A Disulfide Bridge Mediated by Cysteine 574 Is Formed in the Dimer of the 70-kDa Heat Shock Protein

Nemoto, Takayuki K.; Fukuma, Yutaka; Itoh, Hideaki; Takagi, Takashi; Ono, Toshio

doi:10.1093/jb/mvj071

Cited by 17 publications

(24 citation statements)

References 29 publications

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“…HSP70 family members including Hsp70, Hsc70, and the endoplasmic reticulum member BiP have been shown to self-associate (Freiden et al 1992;Benaroudj et al 1995;Wei et al 1995;Gao et al 1996;Angelidis et al 1999;Nemoto et al 2006). In the present report, we demonstrate that Hsp70B′, Hsp70, and Hsc70 form heteromeric complexes in differentiated human neuronal cells.…”

Section: Discussionsupporting

confidence: 57%

“…Structural studies to pinpoint the region involved in selfassociation have focused on Hsc70 (Angelidis et al 1999;Fouchaq et al 1999;Chou et al 2003;Nemoto et al 2006;Amor-Mahjoub et al 2007). The regions essential for selfassociation of Hsc70 were found to be the conserved hydrophobic residues within the interdomain linker region and the helices at the end of the C terminus (AmorMahjoub et al 2007).…”

Section: Discussionmentioning

confidence: 99%

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Heteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B′, in differentiated human neuronal cells

Chow

Mok

Xiao

et al. 2010

Cell Stress and Chaperones

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Human neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis have been termed "protein misfolding disorders." Upregulation of heat shock proteins that target misfolded aggregation-prone proteins has been proposed as a potential therapeutic strategy to counter neurodegenerative disorders. The heat shock protein 70 (HSP70) family is well characterized for its cytoprotective effects against cell death and has been implicated in neuroprotection by overexpression studies. HSP70 family members exhibit sequence and structural conservation. The significance of the multiplicity of HSP70 proteins is unknown. In this study, coimmunoprecipitation was employed to determine if association of HSP70 family members occurs, including Hsp70B′ which is present in the human genome but not in mouse and rat. Heteromeric complexes of Hsp70B′, Hsp70, and Hsc70 were detected in differentiated human SH-SY5Y neuronal cells. Hsp70B′ also formed complexes with Hsp40 suggesting a common co-chaperone for HSP70 family members.

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Section: Discussionsupporting

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Heteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B′, in differentiated human neuronal cells

Chow

Mok

Xiao

et al. 2010

Cell Stress and Chaperones

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“…This indicates that binding of HSP72 in the heated fibers was in some way dependent on reversible oxidation of one or more cysteine residues, which might involve formation of intramolecular or intermolecular disulphide bonds or sulphenation, S-glutathionylation, or Snitrosylation of cysteine residues. HSP72 has five cysteine residues and can form cross-linked dimers involving Cys574 (33). Heat shock cognate protein 70, which is closely related to HSP72 and contains four of the same five cysteine residues, is known to undergo S-glutathionylation, which increases its efficacy as a chaperone (18).…”

Section: Discussionmentioning

confidence: 99%

“…HSP25 has a single cysteine residue in its ␣-crystallin-like domain (31), and S-thiolation of HSP25 regulates its multimeric aggregate size independently of phosphorylation (10,32). HSP72 has five cysteine residues and can form cross-linked dimers (33), and oxidative modification (specifically, S-glutathionylation) is known to increase its chaperone activity (18). ␣B-crystallin does not have any cysteine residues (31), but its activity may be modified by oxidation of its other amino acid residues (41).…”

mentioning

confidence: 99%

Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers

Larkins

Murphy

Lamb

2012

American Journal of Physiology-Cell Physiology

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Larkins NT, Murphy RM, Lamb GD. Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. Am J Physiol Cell Physiol 303: C654 -C665, 2012. First published July 3, 2012; doi:10.1152/ajpcell.00180.2012.-Heat shock proteins (HSPs) help maintain cellular function in stressful situations, but the processes controlling their interactions with target proteins are not well defined. This study examined the binding of HSP72, HSP25, and ␣B-crystallin in skeletal muscle fibers following various stresses. Rat soleus (SOL) and extensor digitorum longus (EDL) muscles were subjected in vitro to heat stress or strongly fatiguing stimulation. Superficial fibers were "skinned" by microdissection and HSP diffusibility assessed from the extent of washout following 10-to 30 min exposure to a physiological intracellular solution. In fibers from nonstressed (control) SOL muscle, Ͼ80% of each HSP is readily diffusible. However, after heating a muscle to 40°C for 30 min ϳ95% of HSP25 and ␣B-crystallin becomes tightly bound at nonmembranous myofibrillar sites, whereas HSP72 bound at membranous sites only after heat treatment to Ն44°C. The ratio of reduced to oxidized cytoplasmic glutathione (GSH:GSSG) decreased approximately two-and fourfold after heating muscles to 40°and 45°C, respectively. The reducing agent dithiothreitol reversed HSP72 binding in heated muscles but had no effect on the other HSPs. Intense in vitro stimulation of SOL muscles, sufficient to elicit substantial oxidation-related loss of maximum force and approximately fourfold decrease in the GSH:GSSG ratio, had no effect on diffusibility of any of the HSPs. When skinned fibers from heat-treated muscles were bathed with additional exogenous HSP72, total binding increased approximately two-and 10-fold, respectively, in SOL and EDL fibers, possibly reflective of the relative sarco(endo)plasmic reticulum Ca 2ϩ -ATPase pump densities in the two fiber types. Phosphorylation at Ser59 on ␣B-crystallin and Ser85 on HSP25 increased with heat treatment but did not appear to determine HSP binding. The findings highlight major differences in the processes controlling binding of HSP72 and the two small HSPs. Binding was not directly related to cytoplasmic oxidative status, but oxidation of cysteine residues influenced HSP72 binding. oxidation; stress response; skinned fiber; chaperones HEAT SHOCK PROTEINS (HSPs) are highly conserved and ubiquitously expressed proteins that act as protein chaperones and in stress situations bind and interact with various proteins to help preserve or restore their function (23,32). A great deal of work in skeletal muscle has focused on the increase in HSP protein and/or mRNA expression levels occurring in hours to days after various stressful stimuli, such as eccentric exercise (11,17,26,27,39), oxidative stress (50), heat (4, 35), and glycogen depletion (12). The present study focuses instead on the acute responses of HSPs to stresses, examining the effects of heat, contraction, and o...

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“…Indeed, ZER showed radiosensitization in an in vitro and in vivo mouse xenografting system. Moreover, ZER-mediated cross-linking was specific for HSP27 because ZER did not induce cross-linking in other proteins, such as HSP70, AKT1, JNK, EGFR, NFkB, and b-actin, even though they have cysteine residues and form disulfide bonds (13)(14)(15)(16). Therefore, it is suggested that abolishing HSP27 function by altered crosslinking of HSP27 is unique for ZER and that ZER may be a specific candidate inhibitor of HSP27.…”

mentioning

confidence: 99%

Altered Cross-Linking of HSP27 by Zerumbone as a Novel Strategy for Overcoming HSP27-Mediated Radioresistance

Choi

Lee

Seo

et al. 2011

International Journal of Radiation Oncology*Biology*Physics

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A Disulfide Bridge Mediated by Cysteine 574 Is Formed in the Dimer of the 70-kDa Heat Shock Protein

Cited by 17 publications

References 29 publications

Heteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B′, in differentiated human neuronal cells

Heteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B′, in differentiated human neuronal cells

Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers

Altered Cross-Linking of HSP27 by Zerumbone as a Novel Strategy for Overcoming HSP27-Mediated Radioresistance

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