Genealogy of the α-crystallin—small heat-shock protein superfamily

Jong, Wilfried W. de; Caspers, Gert-Jan; Leunissen, Jack A. M.

doi:10.1016/s0141-8130(98)00013-0

Cited by 461 publications

(368 citation statements)

References 78 publications

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“…Thus, residues 48-55 in Bc contain the RFLDQxFG motif, which is also present in Hsp27 and Hsp20 [241]. Several naturally-occurring mutations in the N-terminal region of Hsp27 have been shown to exist in individuals affected by distal HMN (Table 2; [238]).…”

Section: Mutations In the N-terminal Regionmentioning

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: Mutations In the N-terminal Regionmentioning

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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“…Abbreviations: sHSP, small heat-shock protein: rec-, recombinant; SP buffer, sodium phosphate buffer: DTT, dithiothreitol; CD, circular dichroism; BSA, bovine serum albumin domain which terminates in a short and flexible C-terminal tail [3,9,10]. Subunits generally assemble into large heterogeneous complexes (150-800 kDa), possibly in a flexible micellelike arrangement, with the hydrophobic N-terminal domains directed inward, and the polar C-terminal domains and tails extending into solution [11 14].…”

Section: Introductionmentioning

confidence: 99%

“…In that respect the four 12 kDa sHSPs of Caenorhabditis elegans are of special interest. These are the smallest known representatives of the family, essentially reduced to the core c~-crystallin domain [3,17,18]. Their N-terminal 'domains' comprise a mere 25 26 residues, and C-terminal tails are altogether lacking.…”

Section: Introductionmentioning

confidence: 99%

Caenorhabditis elegans small heat‐shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone‐like activity

et al. 1998

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Four 12.2-12.6 kDa small heat-shock proteins (sHSPs) of Caenorhabditis elegans are the smallest known members of the sHSP family. They essentially comprise the characteristic C-terminal 'ct-crystallin domain' of the sHSPs, having a very short N-terminal region, and lacking a C-terminal tail. Recombinant Hspl2.2 and 12.3 are characterized here. Far-UV CD spectra reveal, as for other sHSPs, predominantly a [~-sheet structure. By gel permeation and crosslinking, they are the first sHSPs shown to occur as tetramers, rather than forming the usual large multimeric complexes. Exceptionally, too, both appear devoid of in vitro chaperone-like abilities. This supports the notion that tetramers are the building blocks of sHSP complexes, and that higher multimer formation, mediated through the N-terminal domains, is a prerequisite for chaperone-like activity.

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“…HSPB8 belongs to the superfamily of mammalian small heat-shock proteins or stress proteins [13][14][15][16] . Members of this superfamily share a conserved α-crystallin domain in their C-terminal part and the WDPF motif in their N-terminal part, whereas other parts of the sequence (N-terminal halves and extreme C-terminal tails) are more variable 17,18 . The missense mutations K141N and K141E are located in the central α-crystallin domain of HSPB8.…”

mentioning

confidence: 99%

Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy

et al. 2004

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Distal hereditary motor neuropathies are pure motor disorders of the peripheral nervous system resulting in severe atrophy and wasting of distal limb muscles 1 . In two pedigrees with distal hereditary motor neuropathy type II linked to chromosome 12q24.3, we identified the same mutation (K141N) in small heat-shock 22-kDa protein 8 (encoded by HSPB8; also called HSP22). We found a second mutation (K141E) in two smaller families. Both mutations target the same amino acid, which is essential to the structural and functional integrity of the small heat-shock protein αA-

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Genealogy of the α-crystallin—small heat-shock protein superfamily

Cited by 461 publications

References 78 publications

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

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

Caenorhabditis elegans small heat‐shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone‐like activity

Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy

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