ArticleThe Journal of biological chemistry2011
A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 43 citations in OpenAlex.
- Membrane-bound Heat Shock Protein mHsp70 Is Required for Migration and Invasion of Brain Tumors.Cancer research communications · 2024Article
- Review
- Glutamine prevents acute kidney injury by modulating oxidative stress and apoptosis in tubular epithelial cells.JCI insight · 2022Article
- HSP70s in Breast Cancer: Promoters of Tumorigenesis and Potential Targets/Tools for Therapy.Cells · 2021Review
- Article
- Expression of the Alternative Oxidase Influences Jun N-Terminal Kinase Signaling and Cell Migration.Molecular and cellular biology · 2018Article
- A small molecule regulator of tissue transglutaminase conformation inhibits the malignant phenotype of cancer cells.Oncotarget · 2018Article
- The diamond anniversary of tissue transglutaminase: a protein of many talents.Drug discovery today · 2018Review
- Opening up about Tissue Transglutaminase: When Conformation Matters More than Enzymatic Activity.Med one · 2018Article
- The stem cell/cancer stem cell marker ALDH1A3 regulates the expression of the survival factor tissue transglutaminase, in mesenchymal glioma stem cells.Oncotarget · 2017Article
- Evidence of a Cell Surface Role for Hsp90 Complex Proteins Mediating Neuroblast Migration in the Subventricular Zone.Frontiers in cellular neuroscience · 2017Article
- Upregulation of heat shock protein 70 and the differential protein expression induced by tumor necrosis factor-alpha enhances migration and inhibits apoptosis of hepatocellular carcinoma cell HepG2.International journal of medical sciences · 2017Article
- CHIP-mediated degradation of transglutaminase 2 negatively regulates tumor growth and angiogenesis in renal cancer.Oncogene · 2016Article
- Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.Cell chemical biology · 2016Review
- Targeting the hsp70 gene delays mammary tumor initiation and inhibits tumor cell metastasis.Oncogene · 2015Article
- Physiological, pathological, and structural implications of non-enzymatic protein-protein interactions of the multifunctional human transglutaminase 2.Cellular and molecular life sciences : CMLS · 2015Review
- Oncogenic extracellular HSP70 disrupts the gap-junctional coupling between capillary cells.Oncotarget · 2015Article
- Simultaneously targeting tissue transglutaminase and kidney type glutaminase sensitizes cancer cells to acid toxicity and offers new opportunities for therapeutic intervention.Molecular pharmaceutics · 2015Article
- Transglutaminase 2 in cancer.American journal of cancer research · 2015Article
- Heat Shock Protein 70 (Hsp70) Peptide Activated Natural Killer (NK) Cells for the Treatment of Patients with Non-Small Cell Lung Cancer (NSCLC) after Radiochemotherapy (RCTx) - From Preclinical Studies to a Clinical Phase II Trial.Frontiers in immunology · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cell migration is essential for several important biological outcomes and is involved in various developmental disorders and disease states including cancer cell invasiveness and metastasis. A fundamental step in cell migration is the development of a leading edge. By using HeLa carcinoma cells as an initial model system, we uncovered a surprising role for the heat shock protein 70 (Hsp70) and its ability to bind the protein cross-linking enzyme, tissue transglutaminase (tTG), in cancer cell migration. Treatment of HeLa cells with EGF results in the activation of a plasma membrane-associated pool of tTG and its redistribution to the leading edges of these cells, which are essential events for EGF-stimulated HeLa cell migration. However, we then found that the ability of tTG to be localized to the leading edge is dependent on Hsp70. Similarly, the localization of tTG to the leading edges of MDAMB231 breast carcinoma cells, where it also plays an essential role in their migration, has a strict requirement for Hsp70. Treatment of these different cell lines with inhibitors against the ATP hydrolytic activity of Hsp70 prevented tTG from localizing to their leading edges and thereby blocked EGF-stimulated HeLa cell migration, as well as the constitutive migration normally exhibited by MDAMB231 cells. These findings highlight a new and unconventional role for the chaperonin activity of Hsp70 in the localization of a key regulatory protein (tTG) at the leading edges of cancer cells and the important consequences that this holds for their ability to migrate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.