Deery W J, Means A R, Brinkley B R
J Cell Biol. 1984 Mar;98(3):904-10. doi: 10.1083/jcb.98.3.904.
A Triton X-100-lysed cell system has been used to identify calmodulin on the cytoskeleton of 3T3 and transformed SV3T3 cells. By indirect immunofluorescence, calmodulin was found to be associated with both the cytoplasmic microtubule complex and the centrosomes. A number of cytoplasmic microtubules more resistant to disassembly upon either cold (0-4 degrees C) or hypotonic treatment, as well as following dilution have been identified. Most of the stable microtubules appeared to be associated with the centrosome at one end and with the plasma membrane at the other end. These microtubules could be induced to depolymerize, however, by micromolar Ca++ concentrations. These data suggest that, by interacting directly with the microtubule, calmodulin may influence microtubule assembly and ensure the Ca++-sensitivity of both mitotic and cytoplasmic microtubules.
利用Triton X-100裂解细胞系统,已在3T3细胞和转化的SV3T3细胞的细胞骨架上鉴定出钙调蛋白。通过间接免疫荧光法发现,钙调蛋白与细胞质微管复合体和中心体均有关联。已鉴定出许多在冷(0-4摄氏度)或低渗处理以及稀释后更抗解聚的细胞质微管。大多数稳定的微管似乎一端与中心体相关,另一端与质膜相关。然而,微摩尔浓度的钙离子可诱导这些微管解聚。这些数据表明,通过直接与微管相互作用,钙调蛋白可能影响微管组装,并确保有丝分裂微管和细胞质微管对钙离子的敏感性。