ArticlePlant physiology2001
Isolation and characterization of kinase interacting protein 1, a pollen protein that interacts with the kinase domain of PRK1, a receptor-like kinase of petunia.
Article in Plant physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
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- Genomic Regions Associated with Fusarium Wilt Resistance in Flax.International journal of molecular sciences · 2021Article
- Labelling Selective Sweeps Used in Durum Wheat Breeding from a Diverse and Structured Panel of Landraces and Cultivars.Biology · 2021Article
- Tomato SD1, encoding a kinase-interacting protein, is a major locus controlling stem development.Journal of experimental botany · 2020Article
- The Rice DNA-Binding Protein ZBED Controls Stress Regulators and Maintains Disease Resistance After a Mild Drought.Frontiers in plant science · 2020Article
- ZmSTK1 and ZmSTK2, encoding receptor-like cytoplasmic kinase, are involved in maize pollen development with additive effect.Plant biotechnology journal · 2018Article
- Arabidopsis kinetochore null2 is an upstream component for centromeric histone H3 variant cenH3 deposition at centromeres.The Plant cell · 2013Article
- PiSCP1 and PiCDPK2 Localize to Peroxisomes and Are Involved in Pollen Tube Growth in Petunia Inflata.Plants (Basel, Switzerland) · 2013Article
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- The amino terminal F-box domain of Petunia inflata S-locus F-box protein is involved in the S-RNase-based self-incompatibility mechanism.AoB PLANTS · 2011Article
- Functional characterization of two chimeric proteins between a Petunia inflata S-locus F-box protein, PiSLF2, and a PiSLF-like protein, PiSLFLb-S2.Plant molecular biology · 2010Article
- Isolation and characterization of NgRLK1, a receptor-like kinase of Nicotiana glutinosa that interacts with the elicitin of Phytophthora capsici.Molecular biology reports · 2010Article
- Ectopic expression of S-RNase of Petunia inflata in pollen results in its sequestration and non-cytotoxic function.Sexual plant reproduction · 2009Article
- Comparison of Petunia inflata S-Locus F-box protein (Pi SLF) with Pi SLF like proteins reveals its unique function in S-RNase based self-incompatibility.The Plant cell · 2007Article
- Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in S-RNase-based self-incompatibility.The Plant cell · 2006Article
- Identification and characterization of PiORP1, a Petunia oxysterol-binding-protein related protein involved in receptor-kinase mediated signaling in pollen, and analysis of the ORP gene family in Arabidopsis.Plant molecular biology · 2006Article
- Petunia phospholipase c1 is involved in pollen tube growth.The Plant cell · 2006Article
- Coiled-coil protein composition of 22 proteomes--differences and common themes in subcellular infrastructure and traffic control.BMC evolutionary biology · 2005Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many receptor-like kinases have been identified in plants and have been shown by genetic or transgenic knockouts to play diverse physiological roles; however, to date, the cytosolic interacting proteins of relatively few of these kinases have been identified. We have previously identified a predominantly pollen-expressed receptor-like kinase of petunia (Petunia inflata), named PRK1, and we have shown by the antisense RNA approach that it is required for microspores to progress from the unicellular to bicellular stage. To investigate the PRK1-mediated signal transduction pathway, PRK1-K cDNA, encoding most of the cytoplasmic domain of PRK1, was used as bait in yeast (Saccharomyces cerevisiae) two-hybrid screens of pollen/pollen tube cDNA libraries of petunia. A protein named kinase interacting protein 1 (KIP1) was found to interact very strongly with PRK1-K. This interaction was greatly reduced when lysine-462 of PRK1-K, believed to be essential for kinase activity, was replaced with arginine (the resulting protein is named PRK1-K462R). The amino acid sequence of KIP1 deduced from full-length cDNA contains an EF-hand Ca(2+)-binding motif and nine predicted coiled-coil regions. The yeast two-hybrid assay and affinity chromatography showed that KIP1 interacts with itself to form a dimer or higher multimer. KIP1 is present in a single copy in the genome, and is expressed predominantly in pollen with a similar temporal pattern to PRK1. In situ hybridization showed that PRK1 and KIP1 transcripts were localized in the cytoplasm of pollen. PRK1-K phosphorylated KIP1-NT (amino acids 1--716), whereas PRK1-K462R only weakly phosphorylated KIP1-NT in vitro.
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