| pubmed-article:19389710 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C0032824 | lld:lifeskim |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C1416545 | lld:lifeskim |
| pubmed-article:19389710 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:19389710 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:19389710 | pubmed:dateCreated | 2009-6-8 | lld:pubmed |
| pubmed-article:19389710 | pubmed:abstractText | Vascular smooth muscle Kv1 delayed rectifier K+ channels (KDR) containing Kv1.2 control membrane potential and thereby regulate contractility. Vasodilatory agonists acting via protein kinase A (PKA) enhance vascule smooth muscle Kv1 activity, but the molecular basis of this regulation is uncertain. We characterized the role of a C-terminal phosphorylation site, Ser-449, in Kv1.2 expressed in HEK 293 cells by biochemical and electrophysiological methods. We found that 1) in vitro phosphorylation of Kv1.2 occurred exclusively at serine residues, 2) one major phosphopeptide that co-migrated with 449pSASTISK was generated by proteolysis of in vitro phosphorylated Kv1.2, 3) the peptide 445KKSRSASTISK exhibited stoichiometric phosphorylation by PKA in vitro, 4) matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectroscopy (MS) and MS/MS confirmed in vitro Ser-449 phosphorylation by PKA, 5) in situ phosphorylation at Ser-449 was detected in HEK 293 cells by MALDI-TOF MS followed by MS/MS. MIDAS (multiple reaction monitoring-initiated detection and sequencing) analysis revealed additional phosphorylated residues, Ser-440 and Ser-441, 6) in vitro 32P incorporation was significantly reduced in Kv1.2-S449A, Kv1.2-S449D, and Kv1.2-S440A/S441A/S449A mutant channels, but Kv1.2-S440A/S441A was identical to wild-type Kv1.2 (Kv1.2-WT), and 7) bath applied 8-Br-cAMP or dialysis with PKA catalytic subunit (cPKA) increased Kv1.2-WT but not Kv1.2-S449A current amplitude. cPKA increased Kv1.2-WT current in inside-out patches. Rp-CPT-cAMPS reduced Kv1.2-WT current, blocked the increase due to 8-Br-cAMP, but had no effect on Kv1.2-S449A. cPKA increased current due to double mutant Kv1.2-S440A/S441A but had no effect on Kv1.2-S449D or Kv1.2-S440A/S441A/S449A. We conclude that Ser-449 in Kv1.2 is a site of PKA phosphorylation and a potential molecular mechanism for Kv1-containing KDR channel modulation by agonists via PKA activation. | lld:pubmed |
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| pubmed-article:19389710 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19389710 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19389710 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19389710 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19389710 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19389710 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:19389710 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:19389710 | pubmed:author | pubmed-author:WalshMichael... | lld:pubmed |
| pubmed-article:19389710 | pubmed:author | pubmed-author:ColeWilliam... | lld:pubmed |
| pubmed-article:19389710 | pubmed:author | pubmed-author:SchriemerDavi... | lld:pubmed |
| pubmed-article:19389710 | pubmed:author | pubmed-author:JohnsonRosaly... | lld:pubmed |
| pubmed-article:19389710 | pubmed:author | pubmed-author:El-YazbiAhmed... | lld:pubmed |
| pubmed-article:19389710 | pubmed:author | pubmed-author:WalshEmma JEJ | lld:pubmed |
| pubmed-article:19389710 | pubmed:author | pubmed-author:HughesMorgan... | lld:pubmed |
| pubmed-article:19389710 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19389710 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:19389710 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:19389710 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19389710 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19389710 | pubmed:pagination | 16562-74 | lld:pubmed |
| pubmed-article:19389710 | pubmed:dateRevised | 2010-9-24 | lld:pubmed |
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| pubmed-article:19389710 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19389710 | pubmed:articleTitle | Identification and functional characterization of protein kinase A-catalyzed phosphorylation of potassium channel Kv1.2 at serine 449. | lld:pubmed |
| pubmed-article:19389710 | pubmed:affiliation | Smooth Muscle Research Group, Southern Alberta Mass Spectrometry Centre, University of Calgary, Calgary, Alberta, Canada. | lld:pubmed |
| pubmed-article:19389710 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19389710 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:100009479 | entrezgene:pubmed | pubmed-article:19389710 | lld:entrezgene |
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