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The dynein class of molecular motors are essential for many eukaryotic cellular processes. These multimeric complexes-composed of as many as 15 subunits
are responsible for vesicle trafficking toward the center of the cell, chromosomal segregation, and most pertinently: dyneins facilitate microtubule sliding in cilia
and flagella. Based in part on studies in the model genetic system Chlamydomonas, defects in assembly, targeting, and regulation of ciliary/flagellar dyneins
have been associated with a number of disease states not limited to: hydrocephaly, male and female infertility, and Primary Ciliary Dyskinesia. The subunits of
the dynein complex are translated within the cytoplasm however, little is known about the mechanisms of assembly, transport, and targeting of dyneins to the
cilium/flagellum. Here we address the assembly state of the ciliary dyneins using the isoform “I1” as a model for dynein taking advantage of the genetic system
Chlamydomonas. Using dynein mutants we have tested the hypothesis that I1 is fully assembled in the cytoplasm prior to transport and incorporation into the
ciliary axoneme (Fig. 1). We approach the question using biochemical fractionation of cytoplasmic components in wild type and dynein mutants.
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