Hop: more than an Hsp70/Hsp90 adaptor protein

Odunuga, Odutayo O.; Longshaw, Victoria M.; Blatch, Gregory L.

doi:10.1002/bies.20107

Cited by 202 publications

(156 citation statements)

References 83 publications

(108 reference statements)

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“…4 D). Hsp70 and -90 have been shown to interact (Carrello et al, 2004;Odunuga et al, 2004;Reyes-Del Valle et al, 2005), and we believe that the apparent increased amount of Hsp90 is a result of a dissociation of the Hsp70/90 complex during the ion exchange process, resulting in either increased antigenicity or increased free Hsp90. Interestingly, although addition of recombinant Hsp90 to motoneuron cultures did promote survival, it does not appear to be able to contribute to survival in MEx when Hsp70 is removed (Fig.…”

Section: Caspase-3 Activation Is Reduced When Motoneurons Are Treatedmentioning

confidence: 69%

Extracellular Heat Shock Protein 70: A Critical Component for Motoneuron Survival

Robinson¹,

Tidwell²,

Gould³

et al. 2005

J. Neurosci.

111

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The dependence of developing spinal motoneuron survival on a soluble factor(s) from their target, muscle tissue is well established both in vivo and in vitro. Considering this apparent dependence, we examined whether a specific component of the stress response mediates motoneuron survival in trophic factor-deprived environments. We demonstrate that, although endogenous expression of heat shock protein 70 (HSP70) did not change during trophic factor deprivation, application of e-rhHsp70 (exogenous recombinant human Hsp70) promoted motoneuron survival. Conversely, depletion of HSP70 from chick muscle extract (MEx) potently reduces the survivalpromoting activity of MEx. Additionally, exogenous treatment with or spinal cord overexpression of Hsp70 enhances motoneuron survival in vivo during the period of naturally occurring cell death [programmed cell death (PCD)]. Hindlimb muscle cells and lumbar spinal astrocytes readily secrete HSP70 in vitro, suggesting potential physiological sources of extracellular Hsp70 for motoneurons. However, in contrast to exogenous treatment with or overexpression of Hsp70 in vivo, muscle-targeted injections of this factor in an ex vivo preparation fail to attenuate motoneuron PCD. These data (1) suggest that motoneuron survival requirements may extend beyond classical trophic factors to include HSP70, (2) indicate that the source of this factor is instrumental in determining its trophic function, and (3) may therefore influence therapeutic strategies designed to increase motoneuron Hsp70 signaling during disease or injury.

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Section: Caspase-3 Activation Is Reduced When Motoneurons Are Treatedmentioning

confidence: 69%

Extracellular Heat Shock Protein 70: A Critical Component for Motoneuron Survival

Robinson¹,

Tidwell²,

Gould³

et al. 2005

J. Neurosci.

111

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“…In addition, Hop is involved in cell-cycle regulation and steroid receptor maturation (24,34,35), and it is homologous to the CHIP complex, of importance to CFTR degradation (36). Hop has a conserved cysteine (C403) (23,24) located in an S-nitrosylation motif believed to be relevant to S-nitrosylation (26). We found that GSNO inhibited Hop expression in all cell lines.…”

Section: Discussionmentioning

confidence: 86%

“…These include Hsp90 itself, protein von Hippel Lindau, S100A class proteins, and others (37)(38)(39)(40). Hop is believed to have an array of important cellular functions that could be affected by GSNO (23,24), an important consideration with regard to potential toxicities of S-nitrosothiol therapies.…”

Section: Discussionmentioning

confidence: 99%

Hsp 70/Hsp 90 organizing protein as a nitrosylation target in cystic fibrosis therapy

Marozkina¹,

Yemen²,

Borowitz³

et al. 2010

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

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The endogenous signaling molecule S-nitrosoglutathione (GSNO) and other S-nitrosylating agents can cause full maturation of the abnormal gene product ΔF508 cystic fibrosis (CF) transmembrane conductance regulator (CFTR). However, the molecular mechanism of action is not known. Here we show that Hsp70/Hsp90 organizing protein (Hop) is a critical target of GSNO, and its S-nitrosylation results in ΔF508 CFTR maturation and cell surface expression. S-nitrosylation by GSNO inhibited the association of Hop with CFTR in the endoplasmic reticulum. This effect was necessary and sufficient to mediate GSNO-induced cell-surface expression of ΔF508 CFTR. Hop knockdown using siRNA recapitulated the effect of GSNO on ΔF508 CFTR maturation and expression. Moreover, GSNO acted additively with decreased temperature, which promoted mutant CFTR maturation through a Hop-independent mechanism. We conclude that GSNO corrects ΔF508 CFTR trafficking by inhibiting Hop expression, and that combination therapiesusing differing mechanisms of action-may have additive benefits in treating CF.cystic fibrosis transmembrane conductance regulator | S-nitrosoglutathione corrector | treatment

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“…Two members of the HSP90 family was also upregulated (HSP90AB1, HSP90AA1) and so was cofactor AHSA1 which interacts with HSP90AA1 as an activator, while the HSP90s assists in protein folding and protein stabilization (Panaretou et al 2002). STIP1, a member of HSP70-HSP90 organizing protein (HOP) family which functions as a cochaperone that reversibly links together HSP70 and HSP90 protein chaperones (Odunuga et al 2004) and prostaglandin E synthase 3 (PTGES3) which functions as a cochaperone, along with HSP90 were also upregulated. HS results in an increase in cytotoxic protein in the endoplasmic reticulum (ER), HERPUD1 which was found to be upregulated in this study functions in processing and degradation of these cytotoxic protein by participating in ER-associated degradation (ERAD) (Nogalska et al 2006).…”

Section: Heat Stress Resulted In the Activation Of Heat Shock Factorsmentioning

confidence: 99%

Characterization of genes and pathways that respond to heat stress in Holstein calves through transcriptome analysis

Srikanth

Kwon

Lee

2017

Cell Stress and Chaperones

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This study aimed to investigate the genes and pathways that respond to heat stress in Holstein bull calves exposed to severe ranges of temperature and humidity. A total of ten animals from 4 to 6 months of age were subjected to heat stress at 37°C and 90 % humidity for 12 h. Skin and rectal temperatures were measured before and after heat stress; while no correlation was found between them before heat stress, a moderate correlation was detected after heat stress, confirming rectal temperature to be a better barometer for monitoring heat stress. RNAseq analysis identified 8567 genes to be differentially regulated, out of which 465 genes were significantly upregulated (≥2-fold, P < 0.05) and 49 genes were significantly downregulated (≤2-fold, P < 0.05) in response to heat stress. Significant terms and pathways enriched in response to heat stress included chaperones, cochaperones, cellular response to heat stress, phosphorylation, kinase activation, immune response, apoptosis, Toll-like receptor signaling pathway, Pi3K/AKT activation, protein processing in endoplasmic reticulum, interferon signaling, pathways in cancer, estrogen signaling pathway, and MAPK signaling pathway. The differentially expressed genes were validated by quantitative realtime PCR analysis, which confirmed the tendency of the expression. The genes and pathways identified in this analysis extend our understanding of transcriptional response to heat stress and their likely functioning in adapting the animal to hyperthermic stress. The identified genes could be used as candidate genes for association studies to select and breed animals with improved heat tolerance.

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Hop: more than an Hsp70/Hsp90 adaptor protein

Cited by 202 publications

References 83 publications

Extracellular Heat Shock Protein 70: A Critical Component for Motoneuron Survival

Extracellular Heat Shock Protein 70: A Critical Component for Motoneuron Survival

Hsp 70/Hsp 90 organizing protein as a nitrosylation target in cystic fibrosis therapy

Characterization of genes and pathways that respond to heat stress in Holstein calves through transcriptome analysis

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