Genomes and Genes
B J Mayer
Affiliation: Harvard University
- Signal transduction: clamping down on Src activityB J Mayer
Howard Hughes Medical Institute, Children s Hospital, Department of Microbiology and Molecular Genetics, Harvard Medical School, 320 Longwood Avenue, Boston, Massachusetts 02115, USA
Curr Biol 7:R295-8. 1997....
- Protein-protein interactions in signaling cascadesB J Mayer
Howard Hughes Medical Institute, Children s Hospital, Boston, MA, USA
Mol Biotechnol 13:201-13. 1999..In this overview a variety of protein interaction modules are discussed, and issues relating to binding specificity and the significance of a particular interaction are considered...
- Endocytosis: EH domains lend a handB J Mayer
Howard Hughes Medical Institute, Children s Hospital, Department of Microbiology, Harvard Medical School, 300 Longwood Avenue, Boston, Massachusetts, 02115, USA
Curr Biol 9:R70-3. 1999..The three-dimensional structure of an EH domain has recently been solved, and is likely to presage significant advances in understanding molecular mechanisms of endocytosis...
- Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptorT Miyoshi-Akiyama
Laboratory of Molecular Medicine, Children s Hospital and Department of Microbiology and Molecular Genetics, Harvard Medical School, 300 Longwood Avenue, Boston, Massachusetts, MA 02115, USA
Oncogene 20:4058-69. 2001..Studies with Nck mutants suggested that the Nck SH2 domain is responsible for inhibiting the activity of Abl toward both Cbl and Nck itself, most likely by competing with the Abl SH2 for tyrosine-phosphorylated binding sites...
- Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathwayR Rohatgi
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA
J Biol Chem 276:26448-52. 2001..These results suggest the existence of an Nck-dependent, Cdc42-independent mechanism to induce actin polymerization at tyrosine-phosphorylated Nck binding sites...
- Profiling the global tyrosine phosphorylation state by Src homology 2 domain bindingP Nollau
Laboratory of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA
Proc Natl Acad Sci U S A 98:13531-6. 2001..The general strategy we describe here is not limited to Src homology 2 domains and could be used to profile the binding sites for any class of protein interaction domain...
- Abl family kinases and Cbl cooperate with the Nck adaptor to modulate Xenopus developmentC E Adler
Laboratory of Molecular Medicine, Children s Hospital and Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA
J Biol Chem 275:36472-8. 2000..These results suggest a role for both Cbl and Abl family kinases in patterning the Xenopus embryo...
- Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switchM Lei
Laboratory of Molecular Medicine, Children s Hospital, Boston, Massachusetts 02115, USA
Cell 102:387-97. 2000..GTPase binding will refold part of the IS domain and unfold the rest. A related switch has been seen in the Wiskott-Aldrich syndrome protein (WASP)...
- NS5A, a nonstructural protein of hepatitis C virus, binds growth factor receptor-bound protein 2 adaptor protein in a Src homology 3 domain/ligand-dependent manner and perturbs mitogenic signalingS L Tan
Department of Microbiology, School of Medicine, University of Washington, Seattle, WA 98195, USA
Proc Natl Acad Sci U S A 96:5533-8. 1999..Therefore, NS5A may function to perturb Grb2-mediated signaling pathways by selectively targeting the adaptor. These findings highlight a viral interceptor of cellular signaling with potential implications for HCV pathogenesis...
- Concentration-dependent positive and negative regulation of a MAP kinase by a MAP kinase kinaseM W Kieran
Division of Hematology Oncology, Howard Hughes Medical Institute, Children s Hospital, Boston, MA 02115, USA
Oncogene 18:6647-57. 1999..These results reveal a potential mechanism for regulating stress-activated kinases, adding to a growing body of evidence suggesting that MAP kinases are controlled by relatively stable interactions with their activators...
- Cdc42 is required for PIP(2)-induced actin polymerization and early development but not for cell viabilityF Chen
Departments of Genetics, The Center for Blood Research, Harvard Medical School, Boston, MA 02115, USA
Curr Biol 10:758-65. 2000..Also, whereas genetic analyses have shown that Cdc42 is essential for cell viability in yeast, its potential roles in the growth and development of mammalian cells have not been directly assessed...