Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: evidence for nonclassical substrate interactions |
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Authors: | Karen I Brackley Julie Grantham |
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Institution: | Department of Cell and Molecular Biology, Göteborgs Universitet, Medicinaregatan 9C, 40530 Gothenburg, Sweden |
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Abstract: | CCT is a member of the chaperonin family of molecular chaperones and consists of eight distinct subunit species which occupy
fixed positions within the chaperonin rings. The activity of CCT is closely linked to the integrity of the cytoskeleton as
newly synthesized actin and tubulin monomers are dependent upon CCT to reach their native conformations. Furthermore, an additional
role for CCT involving interactions with assembling/assembled microfilaments and microtubules is emerging. CCT is also known
to interact with other proteins, only some of which will be genuine folding substrates. Here, we identify the actin filament
remodeling protein gelsolin as a CCT-binding partner, and although it does not behave as a classical folding substrate, gelsolin
binds to CCT with a degree of specificity. In cultured cells, the levels of CCT monomers affect levels of gelsolin, suggesting
an additional link between CCT and the actin cytoskeleton that is mediated via the actin filament severing and capping protein
gelsolin. |
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Keywords: | Molecular chaperone CCT Actin cytoskeleton Gelsolin |
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