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LC-MSMS analysis in Arabidopsis thaliana

ABSTRACT: Spliceosome dephosphorylation is essential control step that enables intron removal from pre-mRNA for the regulation of gene expression. However, the phosphatase that is biologically responsible has not been identified. Here we show that PP2A B́ η, a B subunit of PP2A phosphatase, associates with spliceosome B* to C* complex and dephosphorylates spliceosome regulators by the most-conserved its binding motif that can be absolutely regimented interaction with PP2A substrates.

INSTRUMENT(S): Orbitrap Exploris 240

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Seedling, Seed

SUBMITTER: Seung Hee Jo

LAB HEAD: Hye Sun Cho

PROVIDER: PXD047933 | Pride | 2025-06-02

REPOSITORIES: Pride

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			Action	DRS
	20210917_SHJo_GelSample.raw	Raw
	20220607SHCho01.raw	Raw
	20220607SHCho02.raw	Raw
	20220607SHCho03.raw	Raw
	20220607SHCho07.raw	Raw

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Publications

PROTEIN PHOSPHATASE 2A B'η drives spliceosome subunit dephosphorylation to mediate alternative splicing following heat stress.

Jo Seung Hee SH Park Hyun Ji HJ Jung Haemyeong H Lee Ga Seul GS Moon Jeong Hee JH Kim Hyun-Soon HS Lee Hyo-Jun HJ Jung Choonkyun C Cho Hye Sun HS

The Plant cell 20250501 5

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 c ...[more]

PMID: 40359319

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Mapping the substrate landscape of protein phosphatase 2A catalytic subunit PPP2CA

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