HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.

Autophagy

CNRS; Institut de Biologie Moléculaire et Cellulaire; Immunopathologie et Chimie Thérapeutique/Laboratory of Excellence Medalis; Strasbourg, France.

Published: December 2013


Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively expressed, cognate protein of the HSP70 family, which is central in many cellular processes. In particular, its regulatory role in autophagy is decisive. We focused this review on HSC70 structure-function considerations and based on this, we put a particular emphasis on HSC70 targeting by small molecules and peptides in order to develop intervention strategies that deviate some of HSC70 properties for therapeutic purposes. Generating active biomolecules regulating autophagy via its effect on HSC70 can effectively be designed only if we understand the fine relationships between HSC70 structure and functions.

Download full-text PDF

Source
http://dx.doi.org/10.4161/auto.26448DOI Listing

Publication Analysis

Top Keywords

chaperone protein
8
hsc70
5
hspa8/hsc70 chaperone
4
protein
4
protein structure
4
structure function
4
function chemical
4
chemical targeting
4
targeting hspa8/hsc70
4
hspa8/hsc70 protein
4

Similar Publications

The p53 transcription factor family consists of the three members p53, p63, and p73. Both p63 and p73 exist in different isoforms that are well characterized. Isoforms have also been identified for p53 and it has been proposed that they are responsible for increased cancer metastasis.

View Article and Find Full Text PDF

Genetic variants in HSP40 co-chaperones modulate ischemic heart disease risk.

Mol Biol Rep

September 2025

Laboratory of Genomic Research, Research Institute for Genetic and Molecular Epidemiology, Kursk State Medical University, Kursk, 305041, Russia.

Background: The chaperoning system, which is responsible for protein homeostasis, plays a significant role in cardiovascular diseases. Among molecular chaperones or heat shock proteins (HSPs), the HSP40 family, the main co-chaperone of HSP70, remains largely underexplored, especially in ischemic heart disease (IHD) risk.

Materials And Results: We genotyped 834 IHD patients and 1,328 healthy controls for three SNPs (rs2034598 and rs7189628 DNAJA2 and rs4926222 DNAJB1) using probe-based real-time PCR.

View Article and Find Full Text PDF

Targeting protein misfolding in Alzheimer's disease: The emerging role of molecular chaperones.

Biomed Pharmacother

September 2025

Department of Biomedical Sciences, Institute of Health, Jimma University, Jimma 378, Ethiopia; Division of Research & Development, Lovely Professional University, Phagwara 144411, India. Electronic address:

Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterised by cognitive decline and the accumulation of misfolded proteins, including amyloid-beta and hyperphosphorylated tau, which impair neuronal function and promote cell death. These misfolded proteins disrupt proteostasis by forming toxic aggregates that exacerbate disease progression. Molecular chaperones, such as heat shock proteins, actively maintain protein homeostasis by assisting in proper folding, preventing aggregation, and promoting the clearance of misfolded proteins.

View Article and Find Full Text PDF

High-Level Soluble Expression of Recombinant Human Bone Morphogenetic Protein-2 in .

ACS Synth Biol

September 2025

The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, P. R. China.

Human Bone Morphogenetic Protein-2 (hBMP-2) serves as a critical regulator in bone and cartilage formation; however, its industrial application is hindered by its inherent tendency to form inclusion bodies in prokaryotic expression systems. To address this issue, we established a recombinant hBMP-2 (rhBMP-2) expression system using the pCold II plasmid and the SHuffle T7 strain. We explored several strategies to enhance the solubility of rhBMP-2, including coexpression with molecular chaperones, vesicle-mediated secretory expression, fusion expression with synthetic intrinsically disordered proteins (SynIDPs), and fusion expression with small-molecule peptide tags.

View Article and Find Full Text PDF

Introduction: Spinal muscular atrophy (SMA), caused by pathogenic variants in the survival motor neuron (SMN) gene, is the most common genetic cause of mortality in children under the age of two. Prior reports of obstetric sonograms performed in pregnancies with severe forms of fetal SMA have discrepant findings that may stem from a failure to account for the SMN2 copy number.

Methods: We present a neonate diagnosed with SMA type 0 postnatally (0SMN1/1SMN2 genotype).

View Article and Find Full Text PDF