Prohibitin as the Molecular Binding Switch in the Retinal Pigment Epithelium
Document Type
Article
Publication Date
2-2016
Department
Department of Biological Sciences
Abstract
Previously, our molecular binding study showed that prohibitin interacts with phospholipids, including phosphatidylinositide and cardiolipin. Under stress conditions, prohibitin interacts with cardiolipin as a retrograde response to activate mitochondrial proliferation. The lipid-binding switch mechanism of prohibitin with phosphatidylinositol-3,4,5-triphosphate and cardiolipin may suggest the role of prohibitin effects on energy metabolism and age-related diseases. The current study examined the region-specific expressions of prohibitin with respect to the retina and retinal pigment epithelium (RPE) in age-related macular degeneration (AMD). A detailed understanding of prohibitin binding with lipids, nucleotides, and proteins shown in the current study may suggest how molecular interactions control apoptosis and how we can intervene against the apoptotic pathway in AMD. Our data imply that decreased prohibitin in the peripheral RPE is a significant step leading to mitochondrial dysfunction that may promote AMD progression.
Publication Title
Protein Journal
Recommended Citation
Sripathi, S.,
Sylvester, O.,
He, W.,
Moser, T.,
Um, J.,
Lamoke, F.,
Ramakrishna, W.,
Bernstein, P.,
Bartoli, M.,
&
Jahng, W.
(2016).
Prohibitin as the Molecular Binding Switch in the Retinal Pigment Epithelium.
Protein Journal,
35(1).
http://doi.org/10.1007/s10930-015-9641-y
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/4958