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Your search keyword '"Nikolaev, Anatoly Y."' showing total 2 results
Start Over Author "Nikolaev, Anatoly Y." Topic ligases
2 results on '"Nikolaev, Anatoly Y."'

1. PARC: a potential target for cancer therapy.

Author

Nikolaev AY and Gu W

Subjects
Animals, Cell Transformation, Neoplastic genetics, Cell Transformation, Neoplastic metabolism, Gene Expression Regulation, Neoplastic genetics, Humans, Ligases metabolism, Neoplasms metabolism, Neoplasms therapy, Signal Transduction drug effects, Signal Transduction genetics, Tumor Suppressor Protein p53 metabolism, Active Transport, Cell Nucleus genetics, Cell Compartmentation genetics, Eukaryotic Cells metabolism, Ligases genetics, Neoplasms genetics, Tumor Suppressor Protein p53 genetics, Ubiquitin-Protein Ligases, Ubiquitins metabolism
Published
2003

2. Parc: a cytoplasmic anchor for p53.

Author

Nikolaev AY, Li M, Puskas N, Qin J, and Gu W

Subjects
Amino Acid Motifs, Amino Acid Sequence, Apoptosis, Cell Nucleus metabolism, Cytoplasm enzymology, Cytoplasm physiology, Etoposide pharmacology, Gene Expression Regulation, Neoplastic, Glutathione Transferase metabolism, Humans, Molecular Sequence Data, Neoplasm Proteins chemistry, Neoplasm Proteins physiology, Nucleic Acid Synthesis Inhibitors pharmacology, Protein Structure, Tertiary, RNA, Small Interfering metabolism, Sequence Homology, Amino Acid, Tumor Cells, Cultured, Tumor Suppressor Protein p53 chemistry, Ubiquitins metabolism, Cytoplasm metabolism, Ligases chemistry, Ligases metabolism, Ligases physiology, Neoplasm Proteins metabolism, Tumor Suppressor Protein p53 metabolism, Ubiquitin-Protein Ligases
Abstract

Nuclear localization of p53 is essential for its tumor suppressor function. Here, we have identified Parc, a Parkin-like ubiquitin ligase, as a cytoplasmic anchor protein in p53-associated protein complexes. Parc directly interacts and forms a approximately 1 MDa complex with p53 in the cytoplasm of unstressed cells. In the absence of stress, inactivation of Parc induces nuclear localization of endogenous p53 and activates p53-dependent apoptosis. Overexpression of Parc promotes cytoplasmic sequestration of ectopic p53. Furthermore, abnormal cytoplasmic localization of p53 was observed in a number of neuroblastoma cell lines; RNAi-mediated reduction of endogenous Parc significantly sensitizes these neuroblastoma cells in the DNA damage response. These results reveal that Parc is a critical regulator in controlling p53 subcellular localization and subsequent function.

Published
2003
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