| pubmed-article:14976207 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14976207 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:14976207 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:14976207 | lifeskim:mentions | umls-concept:C1333699 | lld:lifeskim |
| pubmed-article:14976207 | lifeskim:mentions | umls-concept:C0681842 | lld:lifeskim |
| pubmed-article:14976207 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:14976207 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:14976207 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:14976207 | pubmed:dateCreated | 2004-4-19 | lld:pubmed |
| pubmed-article:14976207 | pubmed:abstractText | G protein-coupled receptor kinases (GRKs) specifically phosphorylate agonist-occupied G protein-coupled receptors at the inner surface of the plasma membrane (PM), leading to receptor desensitization. GRKs utilize a variety of mechanisms to bind tightly, and sometimes reversibly, to cellular membranes. Previous studies demonstrated the presence of a membrane binding domain in the C terminus of GRK5. Here we define a mechanism by which this short C-terminal stretch of amino acids of GRK5 mediates PM localization. Secondary structure predictions suggest that a region contained within amino acids 546-565 of GRK5 forms an amphipathic helix, with the key features of the predicted helix being a hydrophobic patch of amino acids on one face of the helix, hydrophilic amino acids on the opposite face, and a number of basic amino acids surrounding the hydrophobic patch. We show that amino acids 546-565 of GRK5 are sufficient to target the cytoplasmic green fluorescent protein (GFP) to the PM, and the hydrophobic amino acids are necessary for PM targeting of GFP-546-565. Moreover, full-length GRK5-GFP is localized to the PM, but mutation of the hydrophobic patch or the surrounding basic amino acids prevents PM localization of GRK5-GFP. Last, we show that mutation of the hydrophobic residues severely diminishes phospholipid-dependent autophosphorylation of GRK5 and phosphorylation of membrane-bound rhodopsin by GRK5. The findings in this report thus suggest the presence of a membrane binding motif in GRK5 and define the importance of a group of hydrophobic amino acids within this motif in mediating its PM localization. | lld:pubmed |
| pubmed-article:14976207 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14976207 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976207 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14976207 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:14976207 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14976207 | pubmed:author | pubmed-author:BenovicJeffre... | lld:pubmed |
| pubmed-article:14976207 | pubmed:author | pubmed-author:ProninAlexey... | lld:pubmed |
| pubmed-article:14976207 | pubmed:author | pubmed-author:WedegaertnerP... | lld:pubmed |
| pubmed-article:14976207 | pubmed:author | pubmed-author:ThiyagarajanM... | lld:pubmed |
| pubmed-article:14976207 | pubmed:author | pubmed-author:EvankoDaniel... | lld:pubmed |
| pubmed-article:14976207 | pubmed:author | pubmed-author:Stracquatanio... | lld:pubmed |
| pubmed-article:14976207 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14976207 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:14976207 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:14976207 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14976207 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14976207 | pubmed:pagination | 17989-95 | lld:pubmed |
| pubmed-article:14976207 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:14976207 | pubmed:meshHeading | pubmed-meshheading:14976207... | lld:pubmed |
| pubmed-article:14976207 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14976207 | pubmed:articleTitle | A predicted amphipathic helix mediates plasma membrane localization of GRK5. | lld:pubmed |
| pubmed-article:14976207 | pubmed:affiliation | Department of Microbiology and Immunology and Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. | lld:pubmed |
| pubmed-article:14976207 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14976207 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14976207 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:2869 | entrezgene:pubmed | pubmed-article:14976207 | lld:entrezgene |
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