Publications (3)4.66 Total impact
Article: The Diverse Roles of Extracellular Leucine-rich Repeat-containing Receptor-like Proteins in Plants[show abstract] [hide abstract]
ABSTRACT: Plant cells use various types of cell surface receptor molecules to sense extracellular signals and modulate cell-to-cell communication in many biological processes. Extracellular leucine-rich repeat (eLRR) receptor-like proteins (RLPs) represent an important class of such cell surface receptors. RLPs differ from receptor-like kinases (RLKs), which compose the largest class of cell surface receptors in many plant species, because they lack a cytoplasmic kinase domain. RLPs play roles in both developmental processes and disease resistance. A total of 57 RLP encoding genes has been identified in Arabidopsis. Two of them, CLAVATA2 (CLV2) and Too Many Mouths (TMM) have a function in meristem maintenance and stomatal distribution, respectively, whereas few others act in basal defense against pathogens. Although the function of most RLPs in Arabidopsis remains unclear, considerable progress has been made in understanding RLP functioning and signaling over the years. This review focuses on the function of RLPs in plants. Furthermore, the function of distinct RLP domains and the role of conserved residues important for perception and ligand specificity are discussed. The role of RLP proteins in multimeric complexes to sense biotic and abiotic extracellular signals is also addressed.Critical Reviews in Plant Sciences 01/2010; 29(5):285-299. · 4.66 Impact Factor
Article: Genome-wide functional analysis of Arabidopsis receptor-like protein genes for roles in plant development and pathogen defense
Article: Functional Analyses of the CLAVATA2-Like Proteins and Their Domains That Contribute to CLAVATA2 Specificity[show abstract] [hide abstract]
ABSTRACT: The Arabidopsis (Arabidopsis thaliana) CLAVATA2 (CLV2) gene encodes a leucine-rich repeat receptor-like protein (RLP) that is involved in controlling the stem cell population size in the shoot apical meristem. Our previous genome-wide functional analysis of 57 AtRLP genes revealed only a few phenotypes for mutant alleles, despite screening a wide range of growth and developmental stages and assaying sensitivity to various stress responses, including susceptibility toward pathogens. To gain further insight into the biological role of AtRLPs, in particular CLV2-related AtRLP genes, we tested their ability to complement the clv2 mutant phenotype. We found that out of four close CLV2 homologs tested, AtRLP2 and AtRLP12 could functionally complement the clv2 mutant when expressed under the control of the CLV2 promoter. This indicates that the functional specificity of these three genes is determined at the level of their transcriptional regulation. Single and double mutant combinations with impaired AtRLP2 and/or AtRLP12 did not show an aberrant phenotype, suggesting that other genes are redundant with these CLV2-like genes. To understand which protein domains are essential for CLV2 function and which parts are interchangeable between related CLV2-like proteins, we performed domain-deletion and domain-swap experiments. These experiments revealed that CLV2 remains functional without the island domain, whereas the C1 and C3 regions of the leucine-rich repeat domain are essential for functionality. Analysis of domain-swap constructs showed that the C3-G region of CLV2 can be replaced by that of AtRLP38, although it could not complement the clv2 mutant under control of the CLV2 promoter. This suggests that the C3-G region is conserved among related AtRLP members, whereas the C1 domain may determine the functional specificity of CLV2Plant Physiology 152 (2010).