A new list of functions of the cytoskeleton

Jaeken, Laurent

doi:10.1080/15216540701320593

Cited by 16 publications

(9 citation statements)

References 26 publications

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“…They exhibit tensegrity properties, which means that they behave as a unified whole in response to external mechanical forces, which become distributed over the entire network and result in global rearrangements. In this way a cell also achieves mechanical coherence [109]. The observed pre-stress [107] means that the cytoskeleton – also when at rest – stores mechanical energy and hence the R-state is also a high-energy structure from the mechanical perspective, complementing Ling’s view.…”

Section: Introductionmentioning

confidence: 99%

“…Because both the cytoskeleton and the extracellular matrix (i.e. collagen) exhibit piezoelectric properties [110], mechanical coherence goes along with electrical coherence [109]. And because many proteins, multi-protein systems and cell organelles are connected to the cytoskeleton [111] and can be directly influenced by data processing along the cytoskeletal network [92-94], chemical coherence may also become aligned with both mechanical and electrical coherence [109].…”

Section: Introductionmentioning

confidence: 99%

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Coherent Behavior and the Bound State of Water and K+ Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds

Jaeken

Матвеев²

2012

TOBIOCJ

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Observations of coherent cellular behavior cannot be integrated into widely accepted membrane (pump) theory (MT) and its steady state energetics because of the thermal noise of assumed ordinary cell water and freely soluble cytoplasmic K+. However, Ling disproved MT and proposed an alternative based on coherence, showing that rest (R) and action (A) are two different phases of protoplasm with different energy levels. The R-state is a coherent metastable low-entropy state as water and K+ are bound to unfolded proteins. The A-state is the higher-entropy state because water and K+ are free. The R-to-A phase transition is regarded as a mechanism to release energy for biological work, replacing the classical concept of high-energy bonds. Subsequent inactivation during the endergonic A-to-R phase transition needs an input of metabolic energy to restore the low entropy R-state. Matveev’s native aggregation hypothesis allows to integrate the energetic details of globular proteins into this view.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Coherent Behavior and the Bound State of Water and K+ Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds

Jaeken

Матвеев²

2012

TOBIOCJ

Self Cite

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“…They are responsible for keeping a cell shape and implementing the cell's motility but also they play a role of the cell's nervous system: together with extracellular matrix [1] the intracellular networks of proteins process information and implement learning [2][3][4][5][6][7][8][9][10]. By modulating dendritic ion channel activity actin filaments determine rule of neural information processing and facilitate computational abilities of dendritic trees via facilitation of ionic condensation and ion cloud propagation [11].…”

Section: Introductionmentioning

confidence: 99%

Actin quantum automata: Communication and computation in molecular networks

Siccardi

Adamatzky

2015

Nano Communication Networks

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“…The classical functions of the cytoskeleton have been summarized as morphology determination, cell polarity formation, structural support, membrane constitution, cell motility, and receptor or channel localization in the plasma membrane [31][32][33].…”

Section: The Physiological Functions Of the Cytoskeleton And The Regumentioning

confidence: 99%

Novel Insights into the Role of the Cytoskeleton in Cancer

Zhang¹,

Pei²,

Ji³

et al. 2017

Cytoskeleton - Structure, Dynamics, Function and Disease

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The cytoskeleton is a complex network of highly ordered intracellular ilaments that plays a central role in controlling cell shape, division, functions, and interactions in human organs and tissues, but dysregulation of this network can contribute to numerous human diseases, including cancer. To clarify the various functions of the cytoskeleton and its role in cancer progression, in this chapter, we will discuss the microilament (actin cytoskeleton), microtubule (β-tubulin), and intermediate ilament (keratins, cytokeratins, vimentin, and lamins) cytoskeletal structures; analyze the physiological functions of the cytoskeleton and its regulation of cell diferentiation; and investigate the roles of the cytoskeleton in cancer progression, the epithelial-mesenchymal transition process (EMT), and the mechanisms of multidrug resistance (MDR) in relation to the cytoskeleton. Importantly, the cytoskeleton, as a key regulator of the transcription and expression of many genes, is known to be involved in various physiological and pathological processes, which makes the cytoskeleton a novel and highly efective target for assessing the response to antitumor therapy in cancer.Keywords: Cytoskeleton, Regulator, cell diferentiation, drug resistance, EMT IntroductionThe cytoskeleton is a structure similar to a bird's nest; it can be tightly packed or sparse and is found in both prokaryotes and eukaryotes [1]. The main component of the cytoskeleton is protein, and the speciic diferences in structure never afect the type of proteins incorporated [2]. The cytoskeletons of prokaryotes display apparent plasticity in composition, without conservation of the core ilament-forming proteins. However, the eukaryotic cytoskeleton has evolved in a variety of functions through the addition of accessory proteins and extensive There are three main cytoskeletal structures in eukaryotes, microilaments (MFs, ≈7 nm diameter), microtubules (MTs, ≈25 nm diameter), and intermediate ilaments (IFs, ≈10 nm diameter) [1]. MFs are responsible for cell contraction and reinforcement of the cell surface and allow changes in cell morphology. Actin and tubulin are the main globular proteins that form MFs and MTs, respectively. Actin is a ubiquitous eukaryotic ilament-forming protein. Actin ilaments (also called microilaments or F-actin) consist of two proto ilament polymers wound together in a right-handed helix [3]. Eukaryotic actin is a member of a large and diverse superfamily of ATPases that includes Hsp70 chaperones and several classes of sugar/sugar alcohol kinases [4,5] as well as eukaryotic actin-related proteins (ARPs) [6,7]. The actin cytoskeleton is involved in actin-based cytoskeletal structures, including various functionally distinct structures of actin organization, and can be regulated by actin regulatory proteins. It is well known that the actin cortex consists of a dense mesh-like array of F-actin anchored to the cell membranes [8,9]. This structure provides the core "skeleton" of the cell, functioning to deine cell shape and provi...

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A new list of functions of the cytoskeleton

Cited by 16 publications

References 26 publications

Coherent Behavior and the Bound State of Water and K+ Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds

Coherent Behavior and the Bound State of Water and K+ Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bonds

Actin quantum automata: Communication and computation in molecular networks

Novel Insights into the Role of the Cytoskeleton in Cancer

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