title: Controlling the Connections of Cells to the Biofilm Matrix.
abstract: The importance of cyclic di-GMP (c-di-GMP) and its control of biofilm matrix assembly and production has been a focal point of researchers in recent history. In this issue, Cooley et al. (Cooley RB, Smith TJ, Leung W, Tierney V, Borlee BR, O'Toole GA, Sondermann H, J Bacteriol 198:66-77, http://dx.doi.org/10.1128/JB.00369-15) demonstrate that two c-di-GMP controlled features of Pseudomonas aeruginosa, the periplasmic protease LapG and the surface adhesin CdrA, are linked. CdrA is shown to be a substrate of LapG, with LapG activity controlled by intracellular c-di-GMP levels. This commentary discusses the significance of this finding.
authors.affiliation: Department of Microbiology, University of Washington, Seattle, Washington, USA parsem@uw.edu.
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Parsek
mesh_terms: D001419:Bacteria / Q000378:metabolism*; D001422:Bacterial Adhesion / Q000502:physiology*; D018407:Bacterial Physiological Phenomena; D018441:Biofilms / Q000254:growth & development*; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000235:genetics / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000502:physiology*
chemical_list: C062025:bis(3',5')-cyclic diguanylic acid; D006152:Cyclic GMP