ArticleProceedings of the National Academy of Sciences of the United States of America2011
Macromolecular assembly of polycystin-2 intracytosolic C-terminal domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Recent advances in understanding ion transport mechanisms in polycystic kidney disease.Clinical science (London, England : 1979) · 2021Review
- SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale.Protein science : a publication of the Protein Society · 2019Article
- Structural studies of the C-terminal tail of polycystin-2 (PC2) reveal insights into the mechanisms used for the functional regulation of PC2.The Journal of physiology · 2016Review
- Oligomerization of the polycystin-2 C-terminal tail and effects on its Ca2+-binding properties.The Journal of biological chemistry · 2015Article
- Cyst growth, polycystins, and primary cilia in autosomal dominant polycystic kidney disease.Kidney research and clinical practice · 2014Review
- Polycystin-1: a master regulator of intersecting cystic pathways.Trends in molecular medicine · 2014Review
- Ion channels in renal disease.Chemical reviews · 2012Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Mutations in PKD2 are responsible for approximately 15% of the autosomal dominant polycystic kidney disease cases. This gene encodes polycystin-2, a calcium-permeable cation channel whose C-terminal intracytosolic tail (PC2t) plays an important role in its interaction with a number of different proteins. In the present study, we have comprehensively evaluated the macromolecular assembly of PC2t homooligomer using a series of biophysical and biochemical analyses. Our studies, based on a new delimitation of PC2t, have revealed that it is capable of assembling as a homotetramer independently of any other portion of the molecule. Our data support this tetrameric arrangement in the presence and absence of calcium. Molecular dynamics simulations performed with a modified all-atoms structure-based model supported the PC2t tetrameric assembly, as well as how different populations are disposed in solution. The simulations demonstrated, indeed, that the best-scored structures are the ones compatible with a fourfold oligomeric state. These findings clarify the structural properties of PC2t domain and strongly support a homotetramer assembly of PC2.
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