Actin cytoskeleton and small heat shock proteins: how do they interact?

Mounier, Nicole; Arrigo, André‐Patrick

doi:10.1379/1466-1268(2002)007<0167:acashs>2.0.co;2

Cited by 321 publications

(251 citation statements)

References 83 publications

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“…Moreover, as a result of their ubiquitous role in interacting with and stabilising a wide range of partially unfolded proteins against aggregation, sHsps are involved in many processes central to disease development and manifestation. These include cellular growth and differentiation [84,162,163]; interaction with cytoskeletal components such as actin and intermediate filaments [70,164,165]; and apoptosis [166]. Several of the sHsp family members (Hsp27, HSPB2, Hsp27, Hsp20 and Bc) have been attributed a protective role in the development of neurodegenerative and neuromuscular diseases, roles thought to be related to their abilities to both stabilise target proteins and to interact with cytoskeletal elements as the key features of these diseases are protein aggregation and defective axonal transport [70].…”

Section: Section Iii: Shsps and Their Roles In Diseasementioning

confidence: 99%

Small heat-shock proteins: important players in regulating cellular proteostasis

Treweek

Meehan

Ecroyd

et al. 2014

Cell. Mol. Life Sci.

180

177

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Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of posttranslational modifications in sHsp chaperone function, particularly in the context of disease. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 2 Abstract (word count = 159)Small heat-shock proteins (sHsps) are a diverse family of intracellular molecular chaperone proteins that play a critical role in preventing protein unfolding, misfolding and aggregation, particularly under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) and thereby avoid the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. There has been much research into the structure and mechanism of chaperone action of sHsps over approximately the past 30 years, and significant progress has been made of late, however, there are still many unanswered questions relating to these aspects of sHsps. In this review, we outline some of the recent advances in understanding the structure and function of mammalian sHsps, particularly in the context of their many and varied roles in disease.

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Section: Section Iii: Shsps and Their Roles In Diseasementioning

confidence: 99%

Small heat-shock proteins: important players in regulating cellular proteostasis

Treweek

Meehan

Ecroyd

et al. 2014

Cell. Mol. Life Sci.

180

177

View full text Add to dashboard Cite

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“…Detailed information on the interplay between sHSPs and the extrinsic and intrinsic apoptotic pathways can be found in excellent recent articles (Acunzo et al 2012;Arrigo and Gibert 2014;Bakthisaran et al 2015;Mymrikov et al 2011). Intriguingly, sHSPs also play essential role in cancer cell migration, invasion and metastasis, most probably due to their biochemical cytoskeletal related functions (Mounier and Arrigo 2002), and in cancer-related angiogenesis, expanding their pleiotropic effects on cancer development. Metastasis is the leading cause of death for patients suffering from malignancies.…”

Section: Shsps In Cancermentioning

confidence: 99%

Small heat shock proteins in ageing and age-related diseases

Charmpilas

Kyriakakis

Tavernarakis

2017

Cell Stress and Chaperones

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Small heat shock proteins (sHSPs) are gatekeepers of cellular homeostasis across species, preserving proteome integrity under stressful conditions. Nonetheless, recent evidence suggests that sHSPs are more than molecular chaperones with merely auxiliary role. In contrast, sHSPs have emerged as central lifespan determinants, and their malfunction has been associated with the manifestation of neurological disorders, cardiovascular disease and cancer malignancies. In this review, we focus on the role of sHSPs in ageing and ageassociated diseases and highlight the most prominent paradigms, where impairment of sHSP function has been implicated in human pathology.

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“…Hsp12 and Hsp26 were unique to Bni1-derived cables, but Hsp42 also was identified in association with Las17-derived actin patches (24). sHsps were reported to function as capping proteins or stabilization factors that protect actin filaments from severing proteins via direct or indirect interaction with actin filaments, indicating that functions for this family of proteins in cable regulation should be investigated further (93)(94)(95)(96).…”

Section: Understanding How Actin Cables Of Defined Architecture and Pmentioning

confidence: 99%

Cell-cycle regulation of formin-mediated actin cable assembly

Miao

Wong

Mennella

et al. 2013

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

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Assembly of appropriately oriented actin cables nucleated by formin proteins is necessary for many biological processes in diverse eukaryotes. However, compared with knowledge of how nucleation of dendritic actin filament arrays by the actin-related protein-2/3 complex is regulated, the in vivo regulatory mechanisms for actin cable formation are less clear. To gain insights into mechanisms for regulating actin cable assembly, we reconstituted the assembly process in vitro by introducing microspheres functionalized with the C terminus of the budding yeast formin Bni1 into extracts prepared from yeast cells at different cell-cycle stages. EM studies showed that unbranched actin filament bundles were reconstituted successfully in the yeast extracts. Only extracts enriched in the mitotic cyclin Clb2 were competent for actin cable assembly, and cyclin-dependent kinase 1 activity was indispensible. Cyclin-dependent kinase 1 activity also was found to regulate cable assembly in vivo. Here we present evidence that formin cellcycle regulation is conserved in vertebrates. The use of the cablereconstitution system to test roles for the key actin-binding proteins tropomyosin, capping protein, and cofilin provided important insights into assembly regulation. Furthermore, using mass spectrometry, we identified components of the actin cables formed in yeast extracts, providing the basis for comprehensive understanding of cable assembly and regulation.Cdk1 | three-dimensional structured-illumination microscopy | actin nucleation E ukaryotic cells contain populations of actin structures with distinct architectures and protein compositions, which mediate varied cellular processes (1). Understanding how F-actin polymerization is regulated in time and space is critical to understanding how actin structures provide mechanical forces for corresponding biological processes. Branched actin filament arrays, which concentrate at sites of clathrin-mediated endocytosis (2, 3) and at the leading edge of motile cells (4), are nucleated by the actin-related protein-2/3 (Arp2/3) complex. In contrast, bundles of unbranched actin filaments, which sometimes mediate vesicle trafficking or form myosin-containing contractile bundles, often are nucleated by formin proteins (5-14).Much has been learned about how branched actin filaments are polymerized by the Arp2/3 complex and how these filaments function in processes such as endocytosis (2, 15). In contrast, relatively little is known about how actin cables are assembled under physiological conditions. In previous studies, branched actin filaments derived from the Arp2/3 complex have been reconstituted using purified proteins (16)(17)(18)(19) or cellular extracts (20-25). When microbeads were coated with nucleation-promoting factors for the Arp2/3 complex and then were incubated in cell extracts, actin comet tails were formed by sequential actin nucleation, symmetry breaking, and tail elongation. Importantly, the motility behavior of F-actin assembled by the Arp2/3 complex using defined, purified pr...

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Actin cytoskeleton and small heat shock proteins: how do they interact?

Cited by 321 publications

References 83 publications

Small heat-shock proteins: important players in regulating cellular proteostasis

Small heat-shock proteins: important players in regulating cellular proteostasis

Small heat shock proteins in ageing and age-related diseases

Cell-cycle regulation of formin-mediated actin cable assembly

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