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Digitale Medien

Microsphere attachment induces glycoprotein redistribution and transmembrane signaling in theChlamydomonas flagellum (1998)

Bloodgood, Robert A. ; Salomonsky, Nancy L.

Springer

Protoplasma 202 (1998), S. 76-83

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ISSN: 1615-6102

Schlagwort(e): Flagella ; Microspheres ; Gliding motility ; Protein dephosphorylation ; Chlamydomonas ; Plasma membrane ; Membrane protein dynamics

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie

Notizen: 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.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01280876

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Digitale Medien

A flagellar surface glycoprotein mediating cell-substrate interaction in Chlamydomonas (1984)

Bloodgood, Robert A. ; Workman, Lisa J.

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 4 (1984), S. 77-87

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Details

ISSN: 0886-1544

Schlagwort(e): Chlamydomonas ; flagella ; cell surface ; adhesion ; glycoproteins ; iodination ; lactoperoxidase ; Iodogen ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie , Medizin

Notizen: The Chlamydomonas flagellar surface exhibits interesting adhesive properties that are associated with flagellar surface motility. This dynamic surface property can be exhibited as the binding and movement of small polystyrene microspheres or as the interaction of the flagellar surface with a solid substrate followed by whole cell locomotion, termed “gliding.” In order to identify flagellar surface proteins that mediate substrate interaction during flagellar surface motility, two immobilized iodination systems were employed that mimic the conditions for flagellar surface motility: small polystyrene microspheres derivatized with lactoperoxidase, and large glass beads derivatized with Iodogen. Use of these iodination conditions resulted in preferential iodination of a high-molecular-weight glycoprotein with apparent molecular weight of 300,000-350,000. These results suggest this glycoprotein as a major candidate for the surface-exposed adhesive component that directly interacts with the substrate and couples the substrate to a system of force transduction presumed to be located within the flagellum.

Zusätzliches Material: 4 Ill.