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Cell adhesion in plants is mediated predominantly by pectins, a group of complex cell wall associated polysaccharides. An  Arabidopsis  mutant,  friable1  ( frb1 ), was identified through a screen of T-DNA insertion lines that exhibited defective cell adhesion. Interestingly, the  frb1  plants displayed both cell and organ dissociations and also ectopic defects in organ separation. The  FRB1  gene encodes a Golgi-localized, plant specific protein with only weak sequence similarities to known proteins (DUF246). Unlike other cell adhesion deficient mutants,  frb1  mutants do not have reduced levels of adhesion related cell wall polymers, such as pectins. Instead, FRB1 affects the abundance of galactose- and arabinose-containing oligosaccharides in the Golgi. Furthermore,  frb1  mutants displayed alteration in pectin methylesterification, cell wall associated extensins and xyloglucan microstructure. We propose that abnormal FRB1 action has pleiotropic consequences on wall architecture, affecting both the extensin and pectin matrices, with consequent changes to the biomechanical properties of the wall and middle lamella, thereby influencing cell-cell adhesion.

The FRIABLE1 Gene Product Affects Cell Adhesion in Arabidopsis