ArticleProtein science : a publication of the Protein Society2009
The Brichos domain of prosurfactant protein C can hold and fold a transmembrane segment.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 43 citations in OpenAlex.
- Clinical characteristics of SFTPC gene mutations in children: a single-center experience.Italian journal of pediatrics · 2025Article
- Noninvasive management of infants with SFTPC pathogenic variants.Pediatric pulmonology · 2024Article
- Exploring protein-protein interactions and oligomerization state of pulmonary surfactant protein C (SP-C) through FRET and fluorescence self-quenching.Protein science : a publication of the Protein Society · 2024Article
- A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain.Protein science : a publication of the Protein Society · 2023Review
- Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue.RSC chemical biology · 2022Article
- Transcriptome-wide prediction of prostate cancer gene expression from histopathology images using co-expression-based convolutional neural networks.Bioinformatics (Oxford, England) · 2022Article
- Mapping SP-C co-chaperone binding sites reveals molecular consequences of disease-causing mutations on protein maturation.Nature communications · 2022Article
- Genetic causes of surfactant protein abnormalities.Current opinion in pediatrics · 2019Review
- Article
- Amyloid and intracellular accumulation of BRINeurobiology of aging · 2017Article
- Specific chaperones and regulatory domains in control of amyloid formation.The Journal of biological chemistry · 2015Review
- The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogaster.Disease models & mechanisms · 2014Article
- BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.The Journal of biological chemistry · 2012Article
- 4-Phenylbutyric acid treatment rescues trafficking and processing of a mutant surfactant protein-C.American journal of respiratory cell and molecular biology · 2012Article
- High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- More than 1,001 problems with protein domain databases: transmembrane regions, signal peptides and the issue of sequence homology.PLoS computational biology · 2010Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prosurfactant protein C (proSP-C) is a 197-residue integral membrane protein, in which the C-terminal domain (CTC, positions 59-197) is localized in the endoplasmic reticulum (ER) lumen and contains a Brichos domain (positions 94-197). Mature SP-C corresponds largely to the transmembrane (TM) region of proSP-C. CTC binds to SP-C, provided that it is in nonhelical conformation, and can prevent formation of intracellular amyloid-like inclusions of proSP-C that harbor mutations linked to interstitial lung disease (ILD). Herein it is shown that expression of proSP-C (1-58), that is, the N-terminal propeptide and the TM region, in HEK293 cells results in virtually no detectable protein, while coexpression of CTC in trans yields SDS-soluble monomeric proSP-C (1-58). Recombinant human (rh) CTC binds to cellulose-bound peptides derived from the nonpolar TM region, but not the polar cytosolic part, of proSP-C, and requires >/=5-residues for maximal binding. Binding of rhCTC to a nonhelical peptide derived from SP-C results in alpha-helix formation provided that it contains a long TM segment. Finally, rhCTC and rhCTC Brichos domain shows very similar substrate specificities, but rhCTC(L188Q), a mutation linked to ILD is unable to bind all peptides analyzed. These data indicate that the Brichos domain of proSP-C is a chaperone that induces alpha-helix formation of an aggregation-prone TM region.
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