Journal
EXPERIMENTAL EYE RESEARCH
Volume 88, Issue 1, Pages 55-60Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.exer.2008.09.022
Keywords
ankyrin-B; beta-2-spectrin; rod photoreceptors; Na/K-ATPase; Na/Ca exchanger; cell polarity; inner segment
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Funding
- VA, Foundation Fighting Blindness [R24EY15638]
- NATIONAL EYE INSTITUTE [R24EY015638] Funding Source: NIH RePORTER
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Rod photoreceptors are highly polarized cells whose exquisite sensitivity to light depends on precise compartmentalization of ion channels/transporters within specialized membrane domains. Here, we report evidence for an ankyrin-B based mechanism for coordinated expression of the beta-2-spectrin-based membrane skeleton, and the Na/K-ATPase and Na/Ca exchanger in the inner segment of rod photoreceptors. We first discovered that ankyrin-B localizes to the inner segments but not outer segments of rod photoreceptors in vertebrates including humans, mice, and frogs. We found that haploinsufficiency of ankyrin-B in mice is accompanied by 50% reduction in inner segments of membrane proteins, including the Na/K-ATPase and the Na/Ca exchanger, as well as beta-2-spectrin, which is a component of the spectrin-actin membrane skeleton. These results are consistent with a mechanism where ankyrin-B is required to restrict the Na/K-ATPase and Na/Ca exchanger to the inner segment of rod photoreceptors by tethering these membrane proteins to beta-2-spectrin. (C) 2008 Elsevier Ltd. All rights reserved.
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