| pubmed-article:16135816 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16135816 | lifeskim:mentions | umls-concept:C0221920 | lld:lifeskim |
| pubmed-article:16135816 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:16135816 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
| pubmed-article:16135816 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:16135816 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:16135816 | lifeskim:mentions | umls-concept:C1418600 | lld:lifeskim |
| pubmed-article:16135816 | lifeskim:mentions | umls-concept:C1538717 | lld:lifeskim |
| pubmed-article:16135816 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:16135816 | pubmed:dateCreated | 2005-9-1 | lld:pubmed |
| pubmed-article:16135816 | pubmed:abstractText | PKD2, or polycystin 2, the product of the gene mutated in type 2 autosomal dominant polycystic kidney disease, belongs to the transient receptor potential channel superfamily and has been shown to function as a nonselective cation channel in the plasma membrane. However, the mechanism of PKD2 activation remains elusive. We show that PKD2 overexpression increases epidermal growth factor (EGF)-induced inward currents in LLC-PK(1) kidney epithelial cells, while the knockdown of endogenous PKD2 by RNA interference or the expression of a pathogenic missense variant, PKD2-D511V, blunts the EGF-induced response. Pharmacological experiments indicate that the EGF-induced activation of PKD2 occurs independently of store depletion but requires the activity of phospholipase C (PLC) and phosphoinositide 3-kinase (PI3K). Pipette infusion of purified phosphatidylinositol-4,5-bisphosphate (PIP(2)) suppresses the PKD2-mediated effect on EGF-induced conductance, while pipette infusion of phosphatidylinositol-3,4,5-trisphosphate (PIP(3)) does not have any effect on this conductance. Overexpression of type Ialpha phosphatidylinositol-4-phosphate 5-kinase [PIP(5)Kalpha], which catalyzes the formation of PIP(2), suppresses EGF-induced currents. Biochemical experiments show that PKD2 physically interacts with PLC-gamma2 and EGF receptor (EGFR) in transfected HEK293T cells and colocalizes with EGFR and PIP(2) in the primary cilium of LLC-PK(1) cells. We propose that plasma membrane PKD2 is under negative regulation by PIP(2). EGF may reduce the threshold of PKD2 activation by mechanical and other stimuli by releasing it from PIP(2)-mediated inhibition. | lld:pubmed |
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| pubmed-article:16135816 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16135816 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16135816 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16135816 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16135816 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:16135816 | pubmed:author | pubmed-author:MaRongR | lld:pubmed |
| pubmed-article:16135816 | pubmed:author | pubmed-author:TsiokasLeonid... | lld:pubmed |
| pubmed-article:16135816 | pubmed:author | pubmed-author:LiWei-PingWP | lld:pubmed |
| pubmed-article:16135816 | pubmed:author | pubmed-author:AkbaraliHamid... | lld:pubmed |
| pubmed-article:16135816 | pubmed:author | pubmed-author:KongJinJ | lld:pubmed |
| pubmed-article:16135816 | pubmed:author | pubmed-author:RundleDanaD | lld:pubmed |
| pubmed-article:16135816 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16135816 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:16135816 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16135816 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16135816 | pubmed:pagination | 8285-98 | lld:pubmed |
| pubmed-article:16135816 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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