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dc.contributor.authorBloodgood, Robert A.  Concept link
dc.contributor.authorTetreault, Joseph  Concept link
dc.contributor.authorSloboda, Roger D.  Concept link
dc.date.accessioned2019-09-10T13:01:02Z
dc.date.issued2019-08-19
dc.identifier.citationBloodgood, R. A., Tetreault, J., & Sloboda, R. D. (2019). The Chlamydomonas flagellar membrane glycoprotein FMG-1B is necessary for expression of force at the flagellar surface. Journal of Cell Science, 132, jcs.233429.en_US
dc.identifier.urihttps://hdl.handle.net/1912/24526
dc.descriptionAuthor 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.en_US
dc.description.abstractIn 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.en_US
dc.description.sponsorshipThis 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.en_US
dc.publisherCompany of Biologistsen_US
dc.relation.urihttps://doi.org/10.1242/jcs.233429
dc.subjectChlamydomonasen_US
dc.subjectFMG-1Ben_US
dc.subjectFlagellaen_US
dc.subjectCiliaen_US
dc.subjectFlagellar membraneen_US
dc.subjectGliding motilityen_US
dc.subjectSurface motilityen_US
dc.titleThe Chlamydomonas flagellar membrane glycoprotein FMG-1B is necessary for expression of force at the flagellar surfaceen_US
dc.typeArticleen_US
dc.description.embargo2020-08-01en_US
dc.identifier.doi10.1242/jcs.233429
dc.embargo.liftdate2020-08-01


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