Mechanism of Hsp70 specialised interactions in protein translocation and the unfolded protein response
| Autor: | Maruf M.U. Ali, Piotr Nowak, Natacha Larburu, Christopher J. Adams, Chao-Sheng Chen |
|---|---|
| Přispěvatelé: | Cancer Research UK |
| Rok vydání: | 2020 |
| Předmět: |
Gene isoform
Models Molecular BiP Immunology Review Review Article IRE1 UPR Biology Endoplasmic Reticulum 0601 Biochemistry and Cell Biology General Biochemistry Genetics and Molecular Biology Substrate Specificity Structure-Activity Relationship Animals Humans Nucleotide HSP70 Heat-Shock Proteins Protein translocation lcsh:QH301-705.5 chemistry.chemical_classification protein translocation Mechanism (biology) General Neuroscience Cell Membrane Hsp70 chaperones Hsp70 Cell biology Mitochondria Tim44 Protein Transport lcsh:Biology (General) chemistry Gene Expression Regulation 1107 Immunology Unfolded protein response Unfolded Protein Response Carrier Proteins Molecular Chaperones Protein Binding 0605 Microbiology |
| Zdroj: | Open Biology Open Biology, Vol 10, Iss 8 (2020) |
| Popis: | Hsp70 chaperones interact with substrate proteins in a coordinated fashion that is regulated by nucleotides and enhanced by assisting cochaperones. There are numerous homologues and isoforms of Hsp70 that participate in a wide variety of cellular functions. This diversity can facilitate adaption or specialization based on particular biological activity and location within the cell. In this review, we highlight two specialized binding partner proteins, Tim44 and IRE1, that interact with Hsp70 at the membrane in order to serve their respective roles in protein translocation and unfolded protein response signalling. Recent mechanistic data suggest analogy in the way the two Hsp70 homologues (BiP and mtHsp70) can bind and release from IRE1 and Tim44 upon substrate engagement. These shared mechanistic features may underlie how Hsp70 interacts with specialized binding partners and may extend our understanding of the mechanistic repertoire that Hsp70 chaperones possess. |
| Databáze: | OpenAIRE |
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