ArticleJournal of virology2006
A PERK-like receptor kinase interacts with the geminivirus nuclear shuttle protein and potentiates viral infection.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 91 citations in OpenAlex.
- Whitefly transmitted begomovirus infection in plant and host response: a review.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Review
- Genome-wide identification and expression analysis of PERK genes in peanut and revelation of bidirectional immune regulatory function.Frontiers in plant science · 2025Article
- Review
- Genome-Wide Analysis and Characterization of the Proline-Rich Extensin-like Receptor Kinases (PERKs) Gene Family Reveals Their Role in Different Developmental Stages and Stress Conditions in Wheat (Plants (Basel, Switzerland) · 2022Article
- Insights into the multifunctional roles of geminivirus-encoded proteins in pathogenesis.Archives of virology · 2022Review
- A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for the begomovirus CabLCV.Plant physiology · 2021Article
- Plant responses to geminivirus infection: guardians of the plant immunity.Virology journal · 2021Review
- Article
- Stability of Begomoviral pathogenicity determinant βC1 is modulated by mutually antagonistic SUMOylation and SIM interactions.BMC biology · 2020Article
- Genome-wide analysis of proline-rich extension-like receptor protein kinase (PERK) in Brassica rapa and its association with the pollen development.BMC genomics · 2020Article
- Molecular insight into cotton leaf curl geminivirus disease resistance in cultivated cotton (Gossypium hirsutum).Plant biotechnology journal · 2020Article
- Phosphorylations of the Abutilon Mosaic Virus Movement Protein Affect Its Self-Interaction, Symptom Development, Viral DNA Accumulation, and Host Range.Frontiers in plant science · 2020Article
- A Begomovirus Nuclear Shuttle Protein-Interacting Immune Hub: Hijacking Host Transport Activities and Suppressing Incompatible Functions.Frontiers in plant science · 2020Review
- Nicotiana benthamiana phosphatidylinositol 4-kinase type II regulates chilli leaf curl virus pathogenesis.Molecular plant pathology · 2019Article
- Virus perception at the cell surface: revisiting the roles of receptor-like kinases as viral pattern recognition receptors.Molecular plant pathology · 2019Review
- Plant Antiviral Immunity Against Geminiviruses and Viral Counter-Defense for Survival.Frontiers in microbiology · 2019Review
- Review
- Mimic Phosphorylation of a βC1 Protein Encoded by TYLCCNB Impairs Its Functions as a Viral Suppressor of RNA Silencing and a Symptom Determinant.Journal of virology · 2017Article
- Sustained NIK-mediated antiviral signalling confers broad-spectrum tolerance to begomoviruses in cultivated plants.Plant biotechnology journal · 2015Article
- NIK1-mediated translation suppression functions as a plant antiviral immunity mechanism.Nature · 2015Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear shuttle protein (NSP) from bipartite geminiviruses facilitates the intracellular transport of viral DNA from the nucleus to the cytoplasm and acts in concert with the movement protein (MP) to promote the cell-to-cell spread of the viral DNA. A proline-rich extensin-like receptor protein kinase (PERK) was found to interact specifically with NSP of Cabbage leaf curl virus (CaLCuV) and of tomato-infecting geminiviruses through a yeast two-hybrid screening. The PERK-like protein, which we designated NsAK (for NSP-associated kinase), is structurally organized into a proline-rich N-terminal domain, followed by a transmembrane segment and a C-terminal serine/threonine kinase domain. The viral protein interacted stably with defective versions of the NsAK kinase domain, but not with the potentially active enzyme, in an in vitro binding assay. In vitro-translated NsAK enhanced the phosphorylation level of NSP, indicating that NSP functions as a substrate for NsAK. These results demonstrate that NsAK is an authentic serine/threonine kinase and suggest a functional link for NSP-NsAK complex formation. This interpretation was corroborated by in vivo infectivity assays showing that loss of NsAK function reduces the efficiency of CaLCuV infection and attenuates symptom development. Our data implicate NsAK as a positive contributor to geminivirus infection and suggest it may regulate NSP function.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.