Interaction of actin filaments with microtubules is mediated by microtubule-associated proteins and regulated by phosphorylation.
نویسندگان
چکیده
We have reconstituted high viscosity networks of actin filaments and microtubules from purified actin, tubulin, and MAPs. MAP-2 can effectively cross-link actin filaments and microtubules, presumably because a low affinity actin binding site is available even when it is bound tightly to microtubules. Phosphorylation of MAP-2 inhibits cross-linking of actin filaments and microtubules. Tau is not an effective cross-linker of actin and microtubules even though it can interact with each polymer individually.
منابع مشابه
Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
We have used low shear viscometry and electron microscopy to study the interaction between pure actin filaments and microtubules. Mixtures of microtubules having microtubule-associated proteins (MAPs) with actin filament have very high viscosities compared with the viscosities of the separate components. MAPs themselves also cause a large increase in the viscosity of actin filaments. In contras...
متن کاملNanobiomechanical Properties of Microtubules
Microtubules, the active filaments with tubular shapes, play important roles in a wide range of cellular functions, including structural supports, mitosis, cytokinesis, and vesicular transport, which are essential for the growth and division of eukaryotic cells. Finding properties of microtubules is one of the main concerns of scientists. This work helps to obtain mechanical properties of m...
متن کاملP 97: Neurodegeneration Induced by Tau protein
Tau is one of several types of microtubule-associated proteins (MAPs), responsible for the assembly and stability of microtubule networks that is present only in neurons and predominantly localized in axons which its functions are tightly regulated by phosphorylation. Via as yet unknown mechanisms, tau becomes hyperphosphorylated and accompanies with neuronal degeneration, loss of synapses...
متن کاملCalmodulin inhibits interaction of actin with MAP2 and Tau, two major microtubule-associated proteins.
We have previously shown that microtubule-associated protein 2 (MAP2) and Tau, two major microtubule-associated proteins, interact with actin differently as measured by low-shear viscosity and that their activities are modified by phosphorylation (Nishida, E., Kotani, S., Kuwaki, T., and Sakai, H. (1982 in Biological Functions of Microtubules and Related Structures (Sakai, H., Mohri, H., and Bo...
متن کاملEffects of microtubule disruption on force, velocity, stiffness and [Ca(2+)](i) in porcine coronary arteries.
Force generated by smooth muscle cells is believed to result from the interaction of actin and myosin filaments and is regulated through phosphorylation of the myosin regulatory light chain (LC(20)). The role of other cytoskeleton filaments, such as microtubules and intermediate filaments, in determining the mechanical output of smooth muscle is unclear. In cultured fibroblasts, microtubule dis...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Annals of the New York Academy of Sciences
دوره 466 شماره
صفحات -
تاریخ انتشار 1986