ArticleMatrix biology : journal of the International Society for Matrix Biology2022
Vertebrate extracellular matrix protein hemicentin-1 interacts physically and genetically with basement membrane protein nidogen-2.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 22 citations in OpenAlex.
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- Novel regulators of heparan sulfate proteoglycans modulate cellular uptake of α-synuclein fibrils.Communications biology · 2025Article
- HMCN1 variants aggravate epidermolysis bullosa simplex phenotype.The Journal of experimental medicine · 2025Article
- Matricellular proteins in immunometabolism and tissue homeostasis.BMB reports · 2024Review
- Human Cell-Derived Matrix Composite Hydrogels with Diverse Composition for Use in Vasculature-on-chip Models.Advanced healthcare materials · 2024Article
- wnt10a is required for zebrafish median fin fold maintenance and adult unpaired fin metamorphosis.Developmental dynamics : an official publication of the American Association of Anatomists · 2024Article
- Genome-wide detection of positive and balancing signatures of selection shared by four domesticated rainbow trout populations (Oncorhynchus mykiss).Genetics, selection, evolution : GSE · 2024Article
- Nidogen in development and disease.Frontiers in cell and developmental biology · 2024Review
- Matricellular Proteins in the Homeostasis, Regeneration, and Aging of Skin.International journal of molecular sciences · 2023Review
- Hemicentin-mediated type IV collagen assembly strengthens juxtaposed basement membrane linkage.The Journal of cell biology · 2023Article
- Lens placode modulates extracellular matrix formation during early eye development.Differentiation; research in biological diversityArticle
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
Hemicentins are large proteins of the extracellular matrix that belong to the fibulin family and play pivotal roles during development and homeostasis of a variety of invertebrate and vertebrate tissues. However, bona fide interaction partners of hemicentins have not been described as yet. Here, applying surface plasmon resonance spectroscopy and co-immunoprecipitation, we identify the basement membrane protein nidogen-2 (NID2) as a binding partner of mouse and zebrafish hemicentin-1 (HMCN1), in line with the formerly described essential role of mouse HMCN1 in basement membrane integrity. We show that HMCN1 binds to the same protein domain of NID2 (G2) as formerly shown for laminins, but with an approximately 3.5-fold lower affinity and in a competitive manner. Furthermore, immunofluorescence and immunogold labeling revealed that HMCN1/Hmcn1 is localized close to basement membranes and in partial overlap with NID2/Nid2a in different tissues of mouse and zebrafish. Genetic knockout and antisense-mediated knockdown studies in zebrafish further show that loss of Nid2a leads to similar defects in fin fold morphogenesis as the loss of Laminin-α5 (Lama5) or Hmcn1. Finally, combined partial loss-of-function studies indicated that nid2a genetically interacts with both hmcn1 and lama5. Together, these findings suggest that despite their mutually exclusive physical binding, hemicentins, nidogens, and laminins tightly cooperate and support each other during formation, maintenance, and function of basement membranes to confer tissue linkage.
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