Phosphorylation of Heterochromatin Protein 1 by Casein Kinase II Is Required for Efficient Heterochromatin Binding inDrosophila
Tao Zhao,Joel C. Eissenberg +1 more
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TLDR
It is reported here that HP1 is phosphorylated by casein kinase II in vivo at three serine residues located at the N and C termini of the protein.About:
This article is published in Journal of Biological Chemistry.The article was published on 1999-05-21 and is currently open access. It has received 78 citations till now. The article focuses on the topics: Heterochromatin assembly & Heterochromatin protein 1.read more
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Journal ArticleDOI
The HP1 protein family: getting a grip on chromatin.
TL;DR: A number of intriguing interactions between HP1 and other proteins have been described, implicating HP1 in gene regulation, DNA replication, and nuclear architecture.
Journal ArticleDOI
HP1-β mobilization promotes chromatin changes that initiate the DNA damage response
TL;DR: An unrecognized signalling cascade that helps to initiate the DNA damage response is revealed, altering chromatin by modifying a histone-code mediator protein, HP1, but not the code itself.
Journal ArticleDOI
The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer
Sally V. Brasher,Brian O. Smith,Rasmus H. Fogh,Daniel Nietlispach,Abarna Thiru,Peter R. Nielsen,R. William Broadhurst,Linda J. Ball,Natalia V. Murzina,Ernest D. Laue +9 more
TL;DR: Results suggest that chromo domains may function as protein interaction motifs, bringing together different proteins in multi‐protein complexes and locating them in heterochromatin.
Journal ArticleDOI
Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin.
Abarna Thiru,Daniel Nietlispach,Helen R. Mott,Mitsuru Okuwaki,Debbie Lyon,Peter R. Nielsen,Miriam Hirshberg,Alain Verreault,Natalia V. Murzina,Ernest D. Laue +9 more
TL;DR: It is shown that targeting of HP1β to heterochromatin requires shadow domain interactions with PXVXL‐containing proteins in addition to chromo domain recognition of Lys‐9‐methylated histone H3, and this finding implies a further complexity to the histone code for regulation of chromatin structure and suggests how binding ofHP1 family proteins may lead to its condensation.
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Molecular Determinants for Targeting Heterochromatin Protein 1-Mediated Gene Silencing: Direct Chromoshadow Domain–KAP-1 Corepressor Interaction Is Essential
TL;DR: It is shown that the chromoshadow domain (CSD) of HP1 is a potent repression domain that binds directly to all four previously described proteins and is a physiologically relevant target for HP1 function.
References
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