Protein-tyrosine phosphorylation in the Archaea.
AUTOR(ES)
Smith, S C
RESUMO
Sulfolobus sulfataricus ATCC 35091, Haloferax volcanii, and Methanosarcina thermophila TM-1, representing the Euryarchaeota and Crenarchaeota subdomains of the Archaea, contain proteins which are phosphorylated on tyrosine. These data raise fundamental questions as to the origin and evolution of tyrosine phosphorylation, a protein modification that is of pivotal importance in the regulation of the physiology of eukaryotic cells.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=178981Documentos Relacionados
- Nerve growth factor induces protein-tyrosine phosphorylation.
- Protein-tyrosine phosphorylation regulates apoptosis in human eosinophils and neutrophils.
- Angiotensin II stimulates protein-tyrosine phosphorylation in a calcium-dependent manner.
- Dissecting the catalytic mechanism of protein-tyrosine phosphatases.
- Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase.
