{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["200(1)"],"submitter":["Melicher P"],"funding":["Palacký University Olomouc student","Palacky University Young Researcher"],"pubmed_abstract":["The generation of reactive oxygen species (ROS) and their regulation by antioxidant enzymes, such as IRON SUPEROXIDE DISMUTASE 1 (FSD1), are critical for managing plant responses to salt stress. However, the protein networks modulating ROS levels during salt stress remain incompletely understood. Our co-immunoprecipitation analysis identified FSD1 as an interaction partner of the scaffolding protein RECEPTOR FOR ACTIVATED C KINASE 1A (RACK1A). Bimolecular fluorescence complementation analysis revealed that RACK1A interacts with FSD1 predominantly in the cytoplasm. Despite elevated FSD1 activity in rack1a mutants, the abundance of FSD1 protein remained unchanged. Additionally, we found that the RACK1A-FSD1 module was involved in root hair tip growth, highlighting the developmental significa"],"journal":["Plant physiology"],"pagination":["kiaf659"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12853880"],"repository":["biostudies-literature"],"pubmed_title":["RACK1A interacts and colocalizes with FSD1 in stress granules to regulate salt stress response in Arabidopsis."],"pmcid":["PMC12853880"],"pubmed_authors":["Hlavackova K","Tsinyk M","Dvorak P","Ovecka M","Rehak J","Takac T","Samaj J","Melicher P","Samajova O"],"additional_accession":[]},"is_claimable":false,"name":"RACK1A interacts and colocalizes with FSD1 in stress granules to regulate salt stress response in Arabidopsis.","description":"The generation of reactive oxygen species (ROS) and their regulation by antioxidant enzymes, such as IRON SUPEROXIDE DISMUTASE 1 (FSD1), are critical for managing plant responses to salt stress. However, the protein networks modulating ROS levels during salt stress remain incompletely understood. Our co-immunoprecipitation analysis identified FSD1 as an interaction partner of the scaffolding protein RECEPTOR FOR ACTIVATED C KINASE 1A (RACK1A). Bimolecular fluorescence complementation analysis revealed that RACK1A interacts with FSD1 predominantly in the cytoplasm. Despite elevated FSD1 activity in rack1a mutants, the abundance of FSD1 protein remained unchanged. Additionally, we found that the RACK1A-FSD1 module was involved in root hair tip growth, highlighting the developmental significa","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-15T03:16:02.419Z","creation":"2026-06-15T03:08:46.227Z"},"accession":"S-EPMC12853880","cross_references":{"pubmed":["41408657"],"doi":["10.1093/plphys/kiaf659"]}}