Functional diversity of the plant glycine-rich proteins superfamily.
The first plant glycine-rich proteins (GRPs) have been isolated more than 20 years ago based on their specific expression pattern and/or modulation by several biotic and abiotic factors. This superfamily is characterized by the presence of a glycine-rich domain arranged in (Gly)(n)-X repeats. The presence of additional motifs, as well as the nature of the glycine repeats, groups them in different classes. The diversity in structure as well as in expression pattern, modulation and sub-cellular localization have always indicated that these proteins, although classified as members of the same superfamily, would perform different functions in planta. Only now, two decades later, with the first functional characterizations of plant GRPs their involvement in diverse biological and biochemical processes are being uncovered. Here, we review the so far ascribed functions of plant GRPs.
Mangeon
Amanda
A
Laboratório de Genômica Funcional e Transdução de Sinal, Departamento de Genética, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
Junqueira
Ricardo Magrani
RM
Sachetto-Martins
Gilberto
G
D020816:Amino Acid Motifs; D002473:Cell Wall / Q000502:physiology; D003080:Cold Temperature; D035264:Flowers / Q000502:physiology; D017343:Genes, Plant; D005998:Glycine / Q000378:metabolism*; D008024:Ligands; D050356:Lipid Metabolism; D005810:Multigene Family; D009997:Osmotic Pressure; D010940:Plant Proteins / Q000378:metabolism*; D011058:Pollen / Q000502:physiology; D011494:Protein Kinases / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000378:metabolism; D013312:Stress, Physiological
D008024:Ligands; D010940:Plant Proteins; D016601:RNA-Binding Proteins; D011494:Protein Kinases; D005998:Glycine