephosphorylation step has not been identified. Here, we show that Arabidopsis thaliana (Arabidopsis) PROTEIN PHOSPHATASE 2A B'η (PP2A B'η), a B subunit of PP2A, interacts with the splicing factors PRP18a, PRP16, and RH2 and facilitates their dephosphorylation by recognizing substrates through a conserved binding motif. This dephosphorylation is crucial for proper splicing of retained introns in heat stress-responsive genes, which is mediated by the PP2A interactor PRE-MRNA PROCESSING FACTOR 18a. Genetic inactivation of PP2A B'η abolished thermotolerance during seed germination and resulted in widespread intron retention in heat stress-responsive genes. Conversely, overexpression of PP2A B'η conferred enhanced thermotolerance, accompanied by the efficient removal of retained introns under heat stress. We demonstrate that a B regulatory subunit of PP2A plays a central role in dephosphorylating spliceosome components, regulating alternative splicing, facilitating acclimation to heat stress, and targeting specific spliceosome subunits that activate pre-mRNA splicing.