| Literature DB >> 34562244 |
Maia Kinnebrew1, Kristen A Johnson2, Arun Radhakrishnan3, Rajat Rohatgi4.
Abstract
Cholesterol is an abundant lipid in mammalian plasma membranes that regulates the reception of the Hedgehog (Hh) signal in target cells. In vertebrates, cell-surface organelles called primary cilia function as compartments for the propagation of Hh signals. Recent structural, biochemical, and cell-biological studies have led to the model that Patched-1 (PTCH1), the receptor for Hh ligands, uses its transporter-like activity to lower cholesterol accessibility in the membrane surrounding primary cilia. Cholesterol restriction at cilia may represent the long-sought-after mechanism by which PTCH1 inhibits Smoothened (SMO), a cholesterol-responsive transmembrane protein of the G protein-coupled receptor superfamily that transmits the Hh signal across the membrane.Protein probes based on microbial cholesterol-binding proteins revealed that PTCH1 controls only a subset of the total cholesterol molecules, a biochemically defined fraction called accessible cholesterol. The accessible cholesterol pool coexists (and exchanges) with a pool of sequestered cholesterol, which is bound to phospholipids like sphingomyelin. In this chapter, we describe how to measure the accessible and sequestered cholesterol pools in live cells with protein-based probes. We discuss how to purify and fluorescently label these probes for use in flow cytometry and microscopy-based measurements of the cholesterol pools. Additionally, we describe how to modulate accessible cholesterol levels to determine if this pool regulates Hh signaling (or any other cellular process of interest).Entities:
Keywords: Anthrolysin O; Cholesterol; Hedgehog signaling; Lipids; Ostreolysin A; Patched-1; Perfringolysin O; Primary cilia; Signal transduction; Smoothened; Sphingomyelin
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Year: 2022 PMID: 34562244 PMCID: PMC8819901 DOI: 10.1007/978-1-0716-1701-4_7
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745