| pubmed-article:18689676 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18689676 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:18689676 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:18689676 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:18689676 | lifeskim:mentions | umls-concept:C1149337 | lld:lifeskim |
| pubmed-article:18689676 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:18689676 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18689676 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:18689676 | pubmed:dateCreated | 2008-8-20 | lld:pubmed |
| pubmed-article:18689676 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18689676 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18689676 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18689676 | pubmed:abstractText | On starvation, Dictyostelium cells aggregate to form multicellular fruiting bodies containing spores that germinate when transferred to nutrient-rich medium. This developmental cycle correlates with the extent of actin phosphorylation at Tyr-53 (pY53-actin), which is low in vegetative cells but high in viable mature spores. Here we describe high-resolution crystal structures of pY53-actin and unphosphorylated actin in complexes with gelsolin segment 1 and profilin. In the structure of pY53-actin, the phosphate group on Tyr-53 makes hydrogen-bonding interactions with residues of the DNase I-binding loop (D-loop) of actin, resulting in a more stable conformation of the D-loop than in the unphosphorylated structures. A more rigidly folded D-loop may explain some of the previously described properties of pY53-actin, including its increased critical concentration for polymerization, reduced rates of nucleation and pointed end elongation, and weak affinity for DNase I. We show here that phosphorylation of Tyr-53 inhibits subtilisin cleavage of the D-loop and reduces the rate of nucleotide exchange on actin. The structure of profilin-Dictyostelium-actin is strikingly similar to previously determined structures of profilin-beta-actin and profilin-alpha-actin. By comparing this representative set of profilin-actin structures with other structures of actin, we highlight the effects of profilin on the actin conformation. In the profilin-actin complexes, subdomains 1 and 3 of actin close around profilin, producing a 4.7 degrees rotation of the two major domains of actin relative to each other. As a result, the nucleotide cleft becomes moderately more open in the profilin-actin complex, probably explaining the stimulation of nucleotide exchange on actin by profilin. | lld:pubmed |
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| pubmed-article:18689676 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18689676 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18689676 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18689676 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18689676 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18689676 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18689676 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18689676 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18689676 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:18689676 | pubmed:author | pubmed-author:LAIM SMS | lld:pubmed |
| pubmed-article:18689676 | pubmed:author | pubmed-author:DominguezRobe... | lld:pubmed |
| pubmed-article:18689676 | pubmed:author | pubmed-author:JinXimeiX | lld:pubmed |
| pubmed-article:18689676 | pubmed:author | pubmed-author:FerronFrançoi... | lld:pubmed |
| pubmed-article:18689676 | pubmed:author | pubmed-author:KornEdward... | lld:pubmed |
| pubmed-article:18689676 | pubmed:author | pubmed-author:BaekKyuwonK | lld:pubmed |
| pubmed-article:18689676 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18689676 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:18689676 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:18689676 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18689676 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18689676 | pubmed:pagination | 11748-53 | lld:pubmed |
| pubmed-article:18689676 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
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| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
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| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:meshHeading | pubmed-meshheading:18689676... | lld:pubmed |
| pubmed-article:18689676 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18689676 | pubmed:articleTitle | Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding. | lld:pubmed |
| pubmed-article:18689676 | pubmed:affiliation | Department of Physiology, 3700 Hamilton Walk, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6085, USA. | lld:pubmed |
| pubmed-article:18689676 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18689676 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18689676 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| pubmed-article:18689676 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
