Gadd34 functional domains involved in growth suppression and apoptosis
Gadd34 (also known as MyD116) was originally described as a growth arrest and DNA damage-inducible gene. Increased expression of Gadd34 was subsequently found to correlate with apoptosis, and forced overexpression of the protein leads to apoptosis. Gadd34 protein modulates protein phosphatase type 1...
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Published in | Oncogene Vol. 22; no. 25; pp. 3827 - 3832 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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Nature Publishing
19.06.2003
Nature Publishing Group |
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Abstract | Gadd34 (also known as MyD116) was originally described as a growth arrest and DNA damage-inducible gene. Increased expression of Gadd34 was subsequently found to correlate with apoptosis, and forced overexpression of the protein leads to apoptosis. Gadd34 protein modulates protein phosphatase type 1 activity through both direct binding to the protein, as well as through binding to other proteins that also modulate phosphatase activity. In addition, Gadd34 has a region of homology with the herpes simplex virus type 1 ICP34.5 protein that is involved in the prevention of apoptosis in infected cells. Recently it was reported that a novel rat Gadd34-related gene, PEG-3, was upregulated in transformed cells, and that forced expression of this gene led to increased tumorigenic potential of cells implanted into nude mice and increased angiogenesis of these tumors. We have found, however, that PEG-3 does not exist in normal rat cells, which have a single diploid complement of Gadd34. Sequence analysis of the rat Gadd34 gene and comparison with PEG-3 indicates that PEG-3 is most likely a mutant of Gadd34 that perhaps arose as a result of transformation. This finding suggests that truncated Gadd34 may interfere with normal Gadd34 function in transfected cells. However, human Gadd34 lacking the viral homology domain does not interfere with normal Gadd34-induced apoptosis in cultured cells. This suggests that viral similarity sequences may be required for Gadd34-mediated functions other than apoptosis. |
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AbstractList | Gadd34 (also known as MyD116) was originally described as a growth arrest and DNA damage-inducible gene. Increased expression of Gadd34 was subsequently found to correlate with apoptosis, and forced overexpression of the protein leads to apoptosis. Gadd34 protein modulates protein phosphatase type 1 activity through both direct binding to the protein, as well as through binding to other proteins that also modulate phosphatase activity. In addition, Gadd34 has a region of homology with the herpes simplex virus type 1 ICP34.5 protein that is involved in the prevention of apoptosis in infected cells. Recently it was reported that a novel rat Gadd34-related gene, PEG-3, was upregulated in transformed cells, and that forced expression of this gene led to increased tumorigenic potential of cells implanted into nude mice and increased angiogenesis of these tumors. We have found, however, that PEG-3 does not exist in normal rat cells, which have a single diploid complement of Gadd34. Sequence analysis of the rat Gadd34 gene and comparison with PEG-3 indicates that PEG-3 is most likely a mutant of Gadd34 that perhaps arose as a result of transformation. This finding suggests that truncated Gadd34 may interfere with normal Gadd34 function in transfected cells. However, human Gadd34 lacking the viral homology domain does not interfere with normal Gadd34-induced apoptosis in cultured cells. This suggests that viral similarity sequences may be required for Gadd34-mediated functions other than apoptosis. |
Author | POOLA-KELLA, Silpa HOLLANDER, M. Christine FORNACE, Albert J |
Author_xml | – sequence: 1 givenname: M. Christine surname: HOLLANDER fullname: HOLLANDER, M. Christine organization: Basic Research Laboratory, National Cancer Institute, National Institute of Health, Bethesda, MD 20892-4255, United States – sequence: 2 givenname: Silpa surname: POOLA-KELLA fullname: POOLA-KELLA, Silpa organization: Basic Research Laboratory, National Cancer Institute, National Institute of Health, Bethesda, MD 20892-4255, United States – sequence: 3 givenname: Albert J surname: FORNACE fullname: FORNACE, Albert J organization: Basic Research Laboratory, National Cancer Institute, National Institute of Health, Bethesda, MD 20892-4255, United States |
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Cites_doi | 10.1042/bj3520795 10.1016/S0304-4165(99)00060-4 10.1083/jcb.153.5.1011 10.1128/MCB.19.10.7050 10.1006/bbrc.1999.1991 10.1093/nar/18.9.2823 10.1073/pnas.94.17.9125 10.1006/bbrc.1999.0275 10.1073/pnas.191130798 10.1038/sj.onc.1204258 10.1128/MCB.21.20.6841-6850.2001 10.1002/(SICI)1097-4644(20000615)77:4<596::AID-JCB7>3.0.CO;2-K 10.1073/pnas.91.12.5247 10.1128/jvi.70.1.84-90.1996 10.1073/pnas.96.26.15115 10.1074/jbc.272.21.13731 10.1128/MCB.9.10.4196 10.1002/1097-0215(20010220)96:1<22::AID-IJC3>3.0.CO;2-K |
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SubjectTerms | Ageing, cell death Amino Acid Sequence Angiogenesis Animals Antigens, Differentiation Apoptosis Apoptosis - physiology Biological and medical sciences Blotting, Southern Cell Cycle Proteins Cell Division - physiology Cell Line Cell physiology Cell Transformation, Neoplastic - genetics CHOP protein Cricetinae Cricetulus - genetics Diploids DNA damage DNA, Complementary - genetics Fundamental and applied biological sciences. Psychology GADD34 protein Genes Herpes simplex Homology Humans Mice Molecular and cellular biology Molecular Sequence Data Myeloid Cells - cytology Peptide Fragments - chemistry Peptide Fragments - genetics Phosphatase Polymerase Chain Reaction Promoter Regions, Genetic - genetics Protein phosphatase Protein Phosphatase 1 Protein Structure, Tertiary Proteins Proteins - chemistry Proteins - genetics Proteins - physiology Rats - genetics Rats, Sprague-Dawley Recombinant Fusion Proteins - physiology Sequence Alignment Sequence analysis Sequence Deletion Sequence Homology, Amino Acid Species Specificity Structure-Activity Relationship Transfection Transformed cells Tumors |
Title | Gadd34 functional domains involved in growth suppression and apoptosis |
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