ArticleAnnals of botany2011
Interaction of a 14-3-3 protein with the plant microtubule-associated protein EDE1.
Article in Annals of botany, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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Who cites it
10 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.
- Meta-analysis of drought-tolerant genotypes in Oryza sativa: A network-based approach.PloS one · 2019Pooled it
- Calmodulin-Domain Protein Kinase PiCDPK1 Interacts with the 14-3-3-like Protein NtGF14 to Modulate Pollen Tube Growth.Plants (Basel, Switzerland) · 2024Article
- B1-type cyclins control microtubule organization during cell division in Arabidopsis.EMBO reports · 2022Article
- Repair of sub-lethal freezing damage in leaves of Arabidopsis thaliana.BMC plant biology · 2020Article
- Proteomic Analysis of Microtubule Interacting Proteins over the Course of Xylem Tracheary Element Formation in Arabidopsis.The Plant cell · 2015Article
- 14-3-3 Proteins in Guard Cell Signaling.Frontiers in plant science · 2015Review
- The yeast two-hybrid and related methods as powerful tools to study plant cell signalling.Plant molecular biology · 2013Review
- Evidence for the requirement of 14-3-3eta (YWHAH) in meiotic spindle assembly during mouse oocyte maturation.BMC developmental biology · 2013Article
- 14-3-3 proteins SGF14c and SGF14l play critical roles during soybean nodulation.Plant physiology · 2012Article
- The plant cell cycle.Annals of botany · 2011Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
BACKGROUND AND
aimsThe cell cycle-regulated protein ENDOSPERM DEFECTIVE 1 (EDE1) is a novel plant microtubule-associated protein essential for plant cell division and for microtubule organization in endosperm. EDE1 is only present on microtubules at mitosis and its expression is highly cell cycle regulated both at the protein and the transcript levels.
methodsTo search for EDE1-interacting proteins, a yeast two-hybrid screen was used in which EDE1 was fused with GAL4 DNA binding domain and expressed in a yeast strain that was then mated with a strain carrying a cDNA library fused to the GAL4 transactivation domain. Candidate interacting proteins were identified and confirmed in vitro. KEY
results14-3-3 upsilon was isolated several times from the library screen. In in vitro tests, it also interacted with EDE1: 14-3-3 upsilon most strongly associates with EDE1 in its free form, but also weakly when EDE1 is bound to microtubules. This study shows that EDE1 is a cyclin-dependent kinase substrate but that phosphorylation is not required for interaction with 14-3-3 upsilon.
conclusionsThe results suggest that 14-3-3 proteins may play a role in cytoskeletal organization of plant cells. The potential role of this interaction in the dynamics of EDE1 during the cell cycle is discussed.
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