ArticlePlant & cell physiology2016
Identification of Phosphoinositide-Binding Protein PATELLIN2 as a Substrate of Arabidopsis MPK4 MAP Kinase during Septum Formation in Cytokinesis.
Article in Plant & cell physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Molecular Drivers of Developmental Arrest in the Human Preimplantation Embryo: A Systematic Review and Critical Analysis Leading to Mapping Future Research.International journal of molecular sciences · 2021Pooled it
- Melatonin at Crossroads with Phytohormones: Interactions Under High Light Stress.International journal of molecular sciences · 2025Article
- Arabidopsis Produces Distinct Subpopulations of Extracellular Vesicles That Respond Differentially to Biotic Stress, Altering Growth and Infectivity of a Fungal Pathogen.Journal of extracellular vesicles · 2025Article
- Global landscape of protein phosphorylation during plant regeneration initiation in cotton (Gossypium hirsutum L.).BMC biology · 2025Article
- Genome-Wide Identification of MKK Gene Family and Response to Hormone and Abiotic Stress in Rice.Plants (Basel, Switzerland) · 2024Article
- Methyl viologen-induced changes in the Arabidopsis proteome implicate PATELLIN 4 in oxidative stress responses.Journal of experimental botany · 2024Article
- Endocytosis-mediated entry of a caterpillar effector into plants is countered by Jasmonate.Nature communications · 2023Article
- Identification and Expression Analysis of Phosphatidylinositol Transfer Proteins Genes in Rice.Plants (Basel, Switzerland) · 2023Article
- SEC14-GOLD protein PATELLIN2 binds IRON-REGULATED TRANSPORTER1 linking root iron uptake to vitamin E.Plant physiology · 2023Article
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- Mitogen-Activated Protein Kinase 4-Regulated Metabolic Networks.International journal of molecular sciences · 2022Article
- Phosphorylation of BIK1 is critical for interaction with downstream signaling components.Genes & genomics · 2021Article
- Attracted to membranes: lipid-binding domains in plants.Plant physiology · 2021Article
- Phylogenetic analysis of plant multi-domain SEC14-like phosphatidylinositol transfer proteins and structure-function properties of PATELLIN2.Plant molecular biology · 2020Article
- The Solanum chacoense Fertilization-Related Kinase 3 (ScFRK3) is involved in male and female gametophyte development.BMC plant biology · 2019Article
- Genome-wide identification, phylogeny, and expression analysis of Sec14-like PITP gene family in sugarcane.Plant cell reports · 2019Article
- Anionic Lipids: A Pipeline Connecting Key Players of Plant Cell Division.Frontiers in plant science · 2019Review
- Nuclear Signaling of Plant MAPKs.Frontiers in plant science · 2018Review
- Coevolving MAPK and PID phosphosites indicate an ancient environmental control of PIN auxin transporters in land plants.FEBS letters · 2018Article
- Feedback Microtubule Control and Microtubule-Actin Cross-talk inMolecular & cellular proteomics : MCP · 2017Article
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6 authors.
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Abstract
The phosphorylation of proteins by protein kinases controls many cellular and physiological processes, which include intracellular signal transduction. However, the underlying molecular mechanisms of such controls and numerous substrates of protein kinases remain to be characterized. The mitogen-activated protein kinase (MAPK) cascade is of particular importance in a variety of extracellular and intracellular signaling processes. In plant cells, the progression of cytokinesis is an excellent example of an intracellular phenomenon that requires the MAPK cascade. However, the way in which MAPKs control downstream processes during cytokinesis in plant cells remains to be fully determined. We show here that comparisons, by two-dimensional difference gel electrophoresis, of phosphorylated proteins from wild-type Arabidopsis thaliana and mutant plants defective in a MAPK cascade allow identification of substrates of a specific MAPK. Using this method, we identified the PATELLIN2 (PATL2) protein, which has a SEC14 domain, as a substrate of MPK4 MAP kinase. PATL2 was concentrated at the cell division plane, as is MPK4, and had binding affinity for phosphoinositides. This binding affinity was altered after phosphorylation of PATL2 by MPK4, suggesting a role for the MAPK cascade in the formation of cell plates via regeneration of membranes during cytokinesis.
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