Structural molecular details of the endocytic adaptor protein CALM upon binding with phosphatidylinositol 4,5-bisphosphate-containing model membranes.

ABSTRACT: Clathrin assembly lymphoid myeloid leukaemia protein (CALM) is involved in the formation of clathrin-mediated endocytic coats by virtue of binding many proteins involved in the process, including clathrin itself and AP2 cargo adaptor complex. CALM is able to specifically recognize the inner leaflet of the plasma membrane by binding the membrane's phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P₂). Here, a quantitative biophysical approach -combining neutron/X-ray scattering, solid-state NMR, atomic force microscopy, and quartz crystal microbalance with dissipation monitoring-, was exploited to investigate CALM interaction with PtdIns(4,5)P₂-presenting model membranes. The presented experimental data reveal CALM's folded domain partially embeds (12% volume occupancy

SUBMITTER: Santamaria A 

PROVIDER: S-EPMC12307879 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature