Effect of Mutations in the C-Terminal 22-24 Domains of Filamin C Associated with Cardio- and Myopathies on Its Interaction with Small Heat Shock Protein HspB7.

ABSTRACT: We investigated the interaction of HspB7 and its α-crystallin domain with the wild-type (WT) C-terminal fragment of human filamin C (FLNC), containing immunoglobulin-like domains 22-24 and its three mutants associated with cardio- and myopathies. The physicochemical properties of the WT FLNC fragment and its three mutants, p.Glu2472_Asn2473delinsAsp (EN/D) located in the 22nd domain, p.P2643_L2645del (ΔPGL), and p.W2710X (Wmut) both located in the 24th immunoglobulin-like domain were analyzed. Although all FLNC fragments had similar secondary structures, WT FLNC and its EN/D and ΔPGL mutants formed dimers, whereas Wmut formed either monomers or aggregates. The surface hydrophobicity of EN/D, ΔPGL, and especially Wmut mutants was larger than that of the WT fragment. Size exclusion chromatog

SUBMITTER: Muranova LK 

PROVIDER: S-EPMC12193154 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature