It is now generally recognized that protein kinase signaling is involved in virtually every aspect of cell function, including growth and proliferation. The field of protein phosphorylation, including the enzymes involved in this post-translational modification, continues to advance at a fascinating pace.
Since the first international meeting on this topic, held in Heidelberg in 1994, several new avenues of CK2 research have emerged despite persistent deficiencies in our understanding of the regulation of its activity. Among the significant new directions are studies related to the structure of the enzyme, especially its crystal structure, as well as an interesting aspect of CK2 function that involves its subunits as binding partners of several other proteins. In addition, new data have been gathered on the role of CK2 in transcription as well as in certain other cellular functions. To address these various aspects of the progress of CK2, a number of key scientists from different parts of the world came together at the second international meeting on `A Molecular and Cellular View of Protein Kinase CK2', held at Villard de Lans near Grenoble on September 24-26, 1997. The meeting was attended by nearly 50 participants and included 28 presentations, which provide a view of the latest progress on protein kinase CK2.

Inhalt
CK2, a protein kinase of the next millennium.- A multifunctional network of basic residues confers unique properties to protein kinase CK2.- Intermolecular contact sites in protein kinase CK2.- Binding a polylysine to protein kinase CK2, measured by Surface Plasmon Resonance.- Functional analysis of CK2?-derived synthetic fragments.- Dissecting subdomains involved in multiple functions of the CK2? subunit.- Interactions of protein kinase CK2? subunit within the holoenzyme and with other proteins.- CK2? loci in the human genome: Structure and transcriptional activity.- Murine protein kinase CK2: Gene and oncogene.- Interactions of protein kinase CK2 subunits.- Mutations in the C-terminal domain of topoisomerase II affect meiotic function and interaction with the casein kinase 2? subunit.- Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/endoplasmin.- Searching interaction partners of protein kinase CK2? subunit by two-hybrid screening.- Protein kinase CK2 interacts with a multi-protein binding domain of p53.- BTF3 is a potential new substrate of protein kinase CK2.- Protein kinase CK2? may induce gene expression but unlikely acts directly as a DNA-binding transcription-activating factor.- Role of protein kinase CK2 in phosphorylation of nucleosomal proteins in relation to transcriptional activity.- A review of progress towards elucidating the role of protein kinase CK2 in polymerase III transcription : Regulation of the TATA binding protein.- The binding of the? subunit of protein kinase CK2 and RAP74 subunit of TFIIF to protein-coding genes in living cells is DRB sensitive.- Transcriptional regulation of the S. cerivisiae ENA1 gene by casein kinase II.- A role for casein kinase II phosphorylation in theregulation of IRF-1 transcriptional activity.- A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII.- Protein kinase CK2-dependent regulation of p53 function: Evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable.- Distribution of CK2, its substrate MAP1B and phosphatases in neuronal cells.- CK2? protein phosphatase 2A molecular complex: Possible interaction with the MAP kinase pathway.- Expression and regulation of protein kinase CK2 during the cell cycle.- Identification of proteins that associate with protein kinase CK2.- Multiple forms of protein kinase CK2 present in leukemic cells: In vitro study of its origin by proteolysis.- Index to Volume 191.