Heat shock protein family B member 1 facilitates ezrin activation to control cell migration in esophageal squamous cell carcinoma
| Autor: | En-Min Li, Lian-Di Liao, Li-Yan Xu, Xiu-E Xu, Jian-Jun Xie, Qiang Zhang, Ying-Hua Xie, Jian-Zhong He, Li-Yan Li |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
animal structures Esophageal Neoplasms Amino-Acid N-Acetyltransferase Mutation Missense macromolecular substances environment and public health Biochemistry 03 medical and health sciences 0302 clinical medicine Ezrin Cell Movement Cell Line Tumor Heat shock protein Humans Heat-Shock Proteins Coiled coil Gene knockdown Chemistry Cortical actin cytoskeleton Cell migration Cell Biology Actin cytoskeleton digestive system diseases Neoplasm Proteins Cell biology Cytoskeletal Proteins 030104 developmental biology 030220 oncology & carcinogenesis Phosphorylation Esophageal Squamous Cell Carcinoma Molecular Chaperones |
| Zdroj: | The International Journal of Biochemistry & Cell Biology. 112:79-87 |
| ISSN: | 1357-2725 |
| DOI: | 10.1016/j.biocel.2019.05.005 |
| Popis: | Ezrin plays an important role in the development and progression of human esophageal squamous cell carcinoma (ESCC), providing a link between the cortical actin cytoskeleton and the plasma membrane to govern membrane structure and protrusions. However, the mechanism by which ezrin is activated still remains unknown in ESCC. Here, we identify a novel interaction between ezrin and heat shock protein family B (small) member 1 (HSPB1) in ESCC cells by mass spectroscopy and co-immunoprecipitation. HSPB1 only interacts with inactive ezrin and binds to the α-helical coiled coil region of ezrin. Knockdown of HSPB1 resulted to the decline of phosphorylation at ezrin Thr567, markedly suppressing the ability of ezrin to bind to the actin cytoskeleton and migration of ESCC cells. Furthermore, neither the constitutively active phosphomimetic ezrin T567D, nor inactivated ezrin T567A could restore cell migration following HSPB1 knockdown. Low HSPB1 expression was associated with favorable overall survival of ESCC patients. Taken together, HSPB1, as an important partner, participates in the activation of ezrin and merits further evaluation as a novel therapeutic target against human ESCC. |
| Databáze: | OpenAIRE |
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