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Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1
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| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Journal of Cell Science, 2013 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Quilty, Douglas Gray, Fraser Summerfeldt, Nathan Cassel, Dan Melançon, Paul Quilty, Douglas Gray, Fraser Summerfeldt, Nathan Cassel, Dan Melançon, Paul |
|---|---|
| author |
Quilty, Douglas Gray, Fraser Summerfeldt, Nathan Cassel, Dan Melançon, Paul |
| spellingShingle |
Quilty, Douglas Gray, Fraser Summerfeldt, Nathan Cassel, Dan Melançon, Paul Journal of Cell Science Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 Cell Biology |
| author_sort |
quilty, douglas |
| spelling |
Quilty, Douglas Gray, Fraser Summerfeldt, Nathan Cassel, Dan Melançon, Paul 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.130591 <jats:p>ADP-ribosylation factors (Arfs) play central roles in the regulation of vesicular trafficking through the Golgi. Arfs are activated at the Golgi membrane by guanine nucleotide exchange factors (GEFs) that are recruited from cytosol. Here, we describe a novel mechanism for regulation of recruitment and activity of the ArfGEF Golgi-specific BFA resistance factor 1 (GBF1). Conditions that alter the cellular Arf•GDP/Arf•GTP ratio result in GBF1 recruitment. This recruitment of GBF1 occurs selectively on cis-Golgi membranes in direct response to increased Arf•GDP. GBF1 recruitment requires Arf•GDP myristoylation-dependent interactions suggesting regulation of a membrane bound factor. Once recruited, GBF1 causes increased Arf•GTP production at the Golgi, consistent with a feed-forward, self-limiting mechanism of Arf activation. This mechanism is proposed to maintain steady-state levels of Arf•GTP at the cis-Golgi during cycles of Arf-dependent trafficking events.</jats:p> Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 Journal of Cell Science |
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The Company of Biologists, 2013 |
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| title |
Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_unstemmed |
Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_full |
Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_fullStr |
Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_full_unstemmed |
Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_short |
Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_sort |
arf activation at the golgi is modulated by feed-forward stimulation of the exchange factor gbf1 |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.130591 |
| publishDate |
2013 |
| physical |
|
| description |
<jats:p>ADP-ribosylation factors (Arfs) play central roles in the regulation of vesicular trafficking through the Golgi. Arfs are activated at the Golgi membrane by guanine nucleotide exchange factors (GEFs) that are recruited from cytosol. Here, we describe a novel mechanism for regulation of recruitment and activity of the ArfGEF Golgi-specific BFA resistance factor 1 (GBF1). Conditions that alter the cellular Arf•GDP/Arf•GTP ratio result in GBF1 recruitment. This recruitment of GBF1 occurs selectively on cis-Golgi membranes in direct response to increased Arf•GDP. GBF1 recruitment requires Arf•GDP myristoylation-dependent interactions suggesting regulation of a membrane bound factor. Once recruited, GBF1 causes increased Arf•GTP production at the Golgi, consistent with a feed-forward, self-limiting mechanism of Arf activation. This mechanism is proposed to maintain steady-state levels of Arf•GTP at the cis-Golgi during cycles of Arf-dependent trafficking events.</jats:p> |
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| author | Quilty, Douglas, Gray, Fraser, Summerfeldt, Nathan, Cassel, Dan, Melançon, Paul |
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| description | <jats:p>ADP-ribosylation factors (Arfs) play central roles in the regulation of vesicular trafficking through the Golgi. Arfs are activated at the Golgi membrane by guanine nucleotide exchange factors (GEFs) that are recruited from cytosol. Here, we describe a novel mechanism for regulation of recruitment and activity of the ArfGEF Golgi-specific BFA resistance factor 1 (GBF1). Conditions that alter the cellular Arf•GDP/Arf•GTP ratio result in GBF1 recruitment. This recruitment of GBF1 occurs selectively on cis-Golgi membranes in direct response to increased Arf•GDP. GBF1 recruitment requires Arf•GDP myristoylation-dependent interactions suggesting regulation of a membrane bound factor. Once recruited, GBF1 causes increased Arf•GTP production at the Golgi, consistent with a feed-forward, self-limiting mechanism of Arf activation. This mechanism is proposed to maintain steady-state levels of Arf•GTP at the cis-Golgi during cycles of Arf-dependent trafficking events.</jats:p> |
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| spelling | Quilty, Douglas Gray, Fraser Summerfeldt, Nathan Cassel, Dan Melançon, Paul 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.130591 <jats:p>ADP-ribosylation factors (Arfs) play central roles in the regulation of vesicular trafficking through the Golgi. Arfs are activated at the Golgi membrane by guanine nucleotide exchange factors (GEFs) that are recruited from cytosol. Here, we describe a novel mechanism for regulation of recruitment and activity of the ArfGEF Golgi-specific BFA resistance factor 1 (GBF1). Conditions that alter the cellular Arf•GDP/Arf•GTP ratio result in GBF1 recruitment. This recruitment of GBF1 occurs selectively on cis-Golgi membranes in direct response to increased Arf•GDP. GBF1 recruitment requires Arf•GDP myristoylation-dependent interactions suggesting regulation of a membrane bound factor. Once recruited, GBF1 causes increased Arf•GTP production at the Golgi, consistent with a feed-forward, self-limiting mechanism of Arf activation. This mechanism is proposed to maintain steady-state levels of Arf•GTP at the cis-Golgi during cycles of Arf-dependent trafficking events.</jats:p> Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 Journal of Cell Science |
| spellingShingle | Quilty, Douglas, Gray, Fraser, Summerfeldt, Nathan, Cassel, Dan, Melançon, Paul, Journal of Cell Science, Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1, Cell Biology |
| title | Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_full | Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_fullStr | Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_full_unstemmed | Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_short | Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| title_sort | arf activation at the golgi is modulated by feed-forward stimulation of the exchange factor gbf1 |
| title_unstemmed | Arf activation at the Golgi is modulated by feed-forward stimulation of the exchange factor GBF1 |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.130591 |