Dependence of the mechanical properties of actin/α-actinin gels on deformation rate
Dependence of the mechanical properties of actin/α-actinin gels on deformation rate
复制标题
肌动蛋白/α-肌动蛋白凝胶的机械性能对变形率的依赖性
作者：
Masahiko Satō;W. Schwarz;T. Pollard
皮质细胞质，包括卵裂沟，主要由肌动蛋白丝的网络组成，即使在分裂过程中广泛变形，肌动蛋白丝也是刚性的1，2。在这里，我们解决的问题，肌动蛋白丝网络，如那些在皮层可以同时刚性（固体状）和流体状。传统的解释是，肌动蛋白丝通过解聚和再聚合的某种组合重新排列;丝的断裂和退火;以及非离子体之间交联的失活和重建3 -5。我们描述了由肌动蛋白丝和阿米巴α-辅肌动蛋白6 -8组成的模型系统的机械特性，阿米巴和其他细胞中发现的几种肌动蛋白交联蛋白之一4，9。结果表明，另一种分子机制，可能占矛盾的机械性能的皮质。当快速变形时，这些混合物的刚性是不含α-辅肌动蛋白的肌动蛋白丝的40倍，但当缓慢变形时，这些混合物与单独的肌动蛋白丝无法区分。这些时间依赖性的力学性质可以通过肌动蛋白丝之间的多个、快速重排的α-辅肌动蛋白交联来解释，Frey-Wyssling 10提出了一种机制来解释细胞质的行为，早在发现细胞质肌动蛋白或α-辅肌动蛋白之前。如果其他肌动蛋白丝交联蛋白的行为类似于阿米巴α-肌动蛋白，这种机制可以解释皮质如何从小的快速损伤弹性反弹，但在长时间施加微小的力时广泛变形1，11，12
The cortical cytoplasm, including the cleavage furrow, is largely composed of a network of actin filaments that is rigid even as it is extensively deformed during cytokinesis1,2. Here we address the question of how actin-filament networks such as those in the cortex can be simultaneously rigid (solid-like) and fluid-like. Conventional explanations are that actin filaments rearrange by some combination of depolymerization and repolymerization; fragmentation and annealing of filaments; and inactivation and re-establishment of crosslinks between filaments3–5. We describe the mechanical properties of a model system consisting of actin filaments and Acanthamoeba α-actinin6–8, one of several actin crosslinking proteins found in amoeba and other cells4,9. The results suggest another molecular mechanism that may account for the paradoxical mechanical properties of the cortex. When deformed rapidly, these mixtures are 40 times more rigid than actin filaments without α-actinin, but when deformed slowly these mixtures were indistinguishable from filaments alone. These time-dependent mechanical properties can be explained by multiple, rapidly rearranging a-actinin crosslinks between the actin filaments, a mechanism proposed by Frey-Wyssling10 to account for the behaviour of cytoplasm long before the discovery of cyto-plasmic actin or α-actinin. If other actin-filament crosslinking proteins behave like Acanthamoeba α-actinin, this mechanism may explain how the cortex recoils elastically from small rapid insults but deforms extensively when minute forces are applied over long periods of time1,11,12
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影响因子：
5.6
作者：
HARTWIG, JH;STOSSEL, TP
通讯作者：
STOSSEL, TP
F-肌动蛋白流变特性的物理基础。
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Zaner,KS;Stossel,TP
通讯作者：
Stossel,TP
从棘阿米巴中纯化钙敏感肌动蛋白凝胶蛋白。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Pollard,TD
通讯作者：
Pollard,TD
DOI：
10.1016/0006-291x(80)91175-4
发表时间：
1980-01-01
影响因子：
3.1
作者：
MACLEANFLETCHER, S;POLLARD, TD
通讯作者：
POLLARD, TD
DOI：
10.1073/pnas.79.17.5327
发表时间：
1982-01-01
期刊：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子：
--
作者：
PETERSEN, NO;MCCONNAUGHEY, WB;ELSON, EL
通讯作者：
ELSON, EL