MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules.
Agnieszka BiernatowskaKarolina WójtowiczTomasz TrombikAleksander F SikorskiAleksander CzogallaPublished in: Cells (2022)
MPP1 (membrane palmitoylated protein 1) belongs to the MAGUK (membrane-associated guanylate kinase homologs) scaffolding protein family. These proteins organize molecules into complexes, thereby maintaining the structural heterogeneity of the plasma membrane (PM). Our previous results indicated that direct, high-affinity interactions between MPP1 and flotillins (raft marker proteins) display dominant PM-modulating capacity in erythroid cells. In this study, with high-resolution structured illuminated imaging, we investigated how these complexes are organized within erythroid cells on the nanometer scale. Furthermore, using other spectroscopic techniques, namely fluorescence recovery after photobleaching (FRAP) and spot-variation fluorescence correlation spectroscopy (svFCS), we revealed that MPP1 acts as a key raft-capturing molecule, regulating temporal immobilization of flotillin-based nanoclusters, and controls local concentration and confinement of sphingomyelin and Thy-1 in raft nanodomains. Our data enabled us to uncover molecular principles governing the key involvement of MPP1-flotillin complexes in the dynamic nanoscale organization of PM of erythroid cells.
Keyphrases
- induced apoptosis
- high resolution
- cell cycle arrest
- particulate matter
- air pollution
- single molecule
- signaling pathway
- heavy metals
- endoplasmic reticulum stress
- single cell
- cell death
- oxidative stress
- machine learning
- polycyclic aromatic hydrocarbons
- small molecule
- molecular docking
- water soluble
- electronic health record
- cell proliferation
- protein protein
- binding protein
- deep learning