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.
Highlights
Heterochromatin is tightly packed DNA which is usually transcriptionally inactive
We focus on how Heterochromatin Protein 1 (HP1) post-translational modifications (PTMs) influence its function and ability to bind and modify chromatin
We summarize the latest literature on how the passage through mitosis influences the heterochromatin landscape and affects HP1 binding to chromatin, at the pericentromeric chromatin
Summary
Heterochromatin is tightly packed DNA which is usually transcriptionally inactive. It is established in early development through controlled epigenetic processes [1] that need to be maintained from mother to daughter cells to ensure proper genome function. Heterochromatin is characterized by the presence of specific epigenetic marks that are important for its establishment, maintenance and regulation. How HP1 interacts with chromatin and other HP1 molecules has recently been reviewed [7]. We focus on how HP1 post-translational modifications (PTMs) influence its function and ability to bind and modify chromatin. We summarize the latest literature on how the passage through mitosis influences the heterochromatin landscape and affects HP1 binding to chromatin, at the pericentromeric chromatin
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