ArticleBiophysical journal2014
A cholesterol recognition motif in human phospholipid scramblase 1.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 24 citations in OpenAlex.
- The constellation of cholesterol-dependent processes associated with SARS-CoV-2 infection.Progress in lipid research · 2022Review
- Membrane Cholesterol Enrichment of Red Blood Cell-Derived Microparticles Results in Prolonged Circulation.ACS applied bio materials · 2022Article
- Regulation and functions of membrane lipids: Insights fromBBA advances · 2022Review
- Piezo1 Forms Specific, Functionally Important Interactions with Phosphoinositides and Cholesterol.Biophysical journal · 2020Article
- Pb(II) Induces Scramblase Activation and Ceramide-Domain Generation in Red Blood Cells.Scientific reports · 2018Article
- An Unrecognized Function of Cholesterol: Regulating the Mechanism Controlling Membrane Phospholipid Asymmetry.Biochemistry · 2016Article
- A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human phospholipid scramblase 1 (SCR) catalyzes phospholipid transmembrane (flip-flop) motion. This protein is assumed to bind the membrane hydrophobic core through a transmembrane domain (TMD) as well as via covalently bound palmitoyl residues. Here, we explore the possible interaction of the SCR TMD with cholesterol by using a variety of experimental and computational biophysical approaches. Our findings indicate that SCR contains an amino acid segment at the C-terminal region that shows a remarkable affinity for cholesterol, although it lacks the CRAC sequence. Other 3-OH sterols, but not steroids lacking the 3-OH group, also bind this region of the protein. The newly identified cholesterol-binding region is located partly at the C-terminal portion of the TMD and partly in the first amino acid residues in the SCR C-terminal extracellular coil. This finding could be related to the previously described affinity of SCR for cholesterol-rich domains in membranes.
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Registered trials
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