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TitleThe Molecular Chaperone CCT Sequesters Gelsolin and Protects it from Cleavage by Caspase-3.
Journal, issue, pagesJ Mol Biol, Vol. 434, Issue 5, Page 167399, Year 2022
Publish dateMar 15, 2022
AuthorsJorge Cuéllar / Josefine Vallin / Andreas Svanström / Moisés Maestro-López / María Teresa Bueno-Carrasco / W Grant Ludlam / Barry M Willardson / José M Valpuesta / Julie Grantham /
PubMed AbstractThe actin filament severing and capping protein gelsolin plays an important role in modulation of actin filament dynamics by influencing the number of actin filament ends. During apoptosis, gelsolin ...The actin filament severing and capping protein gelsolin plays an important role in modulation of actin filament dynamics by influencing the number of actin filament ends. During apoptosis, gelsolin becomes constitutively active due to cleavage by caspase-3. In non-apoptotic cells gelsolin is activated by the binding of Ca. This activated form of gelsolin binds to, but is not a folding substrate of the molecular chaperone CCT/TRiC. Here we demonstrate that in vitro, gelsolin is protected from cleavage by caspase-3 in the presence of CCT. Cryoelectron microscopy and single particle 3D reconstruction of the CCT:gelsolin complex reveals that gelsolin is located in the interior of the chaperonin cavity, with a placement distinct from that of the obligate CCT folding substrates actin and tubulin. In cultured mouse melanoma B16F1 cells, gelsolin co-localises with CCT upon stimulation of actin dynamics at peripheral regions during lamellipodia formation. These data indicate that localised sequestration of gelsolin by CCT may provide spatial control of actin filament dynamics.
External linksJ Mol Biol / PubMed:34896365
MethodsEM (single particle)
Resolution4.5 - 6.0 Å
Structure data

EMDB-13588: Gelsolin-free CCT
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-13747:
CCT-gelsolin complex
Method: EM (single particle) / Resolution: 6.0 Å

Source
  • Homo sapiens (human)

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