ArticleThe Biochemical journal2004
Binding of proteins to the PDZ domain regulates proteolytic activity of HtrA1 serine protease.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.
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Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 88 citations in OpenAlex.
- Identification and Evolutionary Analysis of Potential Candidate Genes in a Human Eating Disorder.BioMed research international · 2016Pooled it
- "Chocolate Chip Sign" on Susceptibility-Weighted Imaging: A Novel Neuroimaging Biomarker for HTRA1-Related Cerebral Small Vessel Disease.Neurology. Genetics · 2025Article
- Article
- Current Views on Chr10q26 Contribution to Age-Related Macular Degeneration.Advances in experimental medicine and biology · 2023Review
- TGF-β/Smad Signalling Activation by HTRA1 Regulates the Function of Human Lens Epithelial Cells and Its Mechanism in Posterior Subcapsular Congenital Cataract.International journal of molecular sciences · 2022Article
- An allosteric HTRA1-calpain 2 complex with restricted activation profile.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Processing of D1 Protein: A Mysterious Process Carried Out in Thylakoid Lumen.International journal of molecular sciences · 2022Review
- Overview of Human HtrA Family Proteases and Their Distinctive Physiological Roles and Unique Involvement in Diseases, Especially Cancer and Pregnancy Complications.International journal of molecular sciences · 2021Review
- Ongoing controversies and recent insights of the ARMS2-HTRA1 locus in age-related macular degeneration.Experimental eye research · 2021Review
- Pneumococcal Extracellular Serine Proteases: Molecular Analysis and Impact on Colonization and Disease.Frontiers in cellular and infection microbiology · 2021Review
- ThePlant physiology · 2019Article
- Late-onset retinal degeneration pathology due to mutations in CTRP5 is mediated through HTRA1.Aging cell · 2019Article
- Loss of HtrA1 serine protease induces synthetic modulation of aortic vascular smooth muscle cells.PloS one · 2018Article
- Osteoarthritis-Like Changes in Bardet-Biedl Syndrome Mutant Ciliopathy Mice (Frontiers in physiology · 2018Article
- Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2.Cell death & disease · 2017Article
- Protective effects of an HTRA1 insertion-deletion variant against age-related macular degeneration in the Chinese populations.Laboratory investigation; a journal of technical methods and pathology · 2017Article
- Article
- The differential role of HTRA1 in HPV-positive and HPV-negative cervical cell line proliferation.BMC cancer · 2016Article
- Distribution, classification, domain architectures and evolution of prolyl oligopeptidases in prokaryotic lineages.BMC genomics · 2014Article
- The autolysis of human HtrA1 is governed by the redox state of its N-terminal domain.Biochemistry · 2014Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HtrA1, a member of the mammalian HtrA (high temperature requirement A) serine protease family, has a highly conserved protease domain followed by a PDZ domain. Accumulating evidence has indicated that PDZ domains regulate protease activity of HtrA proteins. We searched for binding partners of the PDZ domain of mouse HtrA1 by yeast two-hybrid screening, and isolated proteins that were recognized by the HtrA1 PDZ domain through their C-terminal ends with a core consensus Phi-X-Phi-[V/L/F/A]-COOH sequence (where Phi is a hydrophobic/non-polar amino acid). C-propeptides of fibrillar collagens were most frequently isolated. Type III procollagen alpha1 C-propeptide, which was used as a model protein, was digested by HtrA1. HtrA1 cleavage of the collagen C-propeptide was enhanced by reductive denaturation of the C-propeptide and partly inhibited by removal of the C-terminal four amino acids from the C-propeptide, suggesting that the substrate recognition was facilitated by the binding of the free C-terminal ends of substrates to the PDZ domain of HtrA1. The synthetic oligopeptide (GM130Pep) that fitted the consensus recognition sequence bound to HtrA1 with a high affinity (K(d)=6.0 nM). GM130Pep stimulated HtrA1 protease activity 3- to 4-fold, but did not efficiently stimulate the activity of an HtrA1 mutant lacking the PDZ domain, supporting the notion that the PDZ domain enhances protease activity upon ligand binding. The peptide derived from Type III collagen alpha1 C-propeptide specifically stimulated protease activity of HtrA1, but did not stimulate nor significantly bind to HtrA2, suggesting that the collagen C-propeptide is a specific physiological regulator of HtrA1.
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