© 1999 by Oxford University Press
Journal of the National Cancer Institute, Vol. 91, No. 22, 1922-1932,
November 17, 1999
© 1999 Oxford University Press
REVIEW |
Mutational Spectra of PTEN/MMAC1 Gene: a Tumor Suppressor With Lipid Phosphatase Activity
Affiliations of authors: I. U. Ali, Division of Cancer Prevention, National Cancer Institute, Bethesda, MD; L. M. Schriml, M. Dean, Laboratory of Genomic Diversity, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, MD.
Correspondence to: Iqbal U. Ali, Ph.D., National Institutes of Health, Executive Plaza North, Rm. 201, Bethesda, MD 20892-7332 (e-mail: ia1t{at}nih.gov).
PTEN/MMAC1 (phosphatase, tensin homologue/mutated in multiple advanced cancers) is a tumor suppressor protein that has sequence homology with dual-specificity phosphatases, which are capable of dephosphorylating both tyrosine phosphate and serine/threonine phosphate residues on proteins. The in vivo function of PTEN/MMAC1 appears to be dephosphorylation of phosphotidylinositol 3,4,5-triphosphate. The PTEN/MMAC1 gene is mutated in the germline of patients with rare autosomal dominant cancer syndromes and in subsets of specific cancers. Here we review the mutational spectra of the PTEN/MMAC1 gene in tumors from various tissues, especially endometrium, brain, prostate, and ovary, in which the gene is inactivated very frequently. Germline and somatic mutations in the PTEN/MMAC1 gene occur mostly in the protein coding region and involve the phosphatase domain and poly(A)6 stretches. Compared with germline alterations found in the PTEN/MMAC1 gene, there is a substantially increased frequency of frameshift mutations in tumors. Glioblastomas and endometrial carcinomas appear to have distinct mutational spectra, probably reflecting differences in the underlying mechanisms of inactivation of the PTEN/MMAC1 gene in the two tissue types. Also, depending on the tissue type, the gene appears to be involved in the initiation or the progression of cancers. Further understanding of PTEN/MMAC1 gene mutations in different tumors and the physiologic consequences of these mutations is likely to open up new therapeutic opportunities for targeting this critical gene.
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M. Aoki, E. Blazek, and P. K. Vogt A role of the kinase mTOR in cellular transformation induced by the oncoproteins P3k and Akt PNAS, January 2, 2001; 98(1): 136 - 141. [Abstract] [Full Text] [PDF]
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M. J. You, D. H. Castrillon, B. C. Bastian, R. C. O'Hagan, M. W. Bosenberg, R. Parsons, L. Chin, and R. A. DePinho Genetic analysis of Pten and Ink4a/Arf interactions in the suppression of tumorigenesis in mice PNAS, February 5, 2002; 99(3): 1455 - 1460. [Abstract] [Full Text] [PDF]
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K. Podsypanina, R. T. Lee, C. Politis, I. Hennessy, A. Crane, J. Puc, M. Neshat, H. Wang, L. Yang, J. Gibbons, et al. An inhibitor of mTOR reduces neoplasia and normalizes p70/S6 kinase activity in Pten+/- mice PNAS, August 28, 2001; 98(18): 10320 - 10325. [Abstract] [Full Text] [PDF]
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M. S. Neshat, I. K. Mellinghoff, C. Tran, B. Stiles, G. Thomas, R. Petersen, P. Frost, J. J. Gibbons, H. Wu, and C. L. Sawyers Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR PNAS, August 28, 2001; 98(18): 10314 - 10319. [Abstract] [Full Text] [PDF]
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B. Kwabi-Addo, D. Giri, K. Schmidt, K. Podsypanina, R. Parsons, N. Greenberg, and M. Ittmann Haploinsufficiency of the Pten tumor suppressor gene promotes prostate cancer progression PNAS, September 25, 2001; 98(20): 11563 - 11568. [Abstract] [Full Text] [PDF]
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