Rb Protein - Biochemical and Functional Analysis

Horowitz, Jonathan M.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Cancer Institute (NCI)
• Type: Research Project (R01)
• Project #: 7R01CA053248-08
• Application #: 2696916
• Study Section: Molecular Cytology Study Section (CTY)
• Project Start: 1990-12-12
• Project End: 1999-04-30
• Budget Start: 1998-02-15
• Budget End: 1998-04-30
• Support Year: 8
• Fiscal Year: 1997

Institution

• Name: North Carolina State University Raleigh
• Department: Anatomy/Cell Biology
• Type: Schools of Veterinary Medicine
• City: Raleigh
• State: NC
• Country: United States
• Zip Code: 27695

Publications

Spengler, Mary L; Kennett, Sarah B; Moorefield, K Scott et al. (2005) Sumoylation of internally initiated Sp3 isoforms regulates transcriptional repression via a Trichostatin A-insensitive mechanism. Cell Signal 17:153-66

Moorefield, K Scott; Fry, Sarah J; Horowitz, Jonathan M (2004) Sp2 DNA binding activity and trans-activation are negatively regulated in mammalian cells. J Biol Chem 279:13911-24

Kennett, Sarah B; Moorefield, K Scott; Horowitz, Jonathan M (2002) Sp3 represses gene expression via the titration of promoter-specific transcription factors. J Biol Chem 277:9780-9

Sterner, J M; Dew-Knight, S; Musahl, C et al. (1998) Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7. Mol Cell Biol 18:2748-57

Tao, Y; Kassatly, R F; Cress, W D et al. (1997) Subunit composition determines E2F DNA-binding site specificity. Mol Cell Biol 17:6994-7007

Kennett, S B; Udvadia, A J; Horowitz, J M (1997) Sp3 encodes multiple proteins that differ in their capacity to stimulate or repress transcription. Nucleic Acids Res 25:3110-7

Rogers, K T; Higgins, P D; Milla, M M et al. (1996) DP-2, a heterodimeric partner of E2F: identification and characterization of DP-2 proteins expressed in vivo. Proc Natl Acad Sci U S A 93:7594-9

Sterner, J M; Tao, Y; Kennett, S B et al. (1996) The amino terminus of the retinoblastoma (Rb) protein associates with a cyclin-dependent kinase-like kinase via Rb amino acids required for growth suppression. Cell Growth Differ 7:53-64

Sterner, J M; Murata, Y; Kim, H G et al. (1995) Detection of a novel cell cycle-regulated kinase activity that associates with the amino terminus of the retinoblastoma protein in G2/M phases. J Biol Chem 270:9281-8

Udvadia, A J; Templeton, D J; Horowitz, J M (1995) Functional interactions between the retinoblastoma (Rb) protein and Sp-family members: superactivation by Rb requires amino acids necessary for growth suppression. Proc Natl Acad Sci U S A 92:3953-7