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Molecular and Structural Studies on Dynein Associated Mutations in Chlamydomonas Flagella.

Published online by Cambridge University Press:  02 July 2020

M.E. Porter
Affiliation:
Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis, MN55455
S. Myster
Affiliation:
Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis, MN55455
C. Perrone
Affiliation:
Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis, MN55455
E. O'Toole
Affiliation:
Laboratory for 3-Dimensional Fine Structure, Department of Molecular and Developmental Biology Cellular, University of Colorado, Boulder, CO, 80309.
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Extract

The dynein ATPases are a large family of motor enzymes that provide the driving force for flagellar motility and contribute to microtubule-based transport inside cells. The challenge for the field is to appreciate the functional significance of the multiple dynein motors, to determine how the cell assembles a motor complex and targets each motor to its appropriate location, and to understand how a cell regulates the activity of each motor to accomplish its specific task(s). In our laboratory, we have capitalized on the highly ordered structural organization of the flagellar axoneme and on the ease of genetic analysis in Chlamydomonas to ask how a single cell controls the assembly and activity of its multiple flagellar dyneins. In particular, we have focused our efforts on the inner dynein arms, which are both necessary and sufficient for normal flagellar motility. The significance of this work derives from the conservation of axoneme structure across species, as well as the numerous functional homologies between the flagellar and cytoplasmic dyneins.

Type
Innovative Approaches to 3-D Structure/Function Determination for Cells and Organelles
Copyright
Copyright © Microscopy Society of America 1997

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