HSP100/Clp Proteins: a Common Mechanism Explains Diverse Functions

Overview

Journal Trends Biochem Sci

Specialty Biochemistry

Date 1996 Aug 1

PMID 8772382

Citations 208

Authors

E C Schirmer

J R Glover

M A Singer

S Lindquist

Affiliations

Soon will be listed here.

Abstract

The HSP100/Clp proteins are a newly discovered family with a great diversity of functions, such as increased tolerance to high temperatures, promotion of proteolysis of specific cellular substrates and regulation of transcription. HSP100/Clp proteins are also synthesized in a variety of specific patterns and, in eukaryotes, are localized to different subcellular compartments. Recent data suggest that a common ability to disassemble higher-order protein structures and aggregates unifies the molecular functions of this diverse family.

Citing Articles

More than Just Protein Folding: The Epichaperome, Mastermind of the Cancer Cell.

Amissah H, Antwi M, Amissah T, Combs S, Shevtsov M Cells. 2025; 14(3).

PMID: 39936995 PMC: 11817126. DOI: 10.3390/cells14030204.

Genome-Wide Identification of the Gene Family in Tomato and Expression Analysis Under Heat Stress.

Zhang Y, Yang T, Han J, Su X, Cong Y, Zhou M Int J Mol Sci. 2024; 25(22).

PMID: 39596389 PMC: 11595012. DOI: 10.3390/ijms252212325.

The middle domain of Hsp104 can ensure substrates are functional after processing.

Buchholz H, Dorweiler J, Guereca S, Wisniewski B, Shorter J, Manogaran A PLoS Genet. 2024; 20(10):e1011424.

PMID: 39361717 PMC: 11478891. DOI: 10.1371/journal.pgen.1011424.

Embryonic thermal manipulation: a potential strategy to mitigate heat stress in broiler chickens for sustainable poultry production.

Amaz S, Mishra B J Anim Sci Biotechnol. 2024; 15(1):75.

PMID: 38831417 PMC: 11149204. DOI: 10.1186/s40104-024-01028-1.

Identification of ClpB, a molecular chaperone involved in the stress tolerance and virulence of Streptococcus agalactiae.

Yang L, Wu Z, Ma T, Zeng H, Chen M, Zhang Y Vet Res. 2024; 55(1):60.

PMID: 38750480 PMC: 11094935. DOI: 10.1186/s13567-024-01318-6.