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Advisory Board and Contents
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2025-01-01 DOI: 10.1016/S0968-0004(24)00286-X
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引用次数: 0
Exploring cross-α amyloids: from functional roles to design innovations 探索交叉α淀粉样蛋白：从功能作用到设计创新。
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.10.004
Sukantha Dey , Rohit Kumar , Rajkumar Mishra , Santu Bera
Amyloids are filamentous protein aggregates that have traditionally been associated with neurodegenerative diseases, although they are also known to play pivotal functional roles across diverse forms of life. Although the cross-β structure has represented the hallmark of amyloidal assemblies, a cross-α structure was recently characterized as a functional microbial amyloid, and further work has shown that de novo designed sequences also assemble into cross-α amyloids, emphasizing cross-α as an alternative paradigm for self-assembly into ordered aggregates. In this review, we summarize recent discoveries of cross-α amyloids both in nature and artificially designed systems, and we describe their fundamental structural organization, self-assembly mechanisms, and biological functions. Finally, we outline the future opportunities for research and development in this potential field.
淀粉样蛋白是一种丝状蛋白质聚集体，传统上与神经退行性疾病相关，尽管人们也知道它们在各种生命形式中发挥着关键的功能作用。尽管交叉β结构一直是淀粉样体组装的标志，但最近一种交叉α结构被鉴定为功能性微生物淀粉样体，进一步的研究表明，从头设计的序列也能组装成交叉α淀粉样体，从而强调了交叉α是自组装成有序聚集体的另一种范例。在这篇综述中，我们总结了最近在自然界和人工设计的系统中发现的交叉α淀粉体，并描述了它们的基本结构组织、自组装机制和生物功能。最后，我们概述了这一潜在领域未来的研究和发展机会。
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引用次数: 0
Catchers of folding gone awry: a tale of small heat shock proteins 折叠出错的捕手：小型热休克蛋白的故事。
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.08.003
Carsten Peters , Martin Haslbeck , Johannes Buchner
Small heat shock proteins (sHsps) are an important part of the cellular system maintaining protein homeostasis under physiological and stress conditions. As molecular chaperones, they form complexes with different non-native proteins in an ATP-independent manner. Many sHsps populate ensembles of energetically similar but different-sized oligomers. Regulation of chaperone activity occurs by changing the equilibrium of these ensembles. This makes sHsps a versatile and adaptive system for trapping non-native proteins in complexes, allowing recycling with the help of ATP-dependent chaperones. In this review, we discuss progress in our understanding of the structural principles of sHsp oligomers and their functional principles, as well as their roles in aging and eye lens transparency.
小热休克蛋白（sHsps）是在生理和应激条件下维持蛋白质平衡的细胞系统的重要组成部分。作为分子伴侣，它们以不依赖 ATP 的方式与不同的非本源蛋白质形成复合物。许多 sHsps 形成了能量相似但大小不同的寡聚体组合。通过改变这些组合体的平衡来调节伴侣活性。这使得 sHsps 成为一种多功能的适应性系统，可将非本地蛋白质困在复合物中，并在 ATP 依赖性伴侣的帮助下进行回收。在这篇综述中，我们将讨论对 sHsp 寡聚体结构原理及其功能原理的理解进展，以及它们在衰老和眼睛晶状体透明度中的作用。
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引用次数: 0
Structural diversity of the CE-clan proteases in bacteria to disarm host ubiquitin defenses 细菌中解除宿主泛素防御的 CE 族蛋白酶的结构多样性。
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.09.001
Lucía Sánchez-Alba , Helena Borràs-Gas , Ge Huang , Nathalia Varejão , David Reverter
Ubiquitin (Ub) and ubiquitin-like (UbL) modifications are critical regulators of multiple cellular processes in eukaryotes. These modifications are dynamically controlled by proteases that balance conjugation and deconjugation. In eukaryotes, these proteases include deubiquitinases (DUBs), mostly belonging to the CA-clan of cysteine proteases, and ubiquitin-like proteases (ULPs), belonging to the CE-clan proteases. Intriguingly, infectious bacteria exploit the CE-clan protease fold to generate deubiquitinating activities to disarm the immune system and degradation defenses of the host during infection. In this review, we explore the substrate preferences encoded within the CE-clan proteases and the structural determinants in the protease fold behind its selectivity, in particular those from infectious bacteria and viruses. Understanding this protease family provides crucial insights into the molecular mechanisms underlying infection and transmission of pathogenic organisms.
泛素（Ub）和类泛素（UbL）修饰是真核生物多种细胞过程的关键调节因子。这些修饰受蛋白酶的动态控制，蛋白酶可平衡共轭和解共轭作用。在真核生物中，这些蛋白酶包括主要属于半胱氨酸蛋白酶 CA 族的去泛素酶（DUBs）和属于 CE 族蛋白酶的类泛素蛋白酶（ULPs）。耐人寻味的是，感染性细菌利用 CE 族蛋白酶折叠产生去泛素化活性，从而在感染期间解除宿主免疫系统和降解防御系统的武装。在这篇综述中，我们探讨了 CE 族蛋白酶编码的底物偏好以及蛋白酶折叠结构决定因素在其选择性背后的作用，特别是那些来自传染性细菌和病毒的蛋白酶。了解这一蛋白酶家族有助于深入了解病原体感染和传播的分子机制。
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引用次数: 0
Anything you can do, glycans do better: deglycosylation and noncanonical ubiquitination vie to rule the proteasome 你能做的任何事情，聚糖都能做得更好：脱糖基化和非经典泛素化争夺蛋白酶体的统治权。
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.10.001
Nicolas Lehrbach
The Nrf1/Nfe2L1 transcription factor is a master regulator of proteasome biogenesis. New work by Yoshida and colleagues reveals a surprising mechanism by which ubiquitination of N-glycosylated Nrf1 controls its function.
Nrf1/Nfe2L1 转录因子是蛋白酶体生物生成的主调节因子。Yoshida 及其同事的新研究揭示了 N-糖基化 Nrf1 泛素化控制其功能的惊人机制。
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引用次数: 0
Eph receptor signaling complexes in the plasma membrane 质膜中的 Eph 受体信号复合体
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.10.002
Elena B. Pasquale
Eph receptor tyrosine kinases, together with their cell surface-anchored ephrin ligands, constitute an important cell–cell communication system that regulates physiological and pathological processes in most cell types. This review focuses on the multiple mechanisms by which Eph receptors initiate signaling via the formation of protein complexes in the plasma membrane. Upon ephrin binding, Eph receptors assemble into oligomers that can further aggregate into large complexes. Eph receptors also mediate ephrin-independent signaling through interplay with intracellular kinases or other cell-surface receptors. The distinct characteristics of Eph receptor family members, as well as their conserved domain structure, provide a framework for understanding their functional differences and redundancies. Possible areas of interest for future investigations of Eph receptor signaling complexes are also highlighted.
Eph受体酪氨酸激酶与其细胞表面锚定的ephrin配体共同构成了一个重要的细胞-细胞通讯系统，调节着大多数细胞类型的生理和病理过程。本综述将重点介绍 Eph 受体通过在质膜上形成蛋白复合物来启动信号传导的多种机制。Ephrin结合后，Eph受体聚集成寡聚体，然后进一步聚合成大型复合物。Eph 受体还可通过与细胞内激酶或其他细胞表面受体相互作用，介导不依赖于ephrin的信号传导。Eph 受体家族成员的不同特征及其保守的结构域结构为了解它们的功能差异和冗余提供了一个框架。此外，还强调了未来研究 Eph 受体信号复合体可能关注的领域。
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引用次数: 0
Constructive neutral evolution of homodimer to heterodimer transition 同源二聚体向异源二聚体过渡的建设性中性进化。
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.10.003
Lin Chou , Carly J. Houghton , Aaron Wacholder , Anne-Ruxandra Carvunis
Complexification of macrobiomolecules, such as homodimer to heterodimer transitions, are common during evolution. Is such complexification always adaptive? Using large-scale experiments and in-depth biochemical analyses, Després et al. recently demonstrated that an obligate heterodimer can evolve from a homodimer through neutral, nonadaptive events, and quantified key parameters required for such transitions.
在进化过程中，大生物大分子的复杂化（如同源二聚体向异源二聚体的转变）很常见。这种复合是否总是适应性的？最近，Després 等人利用大规模实验和深入的生化分析证明，强制性异源二聚体可以通过中性、非适应性事件从同源二聚体进化而来，并量化了这种转变所需的关键参数。
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引用次数: 0
Subscription and Copyright Information
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/S0968-0004(24)00264-0
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引用次数: 0
Functionalized DNA secondary structures and nanostructures for specific protein modifications 用于特定蛋白质修饰的功能化 DNA 二级结构和纳米结构。
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.09.003
Bauke Albada
The development of non-biological applications of DNA has not only resulted in delicately shaped DNA-based nano-objects with complex functions but also spawned their use for novel catalytic applications. From the multitude of applications of DNAzymes that operate on a relatively simple substrate, we have witnessed the emergence of multifunctional catalytically active DNA-based nanostructures for one of the most challenging tasks known to a chemist: the controlled and precise modification of a wild-type protein in its natural environment. By incorporating various elements associated with post-translational modification (PTM) writer enzymes into complex nanostructures, it is now possible to chemically modify a specific protein in cell lysates under the influence of an externally added trigger, clearly illustrating the promising future for this approach.
脱氧核糖核酸（DNA）非生物应用的发展不仅造就了形状精致、功能复杂的脱氧核糖核酸（DNA）纳米物体，还催生了它们在新型催化应用中的使用。从 DNA 酶在相对简单的底物上的大量应用中，我们看到了多功能催化活性 DNA 纳米结构的出现，这种结构可用于化学家已知的最具挑战性的任务之一：在自然环境中对野生型蛋白质进行可控和精确的修饰。通过在复杂的纳米结构中加入与翻译后修饰（PTM）作者酶相关的各种元素，现在有可能在外部添加触发器的影响下，对细胞裂解物中的特定蛋白质进行化学修饰，这清楚地表明了这种方法的美好前景。
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引用次数: 0
A two-way relationship between histone acetylation and metabolism 组蛋白乙酰化与新陈代谢之间的双向关系
IF 11.6 1区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Trends in Biochemical Sciences
Pub Date : 2024-12-01 DOI: 10.1016/j.tibs.2024.10.005
Evelina Charidemou , Antonis Kirmizis
A link between epigenetics and metabolism was initially recognized because the cellular metabolic state is communicated to the genome through the concentration of intermediary metabolites that are cofactors of chromatin-modifying enzymes. Recently, an additional interaction was postulated due to the capacity of the epigenome to store substantial amounts of metabolites that could become available again to cellular metabolite pools. Here, we focus on histone acetylation and review recent evidence illustrating this reciprocal relationship: in one direction, signaling-induced acetyl-coenzyme A (acetyl-CoA) changes influence histone acetylation levels to regulate genomic functions, and in the opposite direction histone acetylation acts as an acetate reservoir to directly affect downstream acetyl-CoA-mediated metabolism. This review highlights the current understanding, experimental challenges, and future perspectives of this bidirectional interplay.
人们最初认识到表观遗传学与新陈代谢之间的联系，因为细胞的新陈代谢状态是通过作为染色质修饰酶辅助因子的中间代谢物的浓度传递给基因组的。最近，由于表观基因组能够储存大量代谢物，而这些代谢物又可以重新进入细胞代谢物池，因此又推测出了另一种相互作用。在此，我们将重点关注组蛋白乙酰化，并综述了说明这种相互关系的最新证据：在一个方向上，信号诱导的乙酰辅酶 A（乙酰-CoA）变化会影响组蛋白乙酰化水平，从而调节基因组功能；而在另一个相反的方向上，组蛋白乙酰化则充当乙酸盐库，直接影响下游乙酰-CoA 介导的新陈代谢。这篇综述重点介绍了目前对这种双向相互作用的理解、实验挑战和未来展望。
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