AI Article Synopsis
- Human phospholipid scramblase 1 (SCR) facilitates the movement of phospholipids across membranes and is thought to interact with the membrane's hydrophobic core through its transmembrane domain and palmitoyl groups.
- Recent research investigates how the SCR's transmembrane domain interacts with cholesterol, revealing a specific region at the C-terminal that has a strong affinity for cholesterol despite not having the typical CRAC sequence.
- This cholesterol-binding region is partly located within the C-terminal part of the transmembrane domain and the initial amino acids of the SCR's C-terminal extracellular region, which may explain its preference for cholesterol-rich membrane areas.
Article 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4167295 | PMC |
| http://dx.doi.org/10.1016/j.bpj.2014.07.039 | DOI Listing |
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