ArticlePlant physiology2009
WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1.
Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 30 citations in OpenAlex.
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- Overexpression of AHL proteins enhances root hair production by altering the transcription of RHD6-downstream genes.Plant direct · 2023Article
- Recent advances in understanding the biological roles of the plant nuclear envelope.Nucleus (Austin, Tex.) · 2020Article
- Proximity labeling proteomics reveals critical regulators for inner nuclear membrane protein degradation in plants.Nature communications · 2020Article
- iTRAQ-based quantitative proteomic analysis reveals the lateral meristem developmental mechanism for branched spike development in tetraploid wheat (Triticum turgidum L.).BMC genomics · 2018Article
- Dynamic Changes in Plant Nuclear Organization in Response to Environmental and Developmental Signals.Plant physiology · 2018Review
- Feedback Microtubule Control and Microtubule-Actin Cross-talk inMolecular & cellular proteomics : MCP · 2017Article
- Targeting of tail-anchored membrane proteins to subcellular organelles in Toxoplasma gondii.Traffic (Copenhagen, Denmark) · 2017Article
- Nuclear Pore Permeabilization Is a Convergent Signaling Event in Effector-Triggered Immunity.Cell · 2016Article
- Enriching the pore: splendid complexity from humble origins.Traffic (Copenhagen, Denmark) · 2014Review
- Chloroplast envelope protein targeting fidelity is independent of cytosolic components in dual organelle assays.Frontiers in plant science · 2012Article
- Study of receptor-chaperone interactions using the optical technique of spectroscopic ellipsometry.Biophysical journal · 2011Article
- Tail-anchored membrane proteins: exploring the complex diversity of tail-anchored-protein targeting in plant cells.Plant cell reports · 2011Review
- Nucleocytoplasmic distribution is required for activation of resistance by the potato NB-LRR receptor Rx1 and is balanced by its functional domains.The Plant cell · 2010Article
- Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis.The Plant cell · 2009Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Arabidopsis (Arabidopsis thaliana) tryptophan-proline-proline (WPP)-domain proteins, WPP1 and WPP2, are plant-unique, nuclear envelope-associated proteins of unknown function. They have sequence similarity to the nuclear envelope-targeting domain of plant RanGAP1, the GTPase activating protein of the small GTPase Ran. WPP domain-interacting tail-anchored protein 1 (WIT1) and WIT2 are two Arabidopsis proteins containing a coiled-coil domain and a C-terminal predicted transmembrane domain. They are required for RanGAP1 association with the nuclear envelope in root tips. Here, we show that WIT1 also binds WPP1 and WPP2 in planta, we identify the chaperone heat shock cognate protein 70-1 (HSC70-1) as in vivo interaction partner of WPP1 and WPP2, and we show that HSC70-1 interacts in planta with WIT1. WIT1 and green fluorescent protein (GFP)-WIT1 are targeted to the nuclear envelope in Arabidopsis. In contrast, GFP-WIT1 forms large cytoplasmic aggregates when overexpressed transiently in Nicotiana benthamiana leaf epidermis cells. Coexpression of HSC70-1 significantly reduces GFP-WIT1 aggregation and permits association of most GFP-WIT1 with the nuclear envelope. Significantly, WPP1 and WPP2 show the same activity. A WPP1 mutant with reduced affinity for GFP-WIT1 fails to decrease its aggregation. While the WPP-domain proteins act on a region of WIT1 containing the coiled-coil domain, HSC70-1 additionally acts on the C-terminal transmembrane domain. Taken together, our data suggest that both HSC70-1 and the WPP-domain proteins play a role in facilitating WIT1 nuclear envelope targeting, which is, to our knowledge, the first described in planta activity for the WPP-domain proteins.
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