F
IPR013126

Heat shock protein 70 family

InterPro entry
This entry contains information that has been generated using an AI language model. Please exercise discretion when interpreting the information provided.
Short nameHsp_70_fam
Overlapping
homologous
superfamilies
 
family relationships

Description

Expert-curated
Heat shock proteins, Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region
[5]
.

Expert-curated
Hsp70 proteins have an average molecular weight of 70kDa
[1, 2, 3]
. In most species, there are many proteins that belong to the Hsp70 family. Some of these are only expressed under stress conditions (strictly inducible), while some are present in cells under normal growth conditions and are not heat-inducible (constitutive or cognate)
[6, 4]
. Hsp70 proteins can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, for example).

Expert-curated
This entry represents the Hsp70 family, and includes chaperone protein DnaK and luminal-binding proteins. It also includes heat shock protein 110 (Hsp110) from Caenorhabditis elegans which helps prevent the aggregation of denatured proteins in neurons
[7]
. Also included is endoplasmic reticulum (ER) chaperone BiP (HSPA5) which is important for protein folding and quality control in the ER
[8]
.

AI-generatedReviewed and updated
The Heat Shock Protein 70 (HSP70) family is a group of highly conserved molecular chaperones involved in a variety of cellular processes. Members of this family play crucial roles in the folding of newly synthesized proteins, preventing the aggregation of denatured proteins under stress, assisting in protein translocation into organelles, and participating in the degradation of damaged proteins. They are also implicated in the assembly of multimeric protein complexes within the endoplasmic reticulum. Some HSP70 proteins act as nucleotide-exchange factors, promoting the release of ADP from other chaperones to trigger substrate release. They are essential for cellular protection against stress conditions such as heat shock and hypoxia, where they may help in cytoprotection and protein folding.

References

1.Essential roles of 70kDa heat inducible proteins. Craig EA. Bioessays 11, 48-52, (1989). View articlePMID: 2686623

2.Speculations on the functions of the major heat shock and glucose-regulated proteins. Pelham HR. Cell 46, 959-61, (1986). View articlePMID: 2944601

3.Heat-shock proteins. Coming in from the cold. Pelham H. Nature 332, 776-7, (1988). View articlePMID: 3282176

4.The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization. Snutch TP, Heschl MF, Baillie DL. Gene 64, 241-55, (1988). View articlePMID: 2841196

5.The Hsp70 and Hsp60 chaperone machines. Bukau B, Horwich AL. Cell 92, 351-66, (1998). View articlePMID: 9476895

6.Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Flaherty KM, DeLuca-Flaherty C, McKay DB. Nature 346, 623-8, (1990). View articlePMID: 2143562

7.An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans. Wang J, Farr GW, Hall DH, Li F, Furtak K, Dreier L, Horwich AL. PLoS Genet. 5, e1000350, (2009). View articlePMID: 19165329

8.Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP. Yang J, Nune M, Zong Y, Zhou L, Liu Q. Structure 23, 2191-2203, (2015). View articlePMID: 26655470

GO terms

biological process

  • None

cellular component

  • None

Cross References

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.