Abstract: A novel human protein, CtIP, that interacts with the human cellular protein CtBP, and the nucleotide sequence encoding CtIP are provided. CtIP is useful in diagnostic methods for determining malignancy of cells and in methods for inhibiting neoplasia in patients. Use of CtIP in a method for identifying agents that can inhibit neoplasia of cells is also disclosed.

Abstract: A domain of Bcl-2 that suppresses apoptosis by allowing cell survival permits cell proliferation when mutated. The wild type domain includes amino acid residues 51 to 97 (SEQ ID NO:13) of Bcl-2. Peptides including the domain and nucleotides encoding the domain are useful in molecular screening of human tumors for the presence of mutations that allow proliferation of cells that were otherwise marked for apoptosis. The peptides are also useful to screen for proteins that play a role in the modulation of cellular proliferation.

Abstract: A domain of Bcl-2 that suppresses apoptosis by allowing cell survival permits cell proliferation when mutated. The wild type domain includes amino acid residues 51 to 97 (SEQ ID NO:13) of Bcl-2. Peptides including the domain and nucleotides encoding the domain are useful in molecular screening of human tumors for the presence of mutations that allow proliferation of cells that were otherwise marked for apoptosis. The peptides are also useful to screen for proteins that play a role in the modulation of cellular proliferation.

Abstract: A domain of Bcl-2 that suppresses apoptosis by allowing cell survival permits cell proliferation when mutated. The wild type domain includes amino acid residues 51 to 97 (SEQ ID NO: 13) of Bcl-2. Peptides including the domain and nucleotides encoding the domain are useful in molecular screening of human tumors for the presence of mutations that allow proliferation of cells that were otherwise marked for apoptosis. The peptides are also useful to screen for proteins that play a role in the modulation of cellular proliferation.

Abstract: Adenovirus E1B 19 kD protein protects against cell death induced by viral infection and certain external physical and chemical stimuli. Activity of the 19 kD protein is similar to the cell death suppressing activity of the protein coded by the Bcl-2 protooncogene. Bcl-2 protein can functionally substitute for the E1B 19 kD protein during adenovirus infection and in transformation of primary cells with adenovirus E1A. Five different cDNA's for proteins, designated Nip1, Nip2, Nip3, Bip1A and Bip13 that specifically interact with the 19 kD protein were found. Mutational analysis of the interaction indicates that at least four of the proteins (Nip1, Nip2, Nip3 and Bip1A) associate with 19 kD protein at specific sites thereof. Homologous motifs are found on Bcl2. An additional protein, (Bip5), interacts with Bcl-2 but not with the 19K protein.

Abstract: A domain of Bcl-2 that suppresses apoptosis by allowing cell survival permits cell proliferation when mutated. The wild type domain includes amino acid residues 51 to 97 (SEQ ID NO:13) of Bcl-2. Peptides including the domain and nucleotides encoding the domain are useful in molecular screening of human tumors for the presence of mutations that allow proliferation of cells that were otherwise marked for apoptosis. The peptides are also useful to screen for proteins that play a role in the modulation of cellular proliferation.

Abstract: Cloning of the cDNA for CtBP via yeast two hybrid interaction cloning. The DNA encodes a 439 amino acid (48 kD) protein that specifically interacts with exon 2. This protein requires residues 225-238 of the 243R E1A protein for interaction. The predicted protein sequence of the isolated cDNA is identical to amino acid sequences obtained from peptides prepared from biochemically purified CtBP. Fine mapping of the CtBP-binding domain revealed that a six amino acid motif highly conserved among the E1A proteins of various human and animal adenoviruses is required for this interaction.