Control of Cell Division by Very Lysine Rich Histone (F1) Phosphorylation

Bradbury, E. Morton; Inglis, R. J.; Matthews, Harry R.

doi:10.1038/247257a0

Cited by 427 publications

(109 citation statements)

References 39 publications

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“…The cell cycle kinases cdc2+/CDC28 are also Ca z+-and cyclic nucleotideindependent (Bradbury et al, 1974). Addition of MnC12 to the assay inhibited kinase activity.…”

Section: Discussionmentioning

confidence: 99%

The pk-1 Gene of Autographa Californica Multinucleocapsid Nuclear Polyhedrosis Virus Encodes a Protein Kinase

Reilly

Guarino

1994

Journal of General Virology

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Open reading frame (ORF) 9 of the EcoRI I fragment of the baculovirus Autographa californica multinucleocapsid nuclear polyhedrosis virus (AcMNPV) genome encodes a protein, PK-1, which has strong similarity to serine-threonine protein kinases. The published sequence of the pk-1 gene contains an error that, when corrected, extends the ORF by 228 nucleotides. Transcription of pk-1 was first detectable by primer extension at 12 h post-infection, accumulating to high levels during the very late phase of infection. PK-1 produced in rabbit reticulocyte lysates was able to phosphorylate histone H1. Together, our results suggest that ORF 9 encodes a protein kinase that is expressed during the beginning of the late and throughout the very late phases of AcMNPV infection.

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“…The cell cycle kinases cdc2+/CDC28 are also Ca z+-and cyclic nucleotideindependent (Bradbury et al, 1974). Addition of MnC12 to the assay inhibited kinase activity.…”

Section: Discussionmentioning

confidence: 99%

The pk-1 Gene of Autographa Californica Multinucleocapsid Nuclear Polyhedrosis Virus Encodes a Protein Kinase

Reilly

Guarino

1994

Journal of General Virology

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“…The linker histone H1 is also known to be phosphorylated, especially during mitosis [24,25]. Thus, we investigated the possibility that H1 phosphorylation could be altered upon cAMP treatment.…”

Section: Hplc Analysis Of Histone Phosphorylation In Metabolically-lamentioning

confidence: 99%

cAMP signaling induces rapid loss of histone H3 phosphorylation in mammary adenocarcinoma-derived cell lines

Rodriguez-Collazo

Snyder

Chiffer

et al. 2008

Experimental Cell Research

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The phosphorylation of histone H3 is known to play a role in regulation of transcription as well as preparation of chromosomes for mitosis. Various signaling cascades induce H3 phosphorylation, particularly at genes activated by these pathways. In this study we show that signaling can also have the opposite effect. Activators of cAMP signaling induce a rapid and potent loss of H3 phosphorylation. This effect is not mediated through a cAMP metabolite since a membranepermeable form of AMP had no effect on H3 phosphorylation and a phosphodiesterase-resistant cAMP analog efficiently reduced it. cAMP is also the likely regulator of H3 phosphorylation under physiological conditions since only supra-pharmacological doses of cGMP induce the loss of H3 phosphorylation. The loss of phosphorylation is specific for histone H3 since we do not observe drastic losses in total phosphorylation of other histones. In addition, other H3 modifications are unaffected with the exception of lysine 9 methylation, which is elevated. Analysis of cell growth and cell cycle show that cAMP signaling inhibits cell growth and arrests cells at both G1 and G2/M. Similar effects of cAMP signaling on H3 phosphorylation are observed in a variety of mammary adenocarcinoma-derived cell lines. In syngeneic human breast derived cell lines, one diploid and non-transformed, the other derived from a ductal carcinoma, the loss of H3 phosphorylation is significantly more sensitive to cAMP concentration in the transformed cell line.

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“…MPF has been purified from Xenopus and starfish oocytes and has been shown to contain, as an essential component, the Cdc2/Cdc28 protein kinase {Gautier Lohka et al 1988;Labbe et al 1989a). It also appears that an activity known as growth-associated histone H1 kinase, which is present during mitosis in a number of organisms (Bradbury et al 1974;Chambers et al 1983), contains the Cdc2/Cdc28 protein and is likely to be identical to MPF (Arion et al 1988;Labbe et al 1988Labbe et al , 1989aBrizuela et al 1989;Langan et al 1989}.…”

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confidence: 99%

Human cDNAs encoding homologs of the small p34Cdc28/Cdc2-associated protein of Saccharomyces cerevisiae and Schizosaccharomyces pombe.

Richardson¹,

Stueland²,

Thomas³

et al. 1990

Genes Dev.

181

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The Cksl protein is a component of the Cdc28 protein kinase in the budding yeast Saccharomyces cererisiae. This paper reports the cloning of two homologs of the S. cererisiae CKS1 gene from human cells. These homologs, CKShsl and CKShs2, both encode proteins of 79 amino acids that share considerable homology at the amino acid level with the products of CKS1 from S. cererisiae and sucl + from the fission yeast Schizosaccharomyces pombe. Both human homologs are capable of rescuing a null mutation of the S. cererisiae CKS1 gene when expressed from the S. cererisiae GALl promoter. S. pombe sucl + expressed from the GALl promoter is also capable of rescuing a S. cererisiae cksl null mutation. Ckshsl or Ckshs2 protein linked to Sepharose beads can bind the Cdc28/Cdc2 protein kinase from both S. cererisiae and human cells. The CKShsl and CKShs2 mRNAs are expressed in different patterns through the cell cycle in HeLa cells, which may reflect specialized roles for the encoded proteins.

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Control of Cell Division by Very Lysine Rich Histone (F1) Phosphorylation

Cited by 427 publications

References 39 publications

The pk-1 Gene of Autographa Californica Multinucleocapsid Nuclear Polyhedrosis Virus Encodes a Protein Kinase

The pk-1 Gene of Autographa Californica Multinucleocapsid Nuclear Polyhedrosis Virus Encodes a Protein Kinase

cAMP signaling induces rapid loss of histone H3 phosphorylation in mammary adenocarcinoma-derived cell lines

Human cDNAs encoding homologs of the small p34Cdc28/Cdc2-associated protein of Saccharomyces cerevisiae and Schizosaccharomyces pombe.

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