Literature DB >> 9427841

On the physiological role of casein kinase II in Saccharomyces cerevisiae.

C V Glover1.   

Abstract

Casein kinase II (CKII) is a highly conserved serine/threonine protein kinase that is ubiquitous in eukaryotic organisms. This review summarizes available data on CKII of the budding yeast Saccharomyces cerevisiae, with a view toward defining the possible physiological role of the enzyme. Saccharomyces cerevisiae CKII is composed of two catalytic and two regulatory subunits encoded by the CKA1, CKA2, CKB1, and CKB2 genes, respectively. Analysis of null and conditional alleles of these genes identifies a requirement for CKII in at least four biological processes: flocculation (which may reflect an effect on gene expression), cell cycle progression, cell polarity, and ion homeostasis. Consistent with this, isolation of multicopy suppressors of conditional cka mutations has identified three genes that have a known or potential role in either the cell cycle or cell polarity: CDC37, which is required for cell cycle progression in both G1 and G2/M; ZDS1 and 2, which appear to have a function in cell polarity; and SUN2, which encodes a protein of the regulatory component of the 26S protease. The identity and properties of known CKII substrates in S. cerevisiae are also reviewed, and advantage is taken of the complete genomic sequence to predict globally the substrates of CKII in this organism. Although the combined data do not yield a definitive picture of the physiological role of CKII, it is proposed that CKII serves a signal transduction function in sensing and/or communicating information about the ionic status of the cell to the cell cycle machinery.

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Year:  1998        PMID: 9427841     DOI: 10.1016/s0079-6603(08)61030-2

Source DB:  PubMed          Journal:  Prog Nucleic Acid Res Mol Biol        ISSN: 0079-6603


  62 in total

1.  Protein kinase CK2alpha may induce gene expression but unlikely acts directly as a DNA-binding transcription-activating factor.

Authors:  K Ackermann; W Pyerin
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

2.  Intermolecular contact sites in protein kinase CK2.

Authors:  A Krehan; W Pyerin
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

3.  Transcriptional coordination of the genes encoding catalytic (CK2alpha) and regulatory (CK2beta) subunits of human protein kinase CK2.

Authors:  W Pyerin; K Ackermann
Journal:  Mol Cell Biochem       Date:  2001-11       Impact factor: 3.396

4.  Assembly of protein kinase CK2: investigation of complex formation between catalytic and regulatory subunits using a zinc-finger-deficient mutant of CK2beta.

Authors:  D A Canton; C Zhang; D W Litchfield
Journal:  Biochem J       Date:  2001-08-15       Impact factor: 3.857

5.  Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes.

Authors:  Bodo M H Lange; Elena Rebollo; Andrea Herold; Cayetano González
Journal:  EMBO J       Date:  2002-10-15       Impact factor: 11.598

6.  Isolation of a CK2α subunit and the holoenzyme from the mussel Mytilus galloprovincialis and construction of the CK2α and CK2β cDNAs.

Authors:  Regina-Maria Kolaiti; Andrea Baier; Ryszard Szyszka; Sophia Kouyanou-Koutsoukou
Journal:  Mar Biotechnol (NY)       Date:  2010-10-05       Impact factor: 3.619

Review 7.  Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae.

Authors:  George M Carman; Gil-Soo Han
Journal:  Annu Rev Biochem       Date:  2011       Impact factor: 23.643

Review 8.  Protein kinase CK2: structure, regulation and role in cellular decisions of life and death.

Authors:  David W Litchfield
Journal:  Biochem J       Date:  2003-01-01       Impact factor: 3.857

9.  High-resolution yeast phenomics resolves different physiological features in the saline response.

Authors:  Jonas Warringer; Elke Ericson; Luciano Fernandez; Olle Nerman; Anders Blomberg
Journal:  Proc Natl Acad Sci U S A       Date:  2003-12-15       Impact factor: 11.205

10.  CK2 is responsible for phosphorylation of human La protein serine-366 and can modulate rpL37 5'-terminal oligopyrimidine mRNA metabolism.

Authors:  Elena I Schwartz; Robert V Intine; Richard J Maraia
Journal:  Mol Cell Biol       Date:  2004-11       Impact factor: 4.272

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