CIDeRplusGeneral Information:
| Id: | 13,390 |
| Diseases: |
Ciliopathy
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| Mus musculus | |
| article | |
| Reference: | Nauli SM et al.(2003) Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells Nat Genet 33: 129-137 [PMID: 12514735] |
Interaction Information:
| Comment | PC1 co-localized with the specific ciliary axoneme marker acetylated alpha-tubulin in kidneys of wild-type but not Pkd1del34/del34 mice. Analysis with gamma-tubulin, a specific marker of the basal body of the cilium, showed co-localization of PC1 in the basal body in wild-type but not in Pkd1del34/del34cells. Thus, PC1 seems to be a component of the primary cilium. |
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Formal Description Interaction-ID: 126134 |
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| Comment | PC1 co-localized with the specific ciliary axoneme marker acetylated alpha-tubulin in kidneys of wild-type but not Pkd1del34/del34 mice. Analysis with gamma-tubulin, a specific marker of the basal body of the cilium, showed co-localization of PC1 in the basal body in wild-type but not in Pkd1del34/del34cells. Thus, PC1 seems to be a component of the primary cilium. |
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Formal Description Interaction-ID: 126163 |
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| Comment | PC1 co-localized with the specific ciliary axoneme marker acetylated alpha-tubulin in kidneys of wild-type but not Pkd1del34/del34 mice. Analysis with gamma-tubulin, a specific marker of the basal body of the cilium, showed co-localization of PC1 in the basal body in wild-type but not in Pkd1del34/del34cells. Thus, PC1 seems to be a component of the primary cilium. |
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Formal Description Interaction-ID: 126164 |
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| Comment | The primary cilium of kidney epithelium has been shown to mediate transduction of a mechanical flow stimulus into a Ca2+ signaling response. To explore whether ciliary PC1 could contribute to this response, the authors used fluid shear stress to promote cilium bending and associated Ca2+ signaling in cultured kidney epithelial cells. Wild-type cells showed a specific sensitivity to low levels of shear stress similar to those observed in proximal tubules and other renal tubules in vivo. Cells with mutations in Pkd1 do not activate flow-induced Ca2+ signaling. |
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Formal Description Interaction-ID: 126165 |
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| Comment | The primary cilium of kidney epithelium has been shown to mediate transduction of a mechanical flow stimulus into a Ca2+ signaling response. To explore whether ciliary PC1 could contribute to this response, the authors used fluid shear stress to promote cilium bending and associated Ca2+ signaling in cultured kidney epithelial cells. Wild-type cells showed a specific sensitivity to low levels of shear stress similar to those observed in proximal tubules and other renal tubules in vivo. Cells with mutations in Pkd1 do not activate flow-induced Ca2+ signaling. |
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Formal Description Interaction-ID: 126166 |
process increases_activity of process |
| Comment | PC2 co-localized with acetylated alpha-tubulin, gamma-tubulin and PC1 in wild-type cells, but not in Pkd1del34/del34 cells. |
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Formal Description Interaction-ID: 126167 |
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| Comment | PC2 co-localized with acetylated alpha-tubulin, gamma-tubulin and PC1 in wild-type cells, but not in Pkd1del34/del34 cells. |
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Formal Description Interaction-ID: 126168 |
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| Comment | PC2 co-localized with acetylated alpha-tubulin, gamma-tubulin and PC1 in wild-type cells, but not in Pkd1del34/del34 cells. |
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Formal Description Interaction-ID: 126169 |
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| Comment | Ca2+ entry through PC2 initiates flow-induced Ca2+ signaling. |
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Formal Description Interaction-ID: 126170 |
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| Comment | Collectively, the data indicate that ciliary PC1 and PC2 act in concert with ryanodine receptors to mediate transduction of an extracellular mechanical stimulus into a Ca2+ signaling response inside kidney epithelial cells. The requirement for extracellular Ca2+ indicates that the initial response to mechanical stimulation is the influx of Ca2+ across the plasma membrane, whereas the results obtained with ryanodine and caffeine suggest that the intraorganellar Ca2+ buffering system may mediate downstream signaling. |
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Formal Description Interaction-ID: 126171 |
gene/protein increases_activity of process |
| Comment | Collectively, the data indicate that ciliary PC1 and PC2 act in concert with ryanodine receptors to mediate transduction of an extracellular mechanical stimulus into a Ca2+ signaling response inside kidney epithelial cells. The requirement for extracellular Ca2+ indicates that the initial response to mechanical stimulation is the influx of Ca2+ across the plasma membrane, whereas the results obtained with ryanodine and caffeine suggest that the intraorganellar Ca2+ buffering system may mediate downstream signaling. |
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Formal Description Interaction-ID: 126172 |
gene/protein increases_activity of process |
| Comment | Collectively, the data indicate that ciliary PC1 and PC2 act in concert with ryanodine receptors to mediate transduction of an extracellular mechanical stimulus into a Ca2+ signaling response inside kidney epithelial cells. The requirement for extracellular Ca2+ indicates that the initial response to mechanical stimulation is the influx of Ca2+ across the plasma membrane, whereas the results obtained with ryanodine and caffeine suggest that the intraorganellar Ca2+ buffering system may mediate downstream signaling. |
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Formal Description Interaction-ID: 126173 |
gene/protein RYR increases_activity of process |