ArticleThe Journal of biological chemistry2016
The pH-dependent Client Release from the Collagen-specific Chaperone HSP47 Is Triggered by a Tandem Histidine Pair.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- The anion channel GPR89 is a tumor-specific dependency in breast cancer.Nature communications · 2026Article
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Decoding collagen's thermally induced unfolding and refolding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multifunctional DNA-Collagen Biomaterials: Developmental Advances and Biomedical Applications.ACS biomaterials science & engineering · 2025Review
- HSP47 at the Crossroads of Thrombosis and Collagen Dynamics: Unlocking Therapeutic Horizons and Debates.TH open : companion journal to thrombosis and haemostasis · 2025Review
- A model for collagen secretion by intercompartmental continuities.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Local Net Charge State of Collagen Triple Helix Is a Determinant of FKBP22 Binding to Collagen III.International journal of molecular sciences · 2023Article
- Targeting HSP47 and HSP70: promising therapeutic approaches in liver fibrosis management.Journal of translational medicine · 2022Review
- Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.Scientific reports · 2022Article
- Genomic prediction of growth in a commercially, recreationally, and culturally important marine resource, the Australian snapper (Chrysophrys auratus).G3 (Bethesda, Md.) · 2022Article
- Collagen's primary structure determines collagen:HSP47 complex stoichiometry.The Journal of biological chemistry · 2021Article
- Aberrant binding of mutant HSP47 affects posttranslational modification of type I collagen and leads to osteogenesis imperfecta.PLoS genetics · 2021Article
- Interaction between KDELR2 and HSP47 as a Key Determinant in Osteogenesis Imperfecta Caused by Bi-allelic Variants in KDELR2.American journal of human genetics · 2020Article
- Mechanisms of procollagen and HSP47 sorting during ER-to-Golgi trafficking.Matrix biology : journal of the International Society for Matrix Biology · 2020Article
- Triple-Helix-Stabilizing Effects in Collagen Model Peptides Containing PPII-Helix-Preorganized Diproline Modules.Angewandte Chemie (International ed. in English) · 2020Article
- Lowering the culture temperature corrects collagen abnormalities caused by HSP47 gene knockout.Scientific reports · 2019Article
- Bone biology: insights from osteogenesis imperfecta and related rare fragility syndromes.The FEBS journal · 2019Review
- ER-to-Golgi trafficking of procollagen in the absence of large carriers.The Journal of cell biology · 2019Article
- Roles of the endoplasmic reticulum-resident, collagen-specific molecular chaperone Hsp47 in vertebrate cells and human disease.The Journal of biological chemistry · 2019Review
- TANGO1 and SEC12 are copackaged with procollagen I to facilitate the generation of large COPII carriers.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock protein 47 (HSP47) is an endoplasmic reticulum (ER)-resident collagen-specific chaperone and essential for proper formation of the characteristic collagen triple helix. It preferentially binds to the folded conformation of its clients and accompanies them from the ER to the Golgi compartment, where it releases them and is recycled back to the ER. Unlike other chaperones, the binding and release cycles are not governed by nucleotide exchange and hydrolysis, but presumably the dissociation of the HSP47-procollagen complex is triggered by the lower pH in the Golgi (pH 6.3) compared with the ER (pH 7.4). Histidine residues have been suggested as triggers due to their approximate textbook pKa value of 6.1 for their side chains. We present here an extensive theoretical and experimental study of the 14 histidine residues present in canine HSP47, where we have mutated all histidine residues in the collagen binding interface and additionally all of those that were predicted to undergo a significant change in protonation state between pH 7 and 6. These mutants were characterized by biolayer interferometry for their pH-dependent binding to a collagen model. One mutant (H238N) loses binding, which can be explained by a rearrangement of the Arg(222) and Asp(385) residues, which are crucial for specific collagen recognition. Most of the other mutants were remarkably silent, but a double mutant with His(273) and His(274) exchanged for asparagines exhibits a much less pronounced pH dependence of collagen binding. This effect is mainly caused by a lower koff at the low pH values.
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