Distinct functions for IFT140 and IFT20 in opsin transport. Issue 5 (25th March 2014)

• Record Type: Journal Article
• Authors: Crouse, Jacquelin A.; Lopes, Vanda S.; SanAgustin, Jovenal T.; Keady, Brian T.; Williams, David S.; Pazour, Gregory J.
• Is Part Of: Cytoskeleton. Volume 71:Issue 5(2014:May)
• Page Start: 302
• Page End: 310
• Publication Date: 2014-03-25
• Subjects: Cytoskeleton -- Periodicals; 571.65405
• DOI: 10.1002/cm.21173
• Languages: English
• ISSNs: 1949-3584

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>In the vertebrate retina, light is detected by the outer segments of photoreceptor rods and cones, which are highly modified cilia. Like other cilia, outer segments have no protein synthetic capacity and depend on proteins made in the cell body for their formation and maintenance. The mechanism of transport into the outer segment is not fully understood but intraflagellar transport (IFT) is thought to be a major mechanism for moving protein from the cell body into the cilium. In the case of photoreceptor cells, the high density of receptors and the disk turnover that occurs daily necessitates much higher rates of transport than would be required in other cilia. In this work, we show that the IFT complex A protein IFT140 is required for development and maintenance of outer segments. In earlier work we found that acute deletion of <italic>Ift20</italic> caused opsin to accumulate at the Golgi complex. In this work, we find that acute deletion of <italic>Ift140</italic> does not cause opsin to accumulate at the Golgi complex but rather it accumulates in the plasma membrane of the inner segments. This work is a strong support of a model of opsin transport where IFT20 is involved in the movement from the Golgi complex to the base of the cilium. Then, once at the base, the opsin is carried through the connecting cilium by an IFT complex that includes IFT140. © 2014 Wiley Periodicals, Inc.</p> </abstract>