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Literature DB >> 31884667

RPE65 Palmitoylation: A Tale of Lipid Posttranslational Modification.

Sheetal Uppal¹, Eugenia Poliakov¹, Susan Gentleman¹, T Michael Redmond².

Abstract

RPE65, the retinal pigment epithelium (RPE) smooth endoplasmic reticulum (sER) membrane-associated retinoid isomerase, plays an indispensable role in sustaining visual function in vertebrates. An important aspect which has attracted considerable attention is the posttranslational modification by S-palmitoylation of RPE65. Some studies show that RPE65 is a palmitoylated protein, but others deny that conclusion. While it is considered to be mainly responsible for RPE65's membrane association, we still lack conclusive evidence about RPE65 palmitoylation. In this review, we provide an overview of the history and current understanding of RPE65 palmitoylation.

Entities: Chemical

Keywords: Membrane association; Posttranslational modification; RPE65; Retinoid isomerase; S-palmitoylation; Smooth endoplasmic reticulum

Mesh：

Substances：

Year: 2019 PMID： 31884667 PMCID： PMC9351226 DOI： 10.1007/978-3-030-27378-1_88

Source DB: PubMed Journal: Adv Exp Med Biol ISSN： 0065-2598 Impact factor: 3.650

29 in total

1. RPE65 is the isomerohydrolase in the retinoid visual cycle.

Authors: Gennadiy Moiseyev; Ying Chen; Yusuke Takahashi; Bill X Wu; Jian-Xing Ma
Journal: Proc Natl Acad Sci U S A Date: 2005-08-22 Impact factor: 11.205

Review 2. DHHC palmitoyl transferases: substrate interactions and (patho)physiology.

Authors: Jennifer Greaves; Luke H Chamberlain
Journal: Trends Biochem Sci Date: 2011-03-08 Impact factor: 13.807

3. Molecular cloning and expression of RPE65, a novel retinal pigment epithelium-specific microsomal protein that is post-transcriptionally regulated in vitro.

Authors: C P Hamel; E Tsilou; B A Pfeffer; J J Hooks; B Detrick; T M Redmond
Journal: J Biol Chem Date: 1993-07-25 Impact factor: 5.157

4. Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle.

Authors: T M Redmond; S Yu; E Lee; D Bok; D Hamasaki; N Chen; P Goletz; J X Ma; R K Crouch; K Pfeifer
Journal: Nat Genet Date: 1998-12 Impact factor: 38.330

5. The retinal pigment epithelial membrane receptor for plasma retinol-binding protein. Isolation and cDNA cloning of the 63-kDa protein.

Authors: C O Båvik; F Lévy; U Hellman; C Wernstedt; U Eriksson
Journal: J Biol Chem Date: 1993-09-25 Impact factor: 5.157

RPE65 Palmitoylation: A Tale of Lipid Posttranslational Modification.

1. RPE65 is the isomerohydrolase in the retinoid visual cycle.

Review 2. DHHC palmitoyl transferases: substrate interactions and (patho)physiology.

3. Molecular cloning and expression of RPE65, a novel retinal pigment epithelium-specific microsomal protein that is post-transcriptionally regulated in vitro.

4. Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle.

5. The retinal pigment epithelial membrane receptor for plasma retinol-binding protein. Isolation and cDNA cloning of the 63-kDa protein.

Review 6. Emerging Roles of DHHC-mediated Protein S-palmitoylation in Physiological and Pathophysiological Context.

7. Role of LRAT on the retinoid isomerase activity and membrane association of Rpe65.

Review 8. The physiology of protein S-acylation.

Review 9. Palmitoylation-dependent protein sorting.

10. Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein.

1. An inducible amphipathic α-helix mediates subcellular targeting and membrane binding of RPE65.

Review 2. Retinal pigment epithelium 65 kDa protein (RPE65): An update.