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Heat Shock Protein 27 Phosphorylation Regulates Tumor Cell Migration under Shear Stress.

ABSTRACT: Heat shock protein 27 (HSP27) is a multifunctional protein that undergoes significant changes in its expression and phosphorylation in response to shear stress stimuli, suggesting that it may be involved in mechanotransduction. However, the mechanism of HSP27 affecting tumor cell migration under shear stress is still not clear. In this study, HSP27-enhanced cyan fluorescent protein (ECFP) and HSP27-Ypet plasmids are constructed to visualize the self-polymerization of HSP27 in living cells based on fluorescence resonance energy transfer technology. The results show that shear stress induces polar distribution of HSP27 to regulate the dynamic structure at the cell leading edge. Shear stress also promotes HSP27 depolymerization to small molecules and then regulates polar actin accumulation and focal adhesion kinase (FAK) polar activation, which further promotes tumor cell migration. This study suggests that HSP27 plays an important role in the regulation of shear stress-induced HeLa cell migration, and it also provides a theoretical basis for HSP27 as a potential drug target for metastasis.

SUBMITTER: Zhang B

PROVIDER: S-EPMC6406706 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

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Heat Shock Protein 27 Phosphorylation Regulates Tumor Cell Migration under Shear Stress.

Zhang Baohong B Xie Fei F Aziz Aziz Ur Rehman AUR Shao Shuai S Li Wang W Deng Sha S Liao Xiaoling X Liu Bo B

Biomolecules 20190130 2

Heat shock protein 27 (HSP27) is a multifunctional protein that undergoes significant changes in its expression and phosphorylation in response to shear stress stimuli, suggesting that it may be involved in mechanotransduction. However, the mechanism of HSP27 affecting tumor cell migration under shear stress is still not clear. In this study, HSP27-enhanced cyan fluorescent protein (ECFP) and HSP27-Ypet plasmids are constructed to visualize the self-polymerization of HSP27 in living cells based ...[more]

PMID: 30704117

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Project description:BACKGROUND:Agriculture is highly dependent on climate. Increases in temperature caused by global warming pose challenges for crop production. Heat stress induces oxidative damage to cell membranes and then causes cell death. Plants have developed various responses to elevated temperatures, including hormone signaling pathways and heat shock factors that elevate their thermotolerance. In response to heat stress, the gaseous hormone ethylene is produced through regulation of the expression of signaling-related genes to modulate resource allocation dynamics. For comprehensive understanding of the role of ethylene, this study used an ethylene precursor to analyze the ethylene signaling pathway involved in adjustment of the homeostasis of the antioxidant system and to evaluate heat shock factor expression in rice seedlings under heat stress. RESULTS:Levels of cell membrane oxidation and ion leakage were reduced in rice seedlings under heat treatment combined with ethylene precursor treatment, conferring enhanced thermotolerance. Reduction of the fresh weight and chlorophyll a/b ratio in rice seedlings was lower in rice seedlings under heat stress with ethylene precursor treatment than in those under heat stress only. Moreover, reduction of antioxidant response caused by heat stress was ameliorated by treatment with ethylene precursors such as catalase and total peroxidase. Quantitative reverse transcriptase-polymerase chain reaction showed higher expression levels of heat shock factors such as HSFA1a and HSFA2a, c, d, e, and f and ethylene-signaling-related genes such as ethylene insensitive 2, ethylene insensitive-like 1, and ethylene insensitive-like 2 in rice seedlings under heat stress with ethylene precursor treatment than in rice seedlings under heat stress only. CONCLUSION:Ethylene-mediated signaling was involved in the reduction of oxidative damage, maintenance of chlorophyll content, and enhancement of thermotolerance in rice seedlings under heat stress. Furthermore, this study revealed heat shock factors and ethylene-signaling-related genes involved in complex network regulation that confers thermotolerance to rice seedlings.

Project description:Small heat-shock proteins (sHSPs) are widely expressed 25-28 kDa proteins whose functions are dynamically regulated by phosphorylation. While recent efforts have clearly delineated a stress-responsive p38 mitogen-activated protein-kinase (MAPK)-dependent kinase pathway culminating in activation of the heat-shock (HSP)-kinases, mitogen-activated protein-kinase-activated protein kinase-2 and -3, not all sHSP phosphorylation events can be explained by the p38 MAPK-dependent pathway. The contribution of protein kinase C (PKC) to sHSP phosphorylation was suggested by early studies but later questioned on the basis of the reported poor ability of purified PKC to phosphorylate sHSP in vitro. The current study re-evaluates the role of PKC in sHSP phosphorylation in the light of the isoform complexity of the PKC family. We evaluated the sHSP phosphorylation status in rat corpora lutea obtained from two stages of pregnancy, mid-pregnancy and late-pregnancy, which express different levels of the novel PKC isoform, PKC-delta. Two-dimensional Western blot analysis showed that HSP-27 was more highly phosphorylated in vivo in corpora lutea of late pregnancy, corresponding to the developmental stage in which PKC-delta is abundant and active. Late-pregnant luteal extracts contained a lipid-sensitive HSP-kinase activity which exactly co-purified with PKC-delta using hydroxyapatite and S-Sepharose column chromatography. To determine whether there might be preferential phosphorylation of sHSP by a particular PKC isoform, purified recombinant PKC isoforms corresponding to those PKC isoforms detected in rat corpora lutea were evaluated for HSP-kinase activity in vitro. Recombinant PKC-delta effectively catalysed the phosphorylation of sHSP in vitro, and PKC-alpha was 30-50% as effective as an HSP-kinase; other PKCs tested (beta1, beta2, epsilon and zeta) were poor HSP-kinases. These results show that select PKC family members can function as direct HSP-kinases in vitro. Moreover, the observation of enhanced luteal HSP-27 phosphorylation in vivo, in late pregnancy, when PKC-delta is abundant and active, suggests that select PKC family members contribute to sHSP phosphorylation events in vivo.

Dataset Information

Heat Shock Protein 27 Phosphorylation Regulates Tumor Cell Migration under Shear Stress.

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Heat Shock Protein 27 Phosphorylation Regulates Tumor Cell Migration under Shear Stress.

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