Desmin’s conformational modulation by hydrophobicity

Abstract

Nucleocytoplasmic transport is one of the key features in regulation of cellular physiology. Developing a better understanding of the molecular mechanism underlying the nucleocytoplasmic shuttling of proteins can broaden our perspective and understanding on the elaborate sorting mechanisms within cells. Desmin is a muscle specific intermediate filament with amphiphilic properties and has interactions with the components of the nuclear pore complex which facilitates the transport between the cytoplasm and nucleus. The study aims to develop a better understanding of the amphiphilic nature of desmin and its relation to nucleocytoplasmic transport. We conducted a proteomic analysis of desmin-immunoprecipitates to identify the nuclear partners of desmin. Additionally, we analysed the amphiphilic nature of desmin using a hydrophobicity assay to determine if it can undergo conformational changes to adapt to a hydrophobic environment. Using proteomic and in silico analysis we demonstrated that desmin interacts with several nups. The hydrophobicity assay results showed that desmin can increase its surface hydrophobicity in a hydrophobic environment. Our findings suggest that desmin has the ability to undergo conformational changes under favourable conditions and possibly can be transported through nucleus via direct interaction with nups. Further analysis is required to understand the functional implications of this conformational change in vivo. Data are available via ProteomeXchange with identifier PXD047121.