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First published online May 20, 2008

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IFT proteins: not created equal

Vertebrate photoreceptor cells possess a modified cilium called the outer segment, which contains light-absorbing opsin proteins. Proteins are transported to the outer segment by intraflagellar transport (IFT) particles, which are complexes of IFT proteins that are translocated by axoneme-bound kinesin II. Mutations in IFT proteins perturb ciliogenesis; however, in many cases the roles of the individual IFT proteins in photoreceptor function are unknown. On page 1907, Bryan Krock and Brian Perkins compare the phenotypes of a zebrafish IFT57 loss-of-function mutant and a previously characterised IFT88 mutant. The authors demonstrate that IFT occurs inefficiently in photoreceptors of IFT57 mutant fish; consequently, the cells have short outer segments that contain reduced amounts of opsin. By contrast, outer segments are not visible in the photoreceptors of IFT88 mutants. Kinesin II co-immunoprecipitates with the IFT particle even in the absence of IFT57, but IFT20 (another IFT-particle component) does not. Notably, the ATP-dependent dissociation of kinesin II from the IFT particle is inhibited in the IFT57 mutant. These data indicate that individual IFT proteins have distinct roles in photoreceptor function.

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Related articles in JCS:

The intraflagellar transport protein IFT57 is required for cilia maintenance and regulates IFT-particle–kinesin-II dissociation in vertebrate photoreceptors

Bryan L. Krock and Brian D. Perkins
JCS 2008 121: 1907-1915. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?