title: The FEI2-SOS5 pathway and CELLULOSE SYNTHASE 5 are required for cellulose biosynthesis in the Arabidopsis seed coat and affect pectin mucilage structure.
abstract: A common adaptation in angiosperms is the deposition of hydrophilic mucilage into the apoplast of seed coat epidermal cells during the course of their differentiation. Upon imbibition, seed mucilage, composed mainly of carbohydrates (i.e. pectins, hemicelluloses and glycans) expands rapidly, encapsulating the seed and aiding in seed dispersal and germination. The FEI1/FEI2 receptor-like kinases and the SOS5 extracellular GPI-anchored protein were previously shown to act on a pathway regulating cellulose biosynthesis during Arabidopsis root elongation. In the highlighted study, we demonstrated that FEI2 and SOS5 regulate the production of the cellulosic rays deposited across the inner adherent-layer of seed mucilage. Mutations in either fei2 or sos5 disrupted the formation of rays, which was associated with an increase in the soluble, outer layer of pectin mucilage and accompanied by a reduction in the inner adherent-layer. Mutations in CELLULOSE SYNTHASE 5 also led to reduced rays and mal-partitioning of the pectic component of seed mucilage, further establishing a structural role for cellulose in seed mucilage. Here, we show that FEI2 expressed from a CaMV 35S promoter complemented both root and seed mucilage defects of the fei1 fei2 double mutant. In contrast, expression of FEI1 from a 35S promoter complemented the root, but not the seed phenotype of the fei1 fei2 double mutant, suggesting that unlike in the root, FEI2 plays a unique and non-redundant role in the regulation of cellulose synthesis in seed mucilage. Altogether, these data suggest a novel role for cellulose in anchoring the pectic component of seed mucilage to the seed surface and indicate that the FEI2 protein has a function distinct from that of FEI1, despite the high sequence similarity of these RLKs.
authors.affiliation: Biology Department, University of North Carolina, Chapel Hill, NC, USA.
authors.forename: Smadar
authors.initials: S
authors.lastname: Harpaz-Saad
authors.forename: Tamara L
authors.initials: TL
authors.lastname: Western
authors.forename: Joseph J
authors.initials: JJ
authors.lastname: Kieber
mesh_terms: D000269:Adhesives / Q000737:chemistry; D017360:Arabidopsis / Q000033:anatomy & histology / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism*; D002482:Cellulose / Q000096:biosynthesis* / Q000235:genetics; D017343:Genes, Plant; D005964:Glucosyltransferases / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D010368:Pectins / Q000737:chemistry; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D012639:Seeds / Q000378:metabolism*
chemical_list: D000269:Adhesives; D029681:Arabidopsis Proteins; D015815:Cell Adhesion Molecules; C473610:SOS5 protein, Arabidopsis; D010368:Pectins; D002482:Cellulose; D005964:Glucosyltransferases; C478648:cellulose synthase; D011494:Protein Kinases