Abstract

We will investigate the role of protein phosphorylation in mechanisms of viral transformation and cell growth control. In recent years we have focused on retroviruses whose transforming proteins have tyrosine-specific protein kinase activity. We have identified a number of substrates for tyrosine specific kinases, and we plan to extend our characterization of these substrates and the genes which encode them. We have begun to study growth factor receptors with inducible tyrosine protein kinase activities. We will expand our characterization of these receptors and their relationship to viral transforming proteins. These studies will provide insight into molecular mechanisms of growth control related to cancer.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Unknown (R35)
Project #
5R35CA039780-11
Application #
2089946
Study Section
Special Emphasis Panel (SRC (88))
Project Start
1985-09-30
Project End
1999-05-31
Budget Start
1995-06-01
Budget End
1996-05-31
Support Year
11
Fiscal Year
1995
Total Cost
Indirect Cost

  Institution

Name
Salk Institute for Biological Studies
Department
Type
DUNS #
005436803
City
La Jolla
State
CA
Country
United States
Zip Code
92037

  Publications

Huang, Han-Kuei; Bailis, Julie M; Leverson, Joel D et al. (2005) Suppressors of Bir1p (Survivin) identify roles for the chromosomal passenger protein Pic1p (INCENP) and the replication initiation factor Psf2p in chromosome segregation. Mol Cell Biol 25:9000-15
Verdecia, Mark A; Joazeiro, Claudio A P; Wells, Nicholas J et al. (2003) Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol Cell 11:249-59
Hauck, C R; Hunter, T; Schlaepfer, D D (2001) The v-Src SH3 domain facilitates a cell adhesion-independent association with focal adhesion kinase. J Biol Chem 276:17653-62
Huang, H K; Forsburg, S L; John, U P et al. (2001) Isolation and characterization of the Pin1/Ess1p homologue in Schizosaccharomyces pombe. J Cell Sci 114:3779-88
Loren, C E; Scully, A; Grabbe, C et al. (2001) Identification and characterization of DAlk: a novel Drosophila melanogaster RTK which drives ERK activation in vivo. Genes Cells 6:531-44
Xu, S; Huang, H K; Kaiser, P et al. (2000) Phosphorylation and spindle pole body localization of the Cdc15p mitotic regulatory protein kinase in budding yeast. Curr Biol 10:329-32
Huang, H k; Joazeiro, C A; Bonfoco, E et al. (2000) The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. J Biol Chem 275:26661-4
Jiang, G; den Hertog, J; Hunter, T (2000) Receptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface. Mol Cell Biol 20:5917-29
Pao, G M; Janknecht, R; Ruffner, H et al. (2000) CBP/p300 interact with and function as transcriptional coactivators of BRCA1. Proc Natl Acad Sci U S A 97:1020-5
Potter, L R; Hunter, T (2000) Activation of protein kinase C stimulates the dephosphorylation of natriuretic peptide receptor-B at a single serine residue: a possible mechanism of heterologous desensitization. J Biol Chem 275:31099-106

Showing the most recent 10 out of 88 publications