title: The cilium secretes bioactive ectosomes.
abstract: The release of membrane vesicles from the surface of cells into their surrounding environment is now recognized as an important pathway for the delivery of proteins to extracellular sites of biological function. Membrane vesicles of this kind, termed exosomes and ectosomes, are the result of active processes and have been shown to carry a wide array of biological effector molecules that can play roles in cell-to-cell communication and remodeling of the extracellular space. Degradation of the extracellular matrix (ECM) through the regulated release of proteolytic enzymes is a key process for development, morphogenesis, and cell migration in animal and plant cells. Here we show that the unicellular alga Chlamydomonas achieves the timely degradation of its mother cell wall, a type of ECM, through the budding of ectosomes directly from the membranes of its flagella. Using a combination of immunoelectron microscopy, immunofluorescence microscopy, and functional analysis, we demonstrate that these vesicles, which we term ciliary ectosomes, act as carriers of the proteolytic enzyme necessary for the liberation of daughter cells following mitosis. Chlamydomonas has proven to be the key unicellular model for the highly conserved mechanisms of mammalian cilia, and our results suggest that cilia may be an underappreciated source of bioactive, extracellular membrane vesicles.
authors.affiliation: Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
authors.forename: Christopher R
authors.initials: CR
authors.lastname: Wood
authors.forename: Kaiyao
authors.initials: K
authors.lastname: Huang
authors.forename: Dennis R
authors.initials: DR
authors.lastname: Diener
authors.forename: Joel L
authors.initials: JL
authors.lastname: Rosenbaum
mesh_terms: D055252:Cell-Derived Microparticles; D002696:Chlamydomonas / Q000201:enzymology / Q000378:metabolism*; D002923:Cilia / Q000378:metabolism*; D005109:Extracellular Matrix / Q000201:enzymology / Q000378:metabolism; D008856:Microscopy, Fluorescence; D016253:Microscopy, Immunoelectron; D010447:Peptide Hydrolases / Q000378:metabolism; D059748:Proteolysis
chemical_list: D010447:Peptide Hydrolases