ArticleExperimental cell research2007
Recruitment of phosphorylated small heat shock protein Hsp27 to nuclear speckles without stress.
Article in Experimental cell research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.
- A comparative meta-analysis of membraneless organelle-associated proteins with age related proteome of C. elegans.Cell stress & chaperones · 2022Pooled it
- Centrosome linker protein CEP68 modulates cellular stress responses via nuclear condensate formation and HSP27 interaction.iScience · 2026Article
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- GPATCH11 variants cause mis-splicing and early-onset retinal dystrophy with neurological impairment.Nature communications · 2024Article
- Decoding the temporal nature of brain GR activity in the NFκB signal transition leading to depressive-like behavior.Molecular psychiatry · 2021Article
- Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease.Frontiers in pharmacology · 2019Review
- Aberrant Compartment Formation by HSPB2 Mislocalizes Lamin A and Compromises Nuclear Integrity and Function.Cell reports · 2017Article
- Conservative Mechanisms of Extracellular Trap Formation by Annelida Eisenia andrei: Serine Protease Activity Requirement.PloS one · 2016Article
- Small heat-shock proteins: important players in regulating cellular proteostasis.Cellular and molecular life sciences : CMLS · 2015Review
- Identification of peptides in human Hsp20 and Hsp27 that possess molecular chaperone and anti-apoptotic activities.The Biochemical journal · 2015Article
- Heat shock response associated with hepatocarcinogenesis in a murine model of hereditary tyrosinemia type I.Cancers · 2014Article
- Pseudophosphorylated αB-crystallin is a nuclear chaperone imported into the nucleus with help of the SMN complex.PloS one · 2013Article
- Phosphorylation-dependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in cultured hippocampal neurons.Histochemistry and cell biology · 2012Article
- Heat shock-induced SRSF10 dephosphorylation displays thermotolerance mediated by Hsp27.Molecular and cellular biology · 2011Article
- Article
- Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Progress in neurobiology · 2010Review
- Abnormal interaction of motor neuropathy-associated mutant HspB8 (Hsp22) forms with the RNA helicase Ddx20 (gemin3).Cell stress & chaperones · 2010Article
- Accumulation of oxidized proteins in Herpesvirus infected cells.Free radical biology & medicine · 2010Article
- Inhibition of protein phosphorylation in MIA pancreatic cancer cells: confluence of metabolic and signaling pathways.Journal of proteome research · 2010Article
- Hsp27 associates with the titin filament system in heat-shocked zebrafish cardiomyocytes.Experimental cell research · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
During stress, the mammalian small heat shock protein Hsp27 enters cell nuclei. The present study examines the requirements for entry of Hsp27 into nuclei of normal rat kidney (NRK) renal epithelial cells, and for its interactions with specific nuclear structures. We find that phosphorylation of Hsp27 is necessary for the efficient entry into nuclei during heat shock but not sufficient for efficient nuclear entry under control conditions. We further report that Hsp27 is recruited to an RNAse sensitive fraction of SC35 positive nuclear speckles, but not other intranuclear structures, in response to heat shock. Intriguingly, Hsp27 phosphorylation, in the absence of stress, is sufficient for recruitment to speckles found in post-anaphase stage mitotic cells. Additionally, pseudophosphorylated Hsp27 fused to a nuclear localization peptide (NLS) is recruited to nuclear speckles in unstressed interphase cells, but wildtype and nonphosphorylatable Hsp27 NLS fusion proteins are not. The expression of NLS-Hsp27 mutants does not enhance colony forming abilities of cells subjected to severe heat shock, but does regulate nuclear speckle morphology. These data demonstrate that phosphorylation, but not stress, mediates Hsp27 recruitment to an RNAse soluble fraction of nuclear speckles and support a site-specific role for Hsp27 within the nucleus.
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