Phospholipid exchange shows insulin receptor activity is supported by both the propensity to form wide bilayers and ordered raft domains.

ABSTRACT: Insulin receptor (IR) is a membrane tyrosine kinase that mediates the response of cells to insulin. IR activity has been shown to be modulated by changes in plasma membrane lipid composition, but the properties and structural determinants of lipids mediating IR activity are poorly understood. Here, using efficient methyl-alpha-cyclodextrin mediated lipid exchange, we studied the effect of altering plasma membrane outer leaflet phospholipid composition upon the activity of IR in mammalian cells. After substitution of endogenous lipids with lipids having an ability to form liquid ordered (Lo) domains (sphingomyelins) or liquid disordered (Ld) domains (unsaturated phosphatidylcholines (PCs)), we found that the propensity of lipids to form ordered domains is required for high IR activity. Addi

SUBMITTER: Suresh P 

PROVIDER: S-EPMC8379460 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature