Prohibitin as the Molecular Binding Switch in the Retinal Pigment Epithelium

Srinivas R. Sripathi, O’Donnell D. Sylvester, Weilue He, Trevor Moser, Ji Yeon Um, Folami Lamoke Powell, Wusirika Ramakrishna, Paul S. Bernstein, Manuela Bartoli, Wan Jin Jahng

Research output: Contribution to journalArticle

5 Scopus citations

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.

Original languageEnglish (US)
JournalProtein Journal
Volume35
Issue number1
DOIs
StatePublished - Feb 1 2016

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Keywords

  • Macular degeneration
  • Mitochondria
  • Oxidative stress
  • Prohibitin
  • Retinal pigment epithelium

ASJC Scopus subject areas

  • Analytical Chemistry
  • Bioengineering
  • Biochemistry
  • Organic Chemistry

Cite this

Sripathi, S. R., Sylvester, OD. D., He, W., Moser, T., Um, J. Y., Powell, F. L., Ramakrishna, W., Bernstein, P. S., Bartoli, M., & Jahng, W. J. (2016). Prohibitin as the Molecular Binding Switch in the Retinal Pigment Epithelium. Protein Journal, 35(1). https://doi.org/10.1007/s10930-015-9641-y