Mechanisms of CaaX Protein Processing: Protein Prenylation by FTase and GGTase-I

Blanden, Melanie J.; Ashok, Sudhat; Hougland, James L.

doi:10.1016/b978-0-12-409547-2.14837-1

Cited by 2 publications

(1 citation statement)

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“…The condensation of IPP and DMAPP results in the 10-carbon isoprenoid geranyl pyrophosphate (GPP). Subsequent condensation of 1 or 2 more IPP units to GPP yields the 15-carbon and the 20-carbon isoprenoids FPP and GGPP, respectively ( 17 ). Key mevalonate pathway intermediates IPP, FPP, and GGPP feed into the synthesis of squalene, dolichols, ubiquinone, sterols and derivative steroid hormones, as well as protein prenylation ( 18 ).…”

Section: Introductionmentioning

confidence: 99%

Updates on protein-prenylation and associated inherited retinopathies

Ashok,

Ramachandra Rao

2024

Front. Ophthalmol.

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Membrane-anchored proteins play critical roles in cell signaling, cellular architecture, and membrane biology. Hydrophilic proteins are post-translationally modified by a diverse range of lipid molecules such as phospholipids, glycosylphosphatidylinositol, and isoprenes, which allows their partition and anchorage to the cell membrane. In this review article, we discuss the biochemical basis of isoprenoid synthesis, the mechanisms of isoprene conjugation to proteins, and the functions of prenylated proteins in the neural retina. Recent discovery of novel prenyltransferases, prenylated protein chaperones, non-canonical prenylation-target motifs, and reversible prenylation is expected to increase the number of inherited systemic and blinding diseases with aberrant protein prenylation. Recent important investigations have also demonstrated the role of several unexpected regulators (such as protein charge, sequence/protein-chaperone interaction, light exposure history) in the photoreceptor trafficking of prenylated proteins. Technical advances in the investigation of the prenylated proteome and its application in vision research are discussed. Clinical updates and technical insights into known and putative prenylation-associated retinopathies are provided herein. Characterization of non-canonical prenylation mechanisms in the retina and retina-specific prenylated proteome is fundamental to the understanding of the pathogenesis of protein prenylation-associated inherited blinding disorders.

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Section: Introductionmentioning

confidence: 99%

Updates on protein-prenylation and associated inherited retinopathies

Ashok,

Ramachandra Rao

2024

Front. Ophthalmol.

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Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization

Marchwicka

Kamińska

Monirialamdari

et al. 2022

IJMS

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Protein prenylation is a post-translational modification controlling the localization, activity, and protein–protein interactions of small GTPases, including the Ras superfamily. This covalent attachment of either a farnesyl (15 carbon) or a geranylgeranyl (20 carbon) isoprenoid group is catalyzed by four prenyltransferases, namely farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase-I), Rab geranylgeranyltransferase (GGTase-II), and recently discovered geranylgeranyltransferase type III (GGTase-III). Blocking small GTPase activity, namely inhibiting prenyltransferases, has been proposed as a potential disease treatment method. Inhibitors of prenyltransferase have resulted in substantial therapeutic benefits in various diseases, such as cancer, neurological disorders, and viral and parasitic infections. In this review, we overview the structure of FTase, GGTase-I, GGTase-II, and GGTase-III and summarize the current status of research on their inhibitors.

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Mechanisms of CaaX Protein Processing: Protein Prenylation by FTase and GGTase-I

Cited by 2 publications

References 342 publications

Updates on protein-prenylation and associated inherited retinopathies

Updates on protein-prenylation and associated inherited retinopathies

Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization

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