The C-terminal end of PLIN1 displays structural disorder.

ABSTRACT: Lipid droplets (LDs) serve as crucial organelles for lipid storage and metabolism, with their proteome significantly influencing their regulation. Perilipins (PLINs), in particular PLIN1, play vital role in LD metabolism by orchestrating lipolysis. The C-terminal end of PLIN1 regulates lipolysis through interactions with coactivators such as the CGI-58 protein. Despite its importance, the structural characterization of this domain remains limited. Here, we present a comprehensive bioinformatic and biophysical analysis of the C-terminal end of mouse PLIN1 (mPLIN1C). Our findings suggest that mPLIN1C behaves as an intrinsically disordered region (IDR), exhibiting context-dependent properties of the coil-like or pre-molten globule type. Structural analysis reveals a predominance of disordered

SUBMITTER: Paez-Perez ED 

PROVIDER: S-EPMC11914984 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature