11/7/2022 0 Comments Raft 1.05 lan![]() A general picture emerges now that cell membranes contain cholesterol-rich domains that are generated and regulated by scaffolding proteins like caveolins, stomatins, and flotillin/reggie proteins. ![]() This subcellular distribution and the caveolin-like protein structure suggest important membrane organizing functions for stomatin. Stomatin-carrying endosomes are highly dynamic and interact with lipid droplets suggesting a role in intracellular lipid transport. Stomatin is located at the plasma membrane, particularly in microvilli, in endocytic and exocytic vesicles, and cytoplasmic granules. This mechanism of regulation has been shown for GLUT-1 and may also apply for ion channels. It regulates the activity of various membrane proteins by reversibly recruiting them to lipid rafts. Stomatin associates with cholesterol-rich microdomains (lipid rafts), forms oligomers, and thereby displays a scaffolding function by generating large protein-lipid complexes. ![]() Additional anchoring is provided by palmitoylation and the membrane affinity of the PHB domain. Stomatin has an unusual topology, similar to caveolin-1, with a hydrophobic domain embedded at the cytoplasmic side of the membrane. Related proteins exhibit a common core structure, termed the prohibitin (PHB) domain, with varying extensions. ![]() Orthologues are found in vertebrates, invertebrates, plants, and microorganisms. Stomatin, originally identified as a major protein of the human erythrocyte membrane, is widely expressed in various tissues. ![]()
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