| pubmed-article:19174514 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19174514 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
| pubmed-article:19174514 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:19174514 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:19174514 | lifeskim:mentions | umls-concept:C1159372 | lld:lifeskim |
| pubmed-article:19174514 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:19174514 | lifeskim:mentions | umls-concept:C1707719 | lld:lifeskim |
| pubmed-article:19174514 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:19174514 | pubmed:dateCreated | 2009-2-11 | lld:pubmed |
| pubmed-article:19174514 | pubmed:abstractText | The "GTPase switch" paradigm, in which a GTPase switches between an active, GTP-bound state and an inactive, GDP-bound state through the recruitment of nucleotide exchange factors (GEFs) or GTPase activating proteins (GAPs), has been used to interpret the regulatory mechanism of many GTPases. A notable exception to this paradigm is provided by two GTPases in the signal recognition particle (SRP) and the SRP receptor (SR) that control the co-translational targeting of proteins to cellular membranes. Instead of the classical "GTPase switch," both the SRP and SR undergo a series of discrete conformational rearrangements during their interaction with one another, culminating in their reciprocal GTPase activation. Here, we show that this series of rearrangements during SRP-SR binding and activation provide important control points to drive and regulate protein targeting. Using real-time fluorescence, we showed that the cargo for SRP--ribosomes translating nascent polypeptides with signal sequences--accelerates SRP.SR complex assembly over 100-fold, thereby driving rapid delivery of cargo to the membrane. A series of subsequent rearrangements in the SRP x SR GTPase complex provide important driving forces to unload the cargo during late stages of protein targeting. Further, the cargo delays GTPase activation in the SRP.SR complex by 8-12 fold, creating an important time window that could further improve the efficiency and fidelity of protein targeting. Thus, the SRP and SR GTPases, without recruiting external regulatory factors, constitute a self-sufficient system that provides exquisite spatial and temporal control of a complex cellular process. | lld:pubmed |
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| pubmed-article:19174514 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19174514 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19174514 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19174514 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19174514 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:19174514 | pubmed:author | pubmed-author:ZhangXinX | lld:pubmed |
| pubmed-article:19174514 | pubmed:author | pubmed-author:BanNenadN | lld:pubmed |
| pubmed-article:19174514 | pubmed:author | pubmed-author:ShanShu-ouSO | lld:pubmed |
| pubmed-article:19174514 | pubmed:author | pubmed-author:SchaffitzelCh... | lld:pubmed |
| pubmed-article:19174514 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19174514 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:19174514 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:19174514 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19174514 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19174514 | pubmed:pagination | 1754-9 | lld:pubmed |
| pubmed-article:19174514 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:19174514 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19174514 | pubmed:articleTitle | Multiple conformational switches in a GTPase complex control co-translational protein targeting. | lld:pubmed |
| pubmed-article:19174514 | pubmed:affiliation | Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA. | lld:pubmed |
| pubmed-article:19174514 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19174514 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19174514 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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