Correlative dual-color dSTORM/AFM reveals protein clusters at the cytoplasmic side of human bronchial epithelium membranes.

The organization of a cell membrane is vital for various functions, such as receptor signaling and membrane traffic. However, the understanding of membrane organization remains insufficient, especially the localizations of specific proteins in the cell membrane. Here, we used correlative super-resolution fluorescence/atomic force microscopy to correlate the distributions of specific proteins Na+/K+-ATPase (NKA, an integral membrane protein) and ankyrin G (AnkG, a scaffolding protein) with the topography of the cytoplasmic side of human bronchial epithelium membranes. Our data showed that NKA and AnkG proteins preferred to localize in the protein islands of membranes. Interestingly, we also found that functional domains composed of specific proteins with a few hundreds of nanometers were formed by assembling protein islands with a few tens of nanometers.