PTEN , a Putative Protein Tyrosine Phosphatase Gene Mutated in Human Brain, Breast, and Prostate Cancer
Abstract
Mapping of homozygous deletions on human chromosome 10q23 has led to the isolation of a candidate tumor suppressor gene, PTEN, that appears to be mutated at considerable frequency in human cancers. In preliminary screens, mutations of PTEN were detected in 31% (13/42) of glioblastoma cell lines and xenografts, 100% (4/4) of prostate cancer cell lines, 6% (4/65) of breast cancer cell lines and xenografts, and 17% (3/18) of primary glioblastomas. The predicted PTEN product has a protein tyrosine phosphatase domain and extensive homology to tensin, a protein that interacts with actin filaments at focal adhesions. These homologies suggest that PTEN may suppress tumor cell growth by antagonizing protein tyrosine kinases and may regulate tumor cell invasion and metastasis through interactions at focal adhesions.
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PTEN is inactive in a large number of cancers where miR-21 is upregulated, including glioblastomas.
“PTEN, a well-studied tumor suppressor gene is inactive in a large number of cancers where miR-21 is upregulated, including glioblastomas (17,18).”
From MicroRNA-21 Targets a Network of Key Tumor-Suppressive Pathways in Glioblastoma Cells (2008) · cites this paper as [17]
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- Authors
- Li, J., Yen, C., Liaw, D., Podsypanina, K., Bose, S., Wang, S. I., Puc, J., Miliaresis, C., Rodgers, L., McCombie, R., Bigner, S. H., Giovanella, B. C., Ittmann, M., Tycko, B., Hibshoosh, H., Wigler, M. H., & Parsons, R.
- Affiliations
- Columbia University (US)
- Cold Spring Harbor Laboratory (US)
- C. Yen, L. Rodgers, R. McCombie, M. Wigler, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
- Duke Medical Center (US)
- Christus Stehlin Foundation for Cancer Research (US)
- New York University (US)
- Corresponding author
- Li, Jing
- Yen, Clifford
- Liaw, Danny
- Podsypanina, Katrina
- Parsons, Ramon
- ORCID
- Venue
- Science
- Published
- 1997-03-28
- Volume
- 275
- Issue
- 5308
- Pages
- 1943-1947
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2161810908
- Cited by
- 4,785
- References
- 0
- Citations by year
- 2026: 34 · 2025: 57 · 2024: 95 · 2023: 102 · 2022: 130 · 2021: 108 · 2020: 127 · 2019: 166 · 2018: 130 · 2017: 149 · 2016: 151 · 2015: 193 · 2014: 190 · 2013: 213 · 2012: 223
- FWCI
- 69.93
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- Funders
- National Institutes of Health (5r35ca039829-13)
- National Cancer Institute (5R35 CA39829)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- PTEN, tumor suppressor, protein tyrosine phosphatase, glioblastoma, prostate cancer, breast cancer, tensin, focal adhesions, F-actin, tumor invasion, metastasis
- MeSH terms
- Tensins, Amino Acid Sequence, Brain Neoplasms, Breast Neoplasms, Chromosome Mapping, Chromosomes, Human, Pair 10, Female, Glioblastoma, Humans, Male, Microfilament Proteins, Molecular Sequence Data, Mutation, Neoplasm Transplantation, Neoplasms, Phosphoric Monoester Hydrolases, Prostatic Neoplasms, Protein-Tyrosine Kinases, Transplantation, Heterologous, Tumor Cells, Cultured, Genes, Tumor Suppressor, Frameshift Mutation, Protein Tyrosine Phosphatases, Sequence Deletion, Sequence Homology, Amino Acid, Phosphotyrosine, Tumor Suppressor Proteins, PTEN Phosphohydrolase
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