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The lipid-anchored protein can be located on either side of the cell membrane. Thus, the lipid serves to anchor the protein to the cell membrane. [1] [2] They are a type of proteolipids. The lipid groups play a role in protein interaction and can contribute to the function of the protein to which it is attached. [2]
Glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPI-HBP1) also known as high density lipoprotein-binding protein 1 is a protein that in humans is encoded by the GPIHBP1 gene.
Glycosylated (GPI-anchored) proteins contain a signal sequence, thus directing them to the endoplasmic reticulum (ER). The protein is co-translationally inserted in the ER membrane via a translocon and is attached to the ER membrane by its hydrophobic C terminus; the majority of the protein extends into the ER lumen. The hydrophobic C-terminal ...
The proteolipid code relies on the concept of a zone, which is a functional region of membrane that is assembled and stabilized with both protein and lipid dependency. Integral and lipid-anchored proteins are proposed to form three types of zones: proteins with an associated lipid fingerprint, [9] protein islands, and lipid-only voids. Although ...
Lipid anchored proteins are covalently attached to different fatty acid acyl chains on the cytoplasmic side of the cell membrane via palmitoylation, myristoylation, or prenylation. On the exoplasmic face of the cell membrane, lipid anchored proteins are covalently attached to the lipids glycosylphosphatidylinositol (GPI) and cholesterol.
Type I transmembrane proteins are anchored to the lipid membrane with a stop-transfer anchor sequence and have their N-terminal domains targeted to the endoplasmic reticulum (ER) lumen during synthesis (and the extracellular space, if mature forms are located on cell membranes). Type II and III are anchored with a signal-anchor sequence, with ...
The GPI lipid anchor is a glycolipid found on many blood cells and serves to anchor proteins to the cell surface. The encoded protein is one subunit of the GPI N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to phosphatidylinositol (PI) on the cytoplasmic side of the endoplasmic reticulum. Two alternatively spliced transcripts ...
Glypiation is the addition by covalent bonding of a glycosylphosphatidylinositol (GPI) anchor and is a common post-translational modification that localizes proteins to cell membranes. This special kind of glycosylation is widely detected on surface glycoproteins in eukaryotes and some Archaea .