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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/5130Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.creator | Prieto-Sánchez, Rosario M. | - |
| dc.creator | Berenjeno, Inmaculada M. | - |
| dc.creator | Bustelo, Xosé R. | - |
| dc.date | 2008-06-17T10:10:14Z | - |
| dc.date | 2008-06-17T10:10:14Z | - |
| dc.date | 2006-05 | - |
| dc.date.accessioned | 2017-01-31T01:42:21Z | - |
| dc.date.available | 2017-01-31T01:42:21Z | - |
| dc.identifier | Oncogene 25(21): 2961–2973 (2006) | - |
| dc.identifier | 1078-8956 | - |
| dc.identifier | http://hdl.handle.net/10261/5130 | - |
| dc.identifier | 10.1038/sj.onc.1209333 | - |
| dc.identifier.uri | http://dspace.mediu.edu.my:8181/xmlui/handle/10261/5130 | - |
| dc.description | 13 páginas, 8 figuras.-- El pdf del artículo es el manuscrito de autor. | - |
| dc.description | We show here that the GTPase RhoG is involved in caveolar trafficking. Wild-type RhoG moves sequentially to the plasma membrane, intracellular vesicles, and the Golgi apparatus along markers of this endocytic pathway. Such translocation is associated with changes in RhoG GDP/GTP levels and is highly dependent on lipid raft integrity and on the function of the GTPase dynamin2. In addition, the constitutively active RhoGQ61L mutant is preferentially located in endocytic vesicles that can be decorated with markers of the caveola-derived endocytic pathway. RhoGQ61L, but not the analogous Rac1 mutant protein, affects caveola internalization and the subsequent delivery of endocytic vesicles to the Golgi apparatus. The expression of RhoG/Rac1 chimeric proteins and RhoGQ61L effector mutants in cells induces alterations in the internalization of caveolae and severe changes in vesicle structure, respectively. However, the knockdown of endogenous rhoG transcripts using small interfering RNAs does not affect significantly the trafficking of caveola-derived vesicles, suggesting that RhoG function is dispensable for this endocytic process or, alternatively, that its function is compensated by other molecules. Taken together, these observations assign a novel function to RhoG and suggest that caveolar trafficking, as previously shown for other endocytic routes, is modulated by GTPases of the Ras superfamily. | - |
| dc.description | This work was supported by grants from both the US National Cancer Institute (5-R01-CA73735-08) and the Spanish Ministry of Education and Science (SAF2003-00028). RMP-S and IMB are students of the Molecular and Cellular Cancer Biology graduate program of the CIC and the University of Salamanca and are supported by FPU fellowships (AP2000-3829 and FP2000-6489; Spanish Ministry of Education and Science). | - |
| dc.description | Peer reviewed | - |
| dc.format | 1871635 bytes | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Nature Publishing Group | - |
| dc.rights | openAccess | - |
| dc.subject | RhoG | - |
| dc.subject | Caveolin | - |
| dc.subject | Endocytosis | - |
| dc.subject | Cholera toxin | - |
| dc.subject | Vesicle trafficking | - |
| dc.title | Involvement of the Rho/Rac family member RhoG in caveolar endocytosis | - |
| dc.type | Artículo | - |
| Appears in Collections: | Digital Csic | |
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