title: Histidine kinases and histidine phosphorylated proteins in mammalian cell biology, signal transduction and cancer.
abstract: Intensive investigation of protein tyrosine, serine and threonine phosphorylation has lead to advances in signal transduction research and cancer treatment. This feature summarizes research on mammalian proteins exhibiting histidine phosphorylation. Histidine kinases are well known in prokaryotic and lower eukaryotic systems where they form the 'two-component' signal transduction system. The relative invisibility of histidine phosphorylation in mammalian cells may result from technical obstacles such as its acid lability, which precludes detection in electrophoretic systems, amino acid sequencing, etc. Emerging data have identified mammalian histidine kinases for the kinase suppressor of ras, a scaffold molecule for the Map kinase pathway, as well as histone H4, aldolase C and the beta-subunit of heterotrimeric G proteins. Additional mammalian proteins of interest to signal transduction and cancer research exhibit histidine phosphorylation, including P-selectin, annexin I and the 20S proteasome. Other candidate histidine phosphorylated proteins are identified. These data suggest the existence of another series of phosphorylation patterns in signal transduction.
authors.affiliation: Women's Cancers Section, Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, Building 10, Room 2A33, Bethesda, MD 20892, USA. steegp@mail.nih.gov
authors.forename: Patricia S
authors.initials: PS
authors.lastname: Steeg
authors.forename: Diane
authors.initials: D
authors.lastname: Palmieri
authors.forename: Taoufik
authors.initials: T
authors.lastname: Ouatas
authors.forename: Massimiliano
authors.initials: M
authors.lastname: Salerno
mesh_terms: D000818:Animals; D017305:Annexin A1 / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D006639:Histidine / Q000378:metabolism*; D000071677:Histidine Kinase; D006801:Humans; D008954:Models, Biological; D008956:Models, Chemical; D020559:Monomeric GTP-Binding Proteins / Q000378:metabolism; D009097:Multienzyme Complexes / Q000378:metabolism; D054778:NM23 Nucleoside Diphosphate Kinases; D009362:Neoplasm Metastasis; D009369:Neoplasms / Q000378:metabolism*; D009701:Nucleoside-Diphosphate Kinase; D019007:P-Selectin / Q000378:metabolism; D010766:Phosphorylation; D046988:Proteasome Endopeptidase Complex; D011494:Protein Kinases / Q000502:physiology*; D015398:Signal Transduction; D014157:Transcription Factors / Q000378:metabolism
chemical_list: D017305:Annexin A1; D009097:Multienzyme Complexes; D054778:NM23 Nucleoside Diphosphate Kinases; D019007:P-Selectin; D014157:Transcription Factors; D006639:Histidine; D011494:Protein Kinases; D000071677:Histidine Kinase; D009701:Nucleoside-Diphosphate Kinase; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D019204:GTP-Binding Proteins; D020559:Monomeric GTP-Binding Proteins