The spectraplakin Short stop is an actin-microtubule cross-linker that contributes to organization of the microtubule network.
The spectraplakin Short stop is an actin-microtubule cross-linker that contributes to organization of the microtubule network.
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DOI：
10.1091/mbc.e10-01-0011
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发表时间：
2010-05-15
影响因子：
3.3
通讯作者：
Rogers SL
中科院分区：
文献类型：
--
作者：
Applewhite DA;Grode KD;Keller D;Zadeh AD;Slep KC;Rogers SL
肌动蛋白和微管的动力学在许多细胞过程中是协调的，但对介导串扰的分子知之甚少。我们在结构-功能分析中描述了Shot作为交联剂的作用的细胞内动力学。Sort通过EB1与微管相互作用，并通过Gas2结构域与微管晶格相互作用。肌动蛋白和微管的动力学在各种细胞和形态发生过程中是协调的；然而，对介导这种细胞骨架串扰的分子知之甚少。我们正在研究短停蛋白(Sort)，这是唯一的果蝇sptraplakin，作为肌动蛋白-微管交联蛋白的模型。Spectraplakins是一个古老的巨大细胞骨架蛋白家族，对一系列不同的细胞功能是必不可少的；然而，我们对spectraplakins的动态以及它们如何连接肌动蛋白细丝和微管知之甚少。在这项研究中，我们描述了Sort的细胞内动力学，并对其作为细胞骨架交联剂的作用进行了结构-功能分析。我们发现Shoot通过两种不同的机制与微管相互作用。在细胞内部，Shot通过与EB1的相互作用结合了生长的正端。在细胞外周，Sort通过其Gas2结构域与微管晶格结合，而该Sort池通过其NH2末端肌动蛋白结合钙蛋白同源结构域作为交联剂活跃地参与其中。这种交联通过抵抗在细胞质中产生侧向微管运动的力量来维持微管的组织。我们的结果首次描述了这些重要蛋白质的动态，并提供了关于它们如何在细胞骨架串扰中发挥作用的关键见解。
The dynamics of actin and microtubules are coordinated in many cellular processes, but little is known about molecules mediating cross-talk. We describe intracellular dynamics of Shot in a structure-function analysis of its role as a cross-linker. Shot interacts with microtubules two ways through EB1 and along microtubule lattices by the GAS2 domain. The dynamics of actin and microtubules are coordinated in a variety of cellular and morphogenetic processes; however, little is known about the molecules mediating this cytoskeletal cross-talk. We are studying Short stop (Shot), the sole Drosophila spectraplakin, as a model actin–microtubule cross-linking protein. Spectraplakins are an ancient family of giant cytoskeletal proteins that are essential for a diverse set of cellular functions; yet, we know little about the dynamics of spectraplakins and how they bridge actin filaments and microtubules. In this study we describe the intracellular dynamics of Shot and a structure–function analysis of its role as a cytoskeletal cross-linker. We find that Shot interacts with microtubules using two different mechanisms. In the cell interior, Shot binds growing plus ends through an interaction with EB1. In the cell periphery, Shot associates with the microtubule lattice via its GAS2 domain, and this pool of Shot is actively engaged as a cross-linker via its NH2-terminal actin-binding calponin homology domains. This cross-linking maintains microtubule organization by resisting forces that produce lateral microtubule movements in the cytoplasm. Our results provide the first description of the dynamics of these important proteins and provide key insight about how they function during cytoskeletal cross-talk.
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影响因子：
64.5
作者：
Fukata, M;Watanabe, T;Kaibuchi, K
通讯作者：
Kaibuchi, K
DOI：
10.1083/jcb.200109090
发表时间：
2002-03-04
期刊：
The Journal of cell biology
影响因子：
--
作者：
Kuriyama R;Gustus C;Terada Y;Uetake Y;Matuliene J
通讯作者：
Matuliene J
DOI：
10.1083/jcb.140.4.897
发表时间：
1998-02-23
期刊：
The Journal of cell biology
影响因子：
--
作者：
Lantz VA;Miller KG
通讯作者：
Miller KG
DOI：
10.1083/jcb.149.1.195
发表时间：
2000-04-03
期刊：
The Journal of cell biology
影响因子：
--
作者：
Karakesisoglou I;Yang Y;Fuchs E
通讯作者：
Fuchs E
影响因子：
4
作者：
Sanchez-Soriano, Natalia;Travis, Mark;Prokop, Andreas
通讯作者：
Prokop, Andreas