Article

Phosphorylation-State Modulated Binding of HSP70: Structural Insights and Compensatory Protein Engineering

2025-02-17

Abstract excerpt

<h4>ABSTRACT</h4> Protein quality control is crucial for cellular homeostasis, involving the heat shock response, the ubiquitin-proteasome system, and the autophagy-lysosome pathway. Central to these systems are the chaperone homologs heat shock protein 70 (HSP70) and heat shock cognate 70 (HSC70), which manage protein folding and degradation. This study investigated the impact of the C-terminal phosphorylation o...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: af56dec9-9798-5220-a03c-375851c18a72
DOI: 10.1101/2025.02.17.637997

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation-State Modulated Binding of HSP70: Structural Insights and Compensatory Protein EngineeringDOI 10.1101/2025.02.17.637997Read

Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of “quasi-ordered” statesSemantic proximity Read

Dissecting the Cdc37 cochaperone code: Functional roles in chaperone-mediated stress adaptation.Semantic proximity Read

Hsp70 is phosphorylated in a conserved response to DNA damage and contributes to cell cycle controlSemantic proximity Read

Functional and structural analyses of UbcH5 mutants with enhanced binding to the E3 ubiquitin ligase CHIP.Semantic proximity Read

Activation mechanism of Small Heat Shock Protein HSPB5 revealed by disease-associated mutantsSemantic proximity Read

With or Without You: Co-chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein TriageSemantic proximity Read

Divergent condensates tune transcriptional responses during stressSemantic proximity Read

Domain-specific decoupling of co-chaperone and ligase functions in <i>STUB1</i> underlies biochemical and clinical heterogeneity in SCA48Semantic proximity Read

Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity.Semantic proximity Read

An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.Semantic proximity Read

Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation.Semantic proximity Read

Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Semantic proximity Read