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1.
EMBO Rep ; 22(11): e52061, 2021 11 04.
Article in English | MEDLINE | ID: mdl-34423893

ABSTRACT

H2A.Z is a H2A-type histone variant essential for many aspects of cell biology, ranging from gene expression to genome stability. From deuterostomes, H2A.Z evolved into two paralogues, H2A.Z.1 and H2A.Z.2, that differ by only three amino acids and are encoded by different genes (H2AFZ and H2AFV, respectively). Despite the importance of this histone variant in development and cellular homeostasis, very little is known about the individual functions of each paralogue in mammals. Here, we have investigated the distinct roles of the two paralogues in cell cycle regulation and unveiled non-redundant functions for H2A.Z.1 and H2A.Z.2 in cell division. Our findings show that H2A.Z.1 regulates the expression of cell cycle genes such as Myc and Ki-67 and its depletion leads to a G1 arrest and cellular senescence. On the contrary, H2A.Z.2, in a transcription-independent manner, is essential for centromere integrity and sister chromatid cohesion regulation, thus playing a key role in chromosome segregation.


Subject(s)
Chromosome Segregation , Histones , Animals , Centromere/metabolism , Genomic Instability , Histones/genetics , Histones/metabolism
2.
Cells ; 9(6)2020 06 12.
Article in English | MEDLINE | ID: mdl-32545538

ABSTRACT

Heterochromatin Protein 1 (HP1) is a highly conserved protein that has been used as a classic marker for heterochromatin. HP1 binds to di- and tri-methylated histone H3K9 and regulates heterochromatin formation, functions and structure. Besides the well-established phosphorylation of histone H3 Ser10 that has been shown to modulate HP1 binding to chromatin, several studies have recently highlighted the importance of HP1 post-translational modifications and additional epigenetic features for the modulation of HP1-chromatin binding ability and heterochromatin formation. In this review, we summarize the recent literature of HP1 post-translational modifications that have contributed to understand how heterochromatin is formed, regulated and maintained.


Subject(s)
Chromosomal Proteins, Non-Histone/metabolism , Heterochromatin/metabolism , Protein Processing, Post-Translational/physiology , Chromatin/metabolism , Chromobox Protein Homolog 5 , Chromosomal Proteins, Non-Histone/genetics , Histones/metabolism , Humans
3.
Trends Biochem Sci ; 43(10): 747-748, 2018 10.
Article in English | MEDLINE | ID: mdl-30131191

ABSTRACT

Nuclear antigen Ki-67 is widely accepted as a cell proliferation marker in both research and cancer diagnostic settings. Despite its extensive use and clinical value, very little is still known about the biological function of Ki-67. A recent work published in Cell Reports has revealed important novel aspects of Ki-67 regulation that could provide new and extended prognostic and therapeutic value.


Subject(s)
Cell Proliferation , Ki-67 Antigen , Prognosis
4.
Biochem Soc Trans ; 46(1): 173-182, 2018 02 19.
Article in English | MEDLINE | ID: mdl-29432143

ABSTRACT

The nuclear envelope (NE) is a unique topological structure formed by lipid membranes (Inner and Outer Membrane: IM and OM) interrupted by open channels (Nuclear Pore complexes). Besides its well-established structural role in providing a physical separation between the genome and the cytoplasm and regulating the exchanges between the two cellular compartments, it has become quite evident in recent years that the NE also represents a hub for localized signal transduction. Mechanical, stress, or mitogen signals reach the nucleus and trigger the activation of several pathways, many effectors of which are processed at the NE. Therefore, the concept of the NE acting just as a barrier needs to be expanded to embrace all the dynamic processes that are indeed associated with it. In this context, dynamic protein association and turnover coupled to reversible post-translational modifications of NE components can provide important clues on how this integrated cellular machinery functions as a whole. Reversible protein phosphorylation is the most used mechanism to control protein dynamics and association in cells. Keys to the reversibility of the system are protein phosphatases and the regulation of their activity in space and time. As the NE is clearly becoming an interesting compartment for the control and transduction of several signalling pathways, in this review we will focus on the role of Protein Phosphatases at the NE since the significance of this class of proteins in this context has been little explored.


Subject(s)
Nuclear Envelope/enzymology , Phosphoprotein Phosphatases/metabolism , Cell Nucleus/metabolism , Cytoplasm/metabolism , Humans , Phosphorylation , Protein Processing, Post-Translational , Signal Transduction
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