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  • 1
    ISSN: 1615-6102
    Keywords: Flagella ; Microspheres ; Gliding motility ; Protein dephosphorylation ; Chlamydomonas ; Plasma membrane ; Membrane protein dynamics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The biflagellate green algaChlamydomonas can exhibit substrate-associated gliding motility in addition to its ability to swim through a liquid medium. The flagella are the organelles responsible for both forms of whole-cell locomotion although the mechanism in each case is very different. In this study, we demonstrate that the binding of polystyrene microspheres to the flagellar surface ofChlamydomonas initiates clustering of the major flagellar-membrane glycoprotein, which is known to be involved in motility-associated substrate adhesion. In addition, we demonstrate that microsphere binding to the flagellar surface initiates the same transmembrane signaling pathway that is initiated by antibody- or lectin-induced crosslinking of the major flagellar-membrane glycoprotein. In each case, the signaling pathway involves the activation of a calciumdependent protein phosphatase that dephosphorylates a flagellar phosphoprotein known to be associated with the major flagellar-membrane glycoprotein. Bound microspheres are translocated along the flagellar surface at approximately the same velocity as whole-cell gliding motility. Previous observations suggest that microsphere binding and translocation along the flagellar surface may be a reflection of the same force-transducing system responsible for whole-cell gliding motility. In which case, these observations suggest that the transmembrane signaling pathway initiated by crosslinking the major flagellar-membrane glycoprotein is the same one that is activated when the cell contacts a physiological substrate by its flagellar surface.
    Type of Medium: Electronic Resource
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  • 2
    Publication Date: 2022-05-26
    Description: Author Posting. © Company of Biologists, 2019. This article is posted here by permission of Company of Biologists for personal use, not for redistribution. The definitive version was published in Journal of Cell Science 132 (2019): jcs.233429, doi:10.1242/jcs.233429.
    Description: In addition to bend propagation for swimming, Chlamydomonas cells use their flagella to glide along a surface. When polystyrene microspheres are added to cells, they attach to and move along the flagellar surface, thus serving as a proxy for gliding that can be used to assay for the flagellar components required for gliding motility. Gliding and microsphere movement are dependent on intraflagellar transport (IFT). Circumstantial evidence suggests that mechanical coupling of the IFT force-transducing machinery to a substrate is mediated by the flagellar transmembrane glycoprotein FMG-1B. Here, we show that cells carrying an insertion in the 5′-UTR of the FMG-1B gene lack FMG-1B protein, yet assemble normal-length flagella despite the loss of the major protein component of the flagellar membrane. Transmission electron microscopy shows a complete loss of the glycocalyx normally observed on the flagellar surface, suggesting it is composed of the ectodomains of FMG-1B molecules. Microsphere movements and gliding motility are also greatly reduced in the 5′-UTR mutant. Together, these data provide the first rigorous demonstration that FMG-1B is necessary for the normal expression of force at the flagellar surface in Chlamydomonas. This article has an associated First Person interview with authors from the paper.
    Description: This work was made possible by a Dartmouth FRPDF (faculty research and professional development fund) generously provided by the Dean of the Faculty and by the Ira Allen Eastman (Class of 1829) Professorship, which was established in 1910 by a gift to the College from his widow, Jane Eastman.
    Description: 2020-08-01
    Keywords: Chlamydomonas ; FMG-1B ; Flagella ; Cilia ; Flagellar membrane ; Gliding motility ; Surface motility
    Repository Name: Woods Hole Open Access Server
    Type: Article
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