Department of Cell and Molecular Biology, Göteborgs Universitet, Medicinaregatan 9C, Gothenburg, Sweden.
Cell Stress Chaperones. 2011 Mar;16(2):173-9. doi: 10.1007/s12192-010-0230-x. Epub 2010 Oct 2.
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.
CCT 是分子伴侣 chaperonin 家族的一员，由 8 种不同的亚基组成，这些亚基在 chaperonin 环中占据固定位置。CCT 的活性与细胞骨架的完整性密切相关，因为新合成的肌动蛋白和微管蛋白单体依赖 CCT 来达到其天然构象。此外，CCT 涉及与组装/组装的微丝和微管相互作用的另一个作用正在出现。CCT 也已知与其他蛋白质相互作用，其中只有一些是真正的折叠底物。在这里，我们确定肌动蛋白丝重塑蛋白凝溶胶作为 CCT 的结合伙伴，尽管它不作为经典的折叠底物，但凝溶胶与 CCT 结合具有一定的特异性。在培养细胞中，CCT 单体的水平影响凝溶胶的水平，这表明 CCT 和肌动蛋白细胞骨架之间存在另一种联系，这种联系是通过肌动蛋白丝切断和加帽蛋白凝溶胶介导的。
