The Nanomechanics of Polycystin-1 Extracellular Region

Feng Qian, Wen Wei, Gregory G. Germino, Andrés F. Oberhauser

Journal of Biological Chemistry · 2005 · 82 citations · 39 references

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Abstract

Recent evidence suggests that polycystin-1 (PC1) acts as a mechanosensor, receiving signals from the primary cilia, neighboring cells, and extracellular matrix and transduces them into cellular responses that regulate proliferation, adhesion, and differentiation that are essential for the control of renal tubules and kidney morphogenesis. PC1 has an unusually long extracellular region (∼3000 amino acids) with a multimodular structure. Proteins with a similar architecture have structural and mechanical roles. Based on the structural similarities between PC1 and other modular proteins that have elastic properties we hypothesized that PC1 functions mechanically by providing a flexible and elastic linkage between cells. Here we directly tested this hypothesis by analyzing the mechanical properties of the entire PC1 extracellular region by using single molecule force spectroscopy. We show that the PC1 extracellular region and that this by the of the PC1 extracellular region a with force that have a of force and we that the PC1 extracellular region the of We that mechanical the PC1 extracellular region a the of for and the of by Recent evidence suggests that polycystin-1 (PC1) acts as a mechanosensor, receiving signals from the primary cilia, neighboring cells, and extracellular matrix and transduces them into cellular responses that regulate proliferation, adhesion, and differentiation that are essential for the control of renal tubules and kidney morphogenesis. PC1 has an unusually long extracellular region (∼3000 amino acids) with a multimodular structure. Proteins with a similar architecture have structural and mechanical roles. Based on the structural similarities between PC1 and other modular proteins that have elastic properties we hypothesized that PC1 functions mechanically by providing a flexible and elastic linkage between cells. Here we directly tested this hypothesis by analyzing the mechanical properties of the entire PC1 extracellular region by using single molecule force spectroscopy. We show that the PC1 extracellular region and that this by the of the PC1 extracellular region a with force that have a of force and we that the PC1 extracellular region the of We that mechanical the PC1 extracellular region a the of for and the of by kidney of that and PC1 kidney kidney force kidney and for kidney force kidney and for of the has an of and a of kidney from renal tubules and the and renal of the the for and and a that renal of as as the this the of the PC1 the of the renal this and the of the a with an extracellular amino a of a and a a of a the kidney and a region that for amino that a for Recent that PC1 as a PC1 has as that the renal tubules has a that similar proteins with structural and mechanical as of and elastic extracellular matrix elastic of proteins Recent single molecule have that proteins are and on the structural similarities between PC1 and other modular proteins that have elastic properties we hypothesized that that PC1 functions mechanically by 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References

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