Unraveling the MAX2 Protein Network in Arabidopsis thaliana: Identification of the Protein Phosphatase PAPP5 as a Novel MAX2 Interactor.

作者: Sylwia Struk , Carolien De Cuyper , Anse Jacobs , Lukas Braem , Alan Walton

DOI: 10.1074/MCP.RA119.001766

关键词: InteractorTandem affinity purificationBimolecular fluorescence complementationChemistryCell biologyPhosphorylationKarrikinPhosphataseImmunoprecipitationCOP9 signalosome

摘要: Abstract The F-box protein MORE AXILLARY GROWTH 2 (MAX2) is a central component in the signaling cascade of strigolactones (SLs) as well smoke-derived karrikins (KARs) and so far unknown endogenous KAI2 ligand (KL). two groups molecules are involved overlapping unique developmental processes, signal-specific outcomes attributed to perception by paralogous α/β-hydrolases DWARF14 (D14) for SL KARRIKIN INSENSITIVE 2/HYPOSENSITIVE TO LIGHT (KAI2/HTL) KAR/KL. In addition, depending on which receptor activated, specific members SUPPRESSOR OF MAX2 1 (SMAX1)-LIKE (SMXL) family control KAR/KL responses. As proteins that function same signal transduction pathway often occur large complexes, we aimed at discovering new players MAX2, D14, network tandem affinity purification Arabidopsis cell cultures. When using bait, various were copurified, among general components Skp1-Cullin-F-box complex CONSTITUTIVE PHOTOMORPHOGENIC 9 signalosome. Here, report identification novel interactor type 5 serine/threonine phosphatase, designated PHYTOCHROME-ASSOCIATED PROTEIN PHOSPHATASE (PAPP5). Quantitative pointed PAPP5 being more present rather than D14 complexes. agreement, mutant analysis suggests modulates KAR/KL-dependent seed germination under suboptimal conditions seedling development. phosphopeptide enrichment experiment revealed might dephosphorylate in vivo independently synthetic analog, rac-GR24. Together, analyzing complexes belong, interactor, PAPP5, act through dephosphorylation mainly KAR/KL-related phenotypes and, hence, provide another link with light pathway.

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