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The phosphorylation-specific association of STMN1 with GRP78 promotes breast cancer metastasis.
Kuang, Xia-Ying; Jiang, He-Sheng; Li, Kai; Zheng, Yi-Zi; Liu, Yi-Rong; Qiao, Feng; Li, Shan; Hu, Xin; Shao, Zhi-Ming.
Affiliation
  • Kuang XY; Key Laboratory of Breast Cancer in Shanghai, Department of Breast Surgery, Fudan University Shanghai Cancer Center, Shanghai, China; Department of Breast Surgery, The First Affiliated Hospital, Sun Yat-Sen University, Guangzhou, China.
  • Jiang HS; Key Laboratory of Breast Cancer in Shanghai, Department of Breast Surgery, Fudan University Shanghai Cancer Center, Shanghai, China; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai, China.
  • Li K; Key Laboratory of Breast Cancer in Shanghai, Department of Breast Surgery, Fudan University Shanghai Cancer Center, Shanghai, China.
  • Zheng YZ; Key Laboratory of Breast Cancer in Shanghai, Department of Breast Surgery, Fudan University Shanghai Cancer Center, Shanghai, China; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai, China.
  • Liu YR; Key Laboratory of Breast Cancer in Shanghai, Department of Breast Surgery, Fudan University Shanghai Cancer Center, Shanghai, China; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai, China.
  • Qiao F; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai, China.
  • Li S; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai, China.
  • Hu X; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai, China. Electronic address: xinhu@fudan.edu.cn.
  • Shao ZM; Key Laboratory of Breast Cancer in Shanghai, Department of Breast Surgery, Fudan University Shanghai Cancer Center, Shanghai, China; Department of Oncology, Shanghai Medical College, Fudan University, Shanghai, China; Institutes of Biomedical Science, Fudan University, Shanghai, China. Electronic ad
Cancer Lett ; 377(1): 87-96, 2016 07 10.
Article in En | MEDLINE | ID: mdl-27130664
ABSTRACT
Metastasis is a major cause of death in patients with breast cancer. Stathmin1 (STMN1) is a phosphoprotein associated with cancer metastasis. It exhibits a complicated phosphorylation pattern in response to various extracellular signals, but its signaling mechanism is poorly understood. In this study, we report that phosphorylation of STMN1 at Ser25 and Ser38 is necessary to maintain cell migration capabilities and is associated with shorter disease-free survival (DFS) in breast cancer. In addition, we report that glucose-regulated protein of molecular mass 78 (GRP78) is a novel phospho-STMN1 binding protein upon STMN1 Ser25/Ser38 phosphorylation. This phosphorylation-dependent interaction is regulated by MEK kinase and is required for STMN1-GRP78 complex stability and STMN1-mediated migration. We also propose a prognostic model based on phospho-STMN1 and GRP78 to assess metastatic risk in breast cancer patients.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Breast Neoplasms / Biomarkers, Tumor / Cell Movement / Stathmin / Heat-Shock Proteins / Lung Neoplasms Type of study: Etiology_studies / Prognostic_studies / Risk_factors_studies Language: En Journal: Cancer Lett Year: 2016 Document type: Article Affiliation country: China

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Breast Neoplasms / Biomarkers, Tumor / Cell Movement / Stathmin / Heat-Shock Proteins / Lung Neoplasms Type of study: Etiology_studies / Prognostic_studies / Risk_factors_studies Language: En Journal: Cancer Lett Year: 2016 Document type: Article Affiliation country: China