Structural Basis for Actin Assembly, Activation of ATP Hydrolysis, and Delayed Phosphate Release

Murakami, Kenji; Yasunaga, Takuo; Noguchi, Tarow; Gomibuchi, Yuki; Ngo, Kien Xuan; Uyeda, Taro Q.P.; Wakabayashi, T.

doi:10.1016/j.cell.2010.09.034

Cited by 151 publications

(177 citation statements)

References 48 publications

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“…N and C indicate the N-and Cterminal ends of protein. This diagram is based on the structure of actin subdomains (Kabsch et al 1990;Murakami et al 2010), the position of tropomyosin on F-actin (Lehman et al 2000;Pirani et al 2005;Vibert et al 1997) and the core domain of human troponin (Takeda et al 2003;Vinogradova et al 2005). The tropomyosin overlap region (head-to-tail) depicts interaction with near-neighbor tropomyosin dimer (dark-blue) (Greenfield et al 2006;Murakami et al 2008).…”

Section: Current Conceptions Of the Mechanisms Underlying Length-depementioning

confidence: 99%

Historical perspective on heart function: the Frank–Starling Law

Sequeira

Velden

2015

Biophys Rev

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More than a century of research on the FrankStarling Law has significantly advanced our knowledge about the working heart. The Frank-Starling Law mandates that the heart is able to match cardiac ejection to the dynamic changes occurring in ventricular filling and thereby regulates ventricular contraction and ejection. Significant efforts have been attempted to identify a common fundamental basis for the Frank-Starling heart and, although a unifying idea has still to come forth, there is mounting evidence of a direct relationship between length changes in individual constituents (cardiomyocytes) and their sensitivity to Ca 2+ ions. As the Frank-Starling Law is a vital event for the healthy heart, it is of utmost importance to understand its mechanical basis in order to optimize and organize therapeutic strategies to rescue the failing human heart. The present review is a historic perspective on cardiac muscle function. We Brevive^a century of scientific research on the heart's fundamental protein constituents (contractile proteins), to their assemblies in the muscle (the sarcomeres), culminating in a thorough overview of the several synergistically events that compose the Frank-Starling mechanism. It is the authors' personal beliefs that much can be gained by understanding the Frank-Starling relationship at the cellular and whole organ level, so that we can finally, in this century, tackle the pathophysiologic mechanisms underlying heart failure.

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Section: Current Conceptions Of the Mechanisms Underlying Length-depementioning

confidence: 99%

Historical perspective on heart function: the Frank–Starling Law

Sequeira

Velden

2015

Biophys Rev

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“…For example, protein helical assemblies such as cytoskeletal networks and muscle fibers are essential components in our bodies (1,2). Other helical assemblies include bacterial flagella and secretion systems.…”

mentioning

confidence: 99%

Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches

Zhou

2011

Proc. Natl. Acad. Sci. U.S.A.

116

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Helical assemblies such as filamentous viruses, flagella, and F-actin represent an important category of structures in biology. As the first discovered virus, tobacco mosaic virus (TMV) was at the center of virus research. Previously, the structure of TMV was solved at atomic detail by X-ray fiber diffraction but only for its dormant or high-calcium-concentration state, not its low-calcium-concentration state, which is relevant to viral assembly and disassembly inside host cells. Here we report a helical reconstruction of TMV in its calcium-free, metastable assembling state at 3.3 Å resolution by cryo electron microscopy, revealing both protein side chains and RNA bases. An atomic model was built de novo showing marked differences from the high-calcium, dormant-state structure. Although it could be argued that there might be inaccuracies in the latter structure derived from X-ray fiber diffraction, these differences can be interpreted as conformational changes effected by calcium-driven switches, a common regulatory mechanism in plant viruses. Our comparisons of the structures of the low-and highcalcium states indicate that hydrogen bonds formed by Asp116 and Arg92 in the place of the calcium ion of the dormant (highcalcium) state might trigger allosteric changes in the RNA basebinding pockets of the coat protein. In turn, the coat protein-RNA interactions in our structure favor an adenine-X-guanine (A*G) motif over the G*A motif of the dormant state, thus offering an explanation underlying viral assembly initiation by an AAG motif.H elical assemblies represent a very important class of biological structures, performing various tasks for the proper functions of life or executing malicious functions in disease. For example, protein helical assemblies such as cytoskeletal networks and muscle fibers are essential components in our bodies (1, 2). Other helical assemblies include bacterial flagella and secretion systems. Helical viruses, such as tobacco mosaic virus (TMV), account for a major fraction of the virus kingdom. Such helical structures, bearing a special kind of 2D periodicity and potential flexibility, are difficult for structural determination to atomic resolution by conventional methods including X-ray crystallography and NMR. Thus, the molecular mechanisms of action in many of these systems are not understood to atomic detail. Even for TMV, the first virus ever isolated and extensively studied (3) by both X-ray diffraction (e.g., 4-8) and cryo electron microscopy (cryoEM) (9, 10), we still do not know its structure at atomic detail in a state that is relevant to its assembly and disassembly processes, and the underlying mechanisms of these processes remain unknown.The viral RNA of TMV is infectious by itself, but RNA on its own is very unstable. The addition of a 17-kDa coat protein (CP) around the RNA protects the RNA from degrading and makes TMV very stable. The assembly of a rod-shaped virion begins at a two-turn helical CP complex, called the 20S aggregate (11), which recognizes the initiation moti...

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“…And as is required in our membrane model, an analogous assembly in the opposite direction [16]. The basic element of assembly is monomeric actin.…”

Section: Amyloid and Stacking Assemblymentioning

confidence: 99%

Self-Assembly of Open Protein Systems: A Comprehensive View Based onthe Interactions between 3d Hydrophobic and Electric Dipole MomentVectors

Mozo-Villarías¹,

Cedano²,

Querol³

2017

J Proteomics Bioinform

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Structural Basis for Actin Assembly, Activation of ATP Hydrolysis, and Delayed Phosphate Release

Cited by 151 publications

References 48 publications

Historical perspective on heart function: the Frank–Starling Law

Historical perspective on heart function: the Frank–Starling Law

Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches

Self-Assembly of Open Protein Systems: A Comprehensive View Based onthe Interactions between 3d Hydrophobic and Electric Dipole MomentVectors

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