A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle

Levin, David E.; Fields, F.Owen; Kunisawa, Riyo; Bishop, J. Michael; Thorner, Jeremy

doi:10.1016/0092-8674(90)90360-q

Cited by 418 publications

(348 citation statements)

References 73 publications

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“…At the moment it is still unclear whether this class of proteins is actually involved in regulation of neurotransmitter synthesis or protein kinase C function in vivo. Recently, a gene was identified in S, ~e~ev~s~u~ coding for a protein which is very similar to the mammalian protein kinases C [24]. In addition, protein kinasc C activity was detected in yeast homogenates 1251.…”

Section: Discussionmentioning

confidence: 99%

Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors

et al. 1992

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We describe the identification and characterization of the BMH1 gene from the yeast Saccharomyces cerevisiae. The gene encodes a putative protein of 292 amino acids which is more than 50% identical with the bovine brain 14‐3‐3 protein and proteins isolated from sheep brain which are strong inhibitors of protein kinase C. Disruption mutants and strains with the BMH1 gene on multicopy plasmids have impaired growth on minimal medium with glucose as carbon source, i.e. a 30–50% increase in generation time. These observations suggest a regulatory function of the bmh1 protein. In contrast to strains with an intact or a disrupted BMH1 gene, strains with the BMH1 gene on multicopy plasmids hardly grew on media with acetate or glycerol as carbon source.

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Section: Discussionmentioning

confidence: 99%

Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors

et al. 1992

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“…However, based on several observations Martini et al [82] placed PKCl downstream of Cdc28; Cdc28 activation can partially rescue a pkcl" allele, while PKCl overexpression has no effect on cdc28" alleles. Furthermore, PKCI-defective cells arrest growth at a point following bud emergence with completely replicated chromosomal DNA [85]. This G2-like arrest suggests that PKCl function is downstream of START and Cdc28 activation.…”

Section: Lessons From Yeast Cellsmentioning

confidence: 99%

Linking Protein Kinase C to Cell‐Cycle Control

Livneh

Fishman

1997

European Journal of Biochemistry

199

114

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Protein kinase C (PKC) isoenzymes are involved in diverse cellular functions, including differentiation, growth control, tumor promotion, and cell death. In recent years, evidence has began to emerge suggesting a role for PKC in cell cycle control. A paper published recently, demonstrating a functional link between PKC and cell cycle control in yeast (Marini, N. J., Meldrum, E., Buehrer, B., Hubberstey, A. V., Stone, D. E., Traynor-Kaplan, A. & Reed, S. I. (1996) EMBO J. 15, 3040-3052), strengthens this data. Thus, the existence of cell-cycle-regulated pathways involving PKC in both yeast and mammals indicate that PKC may be a conserved regulator of cell cycle events that links signal transduction pathways and the cell-cycle machinery. In this paper, we will review current data on the cell cycle components that are targets for PKC regulation.PKC enzymes appear to operate as regulators of the cell cycle at two sites, during G1 progression and G 2 M transition. In G1, the overall effect of PKC activation is inhibition of the cell cycle at mid to late G1. This cell cycle inhibition correlates with a blockage in the normal phosphorylation of the tumor suppressor retinoblastoma Rb protein, presumably through an indirect mechanism. The reduced activity of the cyclin-dependent kinase, Cdk2, appears to be the major effect of PKC activation in various cell systems. This may also underlie the inhibition of Rb phosphorylation exhibited by PKC activation. Several mechanisms were described in different studieq on the regulation of Cdk2 activity by PKC; reduced Cdk-activating kinase activity, diminished expression of the Cdk2 partners cyclins E or A, and the increased expression of the cyclin-dependent inhibitors, p2lWAF1 and p27K'P', which are capable of binding to cyclidCdk2 complexes.PKC enzymes were also shown to play a role in G2/M transition. Among the suggested mechanisms is suppression of Cdc2 activity. However, most of the published data strongly implicate PKC in lamin B phosphorylation and nuclear envelope disassembly.Keywords: protein kinase C ; cell cycle; cyclin ; cyclin-dependent kinase; Cdk inhibitor; retinoblastoma protein; p53 protein; phorbol ester; GUS transition; G2/M transition. Protein kinase C and growth regulationThe term protein kinase C (PKC) stands for a group of at least ten serinehhreonine kinases that are characterized by a high degree of similarity in their catalytic kinase domains and cysteine-rich regions [l-41. The PKC family is subdivided into three groups; the classical PKC members (a, p, y) are Ca2+ and diacylglycerol-dependent, the novel PKCs (6, E , q and d) are Ca2+-independent but diacylglycerol-dependent and the atypical PKCs ([ and 2) are not activated by Ca*+ and diacylglycerol in vitro [3, 41. This may account for the multiplicity and diversity of the cellular activities implicated to be mediated by PKC, sinceCorrespondence to

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“…Because CK1 is always isolated as a constitutively active enzyme (Tuazon and Traugh, 1991) and because its substrate selectivity requirements are still under investigation, it is unclear whether CK1 is regulated by a "pseudosubstrate" or "autoinhibitory" domain (Soderling, 1990) or where such a domain would exist in the primary structure we report here. With its short length and divergent amino acid sequence, the amino-terminal portion of CKI1 and CK12 is unlikely to serve a regulatory function analogous to the aminoterminal regions of the cGMP-dependent protein kinase (Takio et al, 1984) or protein kinase C (Levin et al, 1990). Alternatively, if regulation of CK1 activity occurs, it may be through posttranslational modification, through association with other polypeptides (e.g., a regulatory subunit), or through limitation of its access to physiological substrates by changes in its subcellular distribution.…”

Section: Discussionmentioning

confidence: 99%

“…Apparently, detergent extraction coupled with partial proteolysis during purification can produce a soluble 54-kDa fragment with protein kinase activity (because digestion of this protein with trypsin generated peptide T2 from peptide Ti and because Ti is present only in CKIi, the 54-kDa prep-B C 1 2 3 a b c d Figure 5. Levin et al, 1990). The deduced primary structure of the 37-kDa form of mammalian CK1 lacks carboxy-terminal cysteine residues and is probably not associated with membranes (Rowles et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

Two genes in Saccharomyces cerevisiae encode a membrane-bound form of casein kinase-1.

Wang

Vančura

Mitcheson

et al. 1992

MBoC

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Two cDNAs encoding casein kinase-1 have been isolated from a yeast cDNA library and termed CKI1 and CKI2. Each clone encodes a protein of approximately 62,000 Da containing a highly conserved protein kinase domain surrounded by variable amino- and carboxy-terminal domains. The proteins also contain two conserved carboxy-terminal cysteine residues that comprise a consensus sequence for prenylation. Consistent with this posttranslational modification, cell fractionation experiments demonstrate that intact CKI1 is found exclusively in yeast cell membranes. Gene disruption experiments reveal that, although neither of the two CKI genes is essential by itself, at least one CKI gene is required for yeast cell viability. Spores deficient in both CKI1 and CKI2 fail to grow and, therefore, either fail to germinate or arrest as small cells before bud emergence. These results suggest that casein kinase-1, which is distributed widely in nature, plays a pivotal role in eukaryotic cell regulation.

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A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle

Cited by 418 publications

References 73 publications

Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors

Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors

Linking Protein Kinase C to Cell‐Cycle Control

Two genes in Saccharomyces cerevisiae encode a membrane-bound form of casein kinase-1.

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