Hydin seek: finding a function in ciliary motility.
One of the most surprising discoveries in cell biology in the past 5-10 years is the number of diverse human diseases that result from defects in ciliary assembly and/or motility, so-called ciliopathies (Badano, J.L., N. Mitsuma, P.L. Beales, and N. Katsanis. 2006. Annu. Rev. Genomics Hum. Genet. 7:125-148). The results presented by Lechtreck and Witman (see p. 473 of this issue) provide yet another example of how work in the model organism Chlamydomonas reinhardtii can reveal important insights into the underlying mechanisms of ciliary assembly/function and the diseases associated with defects in these organelles. By taking advantage of the wide array of experimental approaches C. reinhardtii offers, Lechtreck and Witman determined the precise axonemal location of hydin, a protein that, when mutated, causes hydrocephalus, and defined a unique role for hydin in ciliary motility.
Smith
Elizabeth F
EF
Department of Biological Sciences, Dartmouth College, Hanover, NH 03755, USA. elizabeth.f.smith@dartmouth.edu
D000818:Animals; D016825:Chlamydomonas reinhardtii / Q000378:metabolism* / Q000648:ultrastructure; D002923:Cilia / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D006849:Hydrocephalus / Q000235:genetics / Q000378:metabolism / Q000503:physiopathology; D008124:Locomotion / Q000502:physiology*; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D020409:Molecular Motor Proteins / Q000378:metabolism; D009154:Mutation / Q000235:genetics
C481382:Hydin protein, mouse; D008840:Microfilament Proteins; D020409:Molecular Motor Proteins