ArticleMolecular and cellular biology2001
The hinge and chromo shadow domain impart distinct targeting of HP1-like proteins.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.
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Who cites it
95 citing papers in PubMed, 175 citations in OpenAlex.
- Microcephaly-associated genes asp and Sas4 influence chromatin organization and nuclear lamina structure in Drosophila melanogaster.Development (Cambridge, England) · 2026Article
- HP1β and H3K9me3 Regulate Olfactory Receptor Choice and Transcriptional Identity.International journal of molecular sciences · 2026Article
- In vitro reconstitution of heterochromatin compartments reveals the spontaneous formation of tunable liquid-liquid interfaces.Nucleic acids research · 2026Article
- HP1γ self-assembles and cooperates with KAP1 in repression of long noncoding RNA AI662270 in ESCs.Cell reports · 2026Article
- Protein language model identifies disordered, conserved motifs implicated in phase separation.eLife · 2025Article
- HP1a promotes chromatin liquidity and drives spontaneous heterochromatin compartmentalization.bioRxiv : the preprint server for biology · 2025Article
- Structural mechanism of HP1⍺-dependent transcriptional repression and chromatin compaction.Structure (London, England : 1993) · 2024Article
- Tracking live-cell single-molecule dynamics enables measurements of heterochromatin-associated protein-protein interactions.Nucleic acids research · 2024Article
- The therapeutic implications of all-in-one AAV-delivered epigenome-editing platform in neurodegenerative disorders.Nature communications · 2024Article
- Conformational diversity of human HP1α.Protein science : a publication of the Protein Society · 2024Article
- Heterochromatic 3D genome organization is directed by HP1a- and H3K9-dependent and independent mechanisms.Molecular cell · 2024Article
- Characterization of Hepatoma-Derived Growth Factor-Related Protein 2 Interactions with Heterochromatin.Cells · 2023Article
- HP1 proteins regulate nucleolar structure and function by secluding pericentromeric constitutive heterochromatin.Nucleic acids research · 2023Article
- Engineering inducible biomolecular assemblies for genome imaging and manipulation in living cells.Nature communications · 2022Article
- Article
- HP1 oligomerization compensates for low-affinity H3K9me recognition and provides a tunable mechanism for heterochromatin-specific localization.Science advances · 2022Article
- Functions of HP1 proteins in transcriptional regulation.Epigenetics & chromatin · 2022Review
- The Sound of Silence: How Silenced Chromatin Orchestrates the Repair of Double-Strand Breaks.Genes · 2021Review
- Review
- The Drosophila HP1 family is associated with active gene expression across chromatin contexts.Genetics · 2021Article
35 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Drosophila heterochromatin-associated protein 1 (HP1) is an abundant component of heterochromatin, a highly condensed compartment of the nucleus that comprises a major fraction of complex genomes. Some organisms have been shown to harbor multiple HP1-like proteins, each exhibiting spatially distinct localization patterns within interphase nuclei. We have characterized the subnuclear localization patterns of two newly discovered Drosophila HP1-like proteins (HP1b and HP1c), comparing them with that of the originally described fly HP1 protein (here designated HP1a). While HP1a targets heterochromatin, HP1b localizes to both heterochromatin and euchromatin and HP1c is restricted exclusively to euchromatin. All HP1-like proteins contain an amino-terminal chromo domain, a connecting hinge, and a carboxyl-terminal chromo shadow domain. We expressed truncated and chimeric HP1 proteins in vivo to determine which of these segments might be responsible for heterochromatin-specific and euchromatin-specific localization. Both the HP1a hinge and chromo shadow domain independently target heterochromatin, while the HP1c chromo shadow domain is implicated solely in euchromatin localization. Comparative sequence analyses of HP1 homologs reveal a conserved sequence block within the hinge that contains an invariant sequence (KRK) and a nuclear localization motif. This block is not conserved in the HP1c hinge, possibly accounting for its failure to function as an independent targeting segment. We conclude that sequence variations within the hinge and shadow account for HP1 targeting distinctions. We propose that these targeting features allow different HP1 complexes to be distinctly sequestered in organisms that harbor multiple HP1-like proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.