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http://purl.uniprot.org/citations/16105044http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16105044http://www.w3.org/2000/01/rdf-schema#comment"

Background

Parathyroid hormone (PTH) rapidly down-regulates type IIa sodium-dependent phosphate transporter (NaPi-IIa) via an endocytic pathway. Since the relationship between PTH signaling and NaPi-IIa endocytosis has not been explored, we investigated the role of membrane microdomains in this process.

Methods

We examined the submembrane localization of NaPi-IIa in opossum kidney (OK-N2) cells that stably expressed human NaPi-IIa, and searched for a PTH-induced specific phosphorylating substrate on their membrane microdomains by immunoblotting with specific antibody against phospho substrates of protein kinases.

Results

We found that NaPi-IIa was primarily localized in low-density membrane (LDM) domains of the plasma membrane; PTH reduced the levels of immunoreactive NaPi-IIa in these domains. Furthermore, PTH activated both protein kinase A (PKA) and protein kinase Calpha (PKCa) and increased the phosphorylation of 250 kD and 80 kD substrates; this latter substrate was identified as ezrin, which a member of the ezrin-radixin-moesin (ERM) protein family. In response to PTH, ezrin was phosphorylated by both PKA and PKC. Dominant negative ezrin blocked the reduction in NaPi-IIa expression in the LDM domains that was induced by PTH.

Conclusion

These data suggest that NaPi-IIa and PTH-induced phosphorylated proteins that include ezrin are compartmentalized in LDM microdomains. This compartmentalization may play an important role in the down-regulation of NaPi-IIa via endocytosis."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.org/dc/terms/identifier"doi:10.1111/j.1523-1755.2005.00505.x"xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Arai H."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Ichikawa M."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Miyamoto K."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Yamamoto H."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Takeda E."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Taketani Y."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Sawada N."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Takeichi T."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/author"Nashiki K."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/name"Kidney Int"xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/pages"1137-1147"xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/title"Role of membrane microdomains in PTH-mediated down-regulation of NaPi-IIa in opossum kidney cells."xsd:string
http://purl.uniprot.org/citations/16105044http://purl.uniprot.org/core/volume"68"xsd:string
http://purl.uniprot.org/citations/16105044http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16105044
http://purl.uniprot.org/citations/16105044http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16105044
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http://purl.uniprot.org/uniprot/#_Q05BP0-mappedCitation-16105044http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16105044
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http://purl.uniprot.org/uniprot/Q8N8W2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16105044
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