Tissue Specificity of Histone Phosphorylation

Gutierrez, Rose Mary; Hnilica, Lubomir S.

doi:10.1126/science.157.3794.1324

Cited by 77 publications

(43 citation statements)

References 15 publications

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“…Since histone H3 phosphorylation was first observed in the 1960s, 3 extensive studies were conducted in many organisms, however, its functions are yet to be resolved. At present, most investigations on phH3/ser10 functions are concentrated on its relation to chromosome condensation, and this issue has been debated continuously (see Introduction).…”

Section: Discussionmentioning

confidence: 99%

Histone Phosphorylation and Pericentromeric Histone Modifications in Oocyte Meiosis

Wang

Wang²,

Ai³

et al. 2006

Cell Cycle

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Epigenetic regulation of pericentromeric heterochromatin is crucial for proper interactions between kinetochores and spindle microtubules governing accurate chromosome segregation. Here, we first examined the dynamic distribution of phosphorylated serine 10 and 28 on H3 during mouse oocyte maturation and early embryo development using immunofluorescent staining and confocal microscopy. Our results revealed strong signals of phosphorylated H3/ser10 and 28 in the pericentromeric heterochromatin area and continuous persistent staining of the chromosome periphery, respectively. A panel of specific antibodies against various acetylated lysine, dimethylated lysine or phosphorylated serine residues on histone H3 or H4 were used to investigate the effects of Trichostatin A (TSA), a general inhibitor of histone deacetylases (HDACs), on histone modifications of pericentromeric heterochromatin. Unexpectedly, TSA treatment was unable to alter the acetylation and methylation status of pericentromeric heterochromatin, however, it resulted in significant dephosphorylation of H3/ser10 at this site during mouse oocyte meiosis, which is likely to play a role in the TSA-induced defective chromosome segregation. Furthermore, by using ZM447439, an inhibitor of Aurora kinases, we revealed that Aurora kinases may participate in the regulation of histone phosphorylation during mouse oocyte maturation.

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Section: Discussionmentioning

confidence: 99%

Histone Phosphorylation and Pericentromeric Histone Modifications in Oocyte Meiosis

Wang

Wang²,

Ai³

et al. 2006

Cell Cycle

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“…Except for methylation modification of DNA, there are diverse forms of modifications at the histone amino termini, including acetylation, phosphorylation, methylation, ADPribosylation, ubiquitination, sumoylation, biotinylation and proline isomerization [19][20][21][22][23][24][25]. It has been well documented that these histone modifications play important roles in cell cycle progression, DNA replication and repair, transcriptional activity and chromosome stability [26][27][28].…”

Section: Special Topicmentioning

confidence: 99%

Epigenetic changes associated with oocyte aging

Liang

Schatten

et al. 2012

Sci. China Life Sci.

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It is well established that the decline in female reproductive outcomes is related to postovulatory aging of oocytes and advanced maternal age. Poor oocyte quality is correlated with compromised genetic integrity and epigenetic changes during the oocyte aging process. Here, we review the epigenetic alterations, mainly focused on DNA methylation, histone acetylation and methylation associated with postovulatory oocyte aging as well as advanced maternal age. Furthermore, we address the underlying epigenetic mechanisms that contribute to the decline in oocyte quality during oocyte aging.

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“…Despite its longstanding history (Stevely and Stocken, 1966;Gutierrez and Hnilica, 1967) and the presence of numerous serine, threonine, and tyrosine residues speckled throughout the primary sequences of histone proteins. Early work in this area focused primarily on the phosphorylation of linker histones (eg, H1, Sweet and Allis, 1993) and of the core histone H3 (eg, H3S10 phosphorylation (H3S10p)) as universal markers of mitotic and meiotic chromatin condensation (Wei et al, 1998(Wei et al, , 1999.…”

Section: Histone Phosphorylation and Cross Talk Interactions In The Cnsmentioning

confidence: 99%

Histone Regulation in the CNS: Basic Principles of Epigenetic Plasticity

Maze

Noh

Allis

2012

Neuropsychopharmacol

115

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Postmitotic neurons are subject to a vast array of environmental influences that require the nuclear integration of intracellular signaling events to promote a wide variety of neuroplastic states associated with synaptic function, circuit formation, and behavioral memory. Over the last decade, much attention has been paid to the roles of transcription and chromatin regulation in guiding fundamental aspects of neuronal function. A great deal of this work has centered on neurodevelopmental and adulthood plasticity, with increased focus in the areas of neuropharmacology and molecular psychiatry. Here, we attempt to provide a broad overview of chromatin regulation, as it relates to central nervous system (CNS) function, with specific emphasis on the modes of histone posttranslational modifications, chromatin remodeling, and histone variant exchange. Understanding the functions of chromatin in the context of the CNS will aid in the future development of pharmacological therapeutics aimed at alleviating devastating neurological disorders.

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Tissue Specificity of Histone Phosphorylation

Cited by 77 publications

References 15 publications

Histone Phosphorylation and Pericentromeric Histone Modifications in Oocyte Meiosis

Histone Phosphorylation and Pericentromeric Histone Modifications in Oocyte Meiosis

Epigenetic changes associated with oocyte aging

Histone Regulation in the CNS: Basic Principles of Epigenetic Plasticity

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