The Cilium Secretes Bioactive Ectosomes
Open accessAbstract
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.
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Ciliary membrane content can be modulated by ectocytosis of vesicles at the ciliary tip.
“Moreover, ciliary membrane content can be modulated by the ectocytosis of vesicles at the ciliary tip 26–28 (Figure 1).”
From Cellular signalling by primary cilia in development, organ function and disease (2019) · cites this paper as [26]
The Results section on ciliary ectosomes reports vesicles budding from Chlamydomonas flagellar membranes, and the Discussion identifies flagellar membrane proteins in the released vesicles. This supports ectocytosis as a way to remove ciliary membrane content, but the copy does not establish that the vesicles bud specifically at the ciliary tip; the immunofluorescence Results report only that the cargo protein often clusters toward the distal end. Page numbers were not provided. (LLM, conf=0.85)
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- Authors
- Wood, C. R., Huang, K., Diener, D. R., & Rosenbaum, J. L.
- Affiliations
- Yale University (US)
- Corresponding author
- Rosenbaum, Joel L.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 23
- Issue
- 10
- Pages
- 906-911
- ISSN
- 0960-9822 (ISSN-L)
- PMC
- PMC3850760
- OpenAlex
- W2035252153
- Cited by
- 233
- References
- 32
- Citations by year
- 2026: 8 · 2025: 16 · 2024: 12 · 2023: 18 · 2022: 23 · 2021: 19 · 2020: 21 · 2019: 15 · 2018: 21 · 2017: 23 · 2016: 17 · 2015: 17 · 2014: 15 · 2013: 8
- FWCI
- 8.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM014642, GM014642)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- cilia, membrane vesicles, exosomes, Chlamydomonas, cell wall degradation, extracellular matrix degradation, proteolytic enzymes, flagella, mitosis, cell division, vesicle budding, cell-to-cell communication
- MeSH terms
- Chlamydomonas, Cilia, Extracellular Matrix, Microscopy, Fluorescence, Peptide Hydrolases, Microscopy, Immunoelectron, Cell-Derived Microparticles, Proteolysis
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