Interaction of the C-terminal immunoglobulin-like domains (Ig 22–24) of filamin C with human small heat shock proteins

Muranova, L.K.; Vostrikova, V.M.; Shatov, V.M.; Sluchanko, N.N.; Gusev, N.B.

Авторы: Muranova Lydia K., Vostrikova Varvara M., Shatov Vladislav M., Sluchanko Nikolai N., Gusev Nikolai B.
Журнал: Biochimie
Том: 219
Год издания: 2024
Издательство: Elsevier BV
Местоположение издательства: Netherlands
Первая страница: 146
Последняя страница: 154
DOI: 10.1016/j.biochi.2023.11.010
Аннотация: Small heat shock proteins are the well-known regulators of the cytoskeleton integrity, yet their complexes with actin-binding proteins are underexplored. Filamin C, a dimeric 560 kDa protein, abundant in cardiac and skeletal muscle, crosslinks actin filaments and contributes to Z-disc formation and membrane-cytoskeleton attachment. Here, we analyzed the interaction of a human filamin C fragment containing immunoglobulin-like domains 22-24 (FLNC22-24) with five small heat shock proteins (HspB1, HspB5, HspB6, HspB7, HspB8) and their α-crystallin domains. On size-exclusion chromatography, only HspB7 or its α-crystallin domain formed complexes with FLNC22-24. Despite similar isoelectric points of the small heat shock proteins analyzed, only HspB7 and its α-crystallin domain interacted with FLNC22-24 on native gel electrophoresis. Crosslinking with glutaraldehyde confirmed the formation of complexes between HspB7 (or its α-crystallin domain) and the filamin С fragment, inhibiting intersubunit FLNC crosslinking. These data are consistent with the structure modeling using Alphafold. Thus, the C-terminal fragment (immunoglobulin-like domains 22-24) of filamin C contains the site for HspB7 (or its α-crystallin domain) interaction, which competes with FLNC22-24 dimerization and its probable interaction with different target proteins.
Добавил в систему: Гусев Николай Борисович

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Interaction of the C-terminal immunoglobulin-like domains (Ig 22–24) of filamin C with human small heat shock proteinsстатья

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