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PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation
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| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Journal of Cell Science, 120, 2007, 5, S. 792-801 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Venkateswarlu, Kanamarlapudi Brandom, Kevin G. Yun, Hongruo Venkateswarlu, Kanamarlapudi Brandom, Kevin G. Yun, Hongruo |
|---|---|
| author |
Venkateswarlu, Kanamarlapudi Brandom, Kevin G. Yun, Hongruo |
| spellingShingle |
Venkateswarlu, Kanamarlapudi Brandom, Kevin G. Yun, Hongruo Journal of Cell Science PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation Cell Biology |
| author_sort |
venkateswarlu, kanamarlapudi |
| spelling |
Venkateswarlu, Kanamarlapudi Brandom, Kevin G. Yun, Hongruo 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.03373 <jats:p>GTPase activating proteins (GAPs) of the centaurin family regulate the actin cytoskeleton and vesicle trafficking through inactivation of the ADP-ribosylation factor (ARF) family of small GTP-binding proteins. We report the functional characterisation of centaurin-α2, which is structurally related to the centaurin-α1 ARF6 GAP. centaurin-α2 contains an N-terminal GAP domain followed by two pleckstrin homology (PH) domains (N-PH and C-PH). In vitro, GFP-centaurin-α2 specifically binds the phosphatidylinositol (PI) 3-kinase lipid products, PI 3,4-P2 and PI 3,4,5-P3 (PIP3), through its C-terminal PH domain. In agreement with this observation, GFP-centaurin-α2 was recruited to the plasma membrane from the cytosol in EGF-stimulated cells in a PI-3-kinase-dependent manner. Moreover, the C-PH domain is sufficient and necessary for membrane recruitment of centaurin-α2. centaurin-α2 shows sustained kinetics of PI-3-kinase-mediated membrane recruitment in EGF-stimulated cells, owing to its binding to PI 3,4-P2. centaurin-α2 prevents ARF6 translocation to, and cortical actin formation at, the plasma membrane, which are phenotypic indications for ARF6 activation in EGF-stimulated cells. Moreover, the constitutively active mutant of ARF6 reverses the effect of centaurin-α2 on cortical actin formation. The membrane targeted centaurin-α2 is constitutively active. Together, these studies indicate that centaurin-α2 is recruited in a sustained manner to the plasma membrane through binding to PI 3,4-P2 and thereby regulates actin reorganisation via ARF6.</jats:p> PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation Journal of Cell Science |
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The Company of Biologists, 2007 |
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The Company of Biologists, 2007 |
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1477-9137 0021-9533 |
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| title |
PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_unstemmed |
PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_full |
PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_fullStr |
PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_full_unstemmed |
PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_short |
PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_sort |
pi-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on arf6-mediated actin cytoskeleton reorganisation |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.03373 |
| publishDate |
2007 |
| physical |
792-801 |
| description |
<jats:p>GTPase activating proteins (GAPs) of the centaurin family regulate the actin cytoskeleton and vesicle trafficking through inactivation of the ADP-ribosylation factor (ARF) family of small GTP-binding proteins. We report the functional characterisation of centaurin-α2, which is structurally related to the centaurin-α1 ARF6 GAP. centaurin-α2 contains an N-terminal GAP domain followed by two pleckstrin homology (PH) domains (N-PH and C-PH). In vitro, GFP-centaurin-α2 specifically binds the phosphatidylinositol (PI) 3-kinase lipid products, PI 3,4-P2 and PI 3,4,5-P3 (PIP3), through its C-terminal PH domain. In agreement with this observation, GFP-centaurin-α2 was recruited to the plasma membrane from the cytosol in EGF-stimulated cells in a PI-3-kinase-dependent manner. Moreover, the C-PH domain is sufficient and necessary for membrane recruitment of centaurin-α2. centaurin-α2 shows sustained kinetics of PI-3-kinase-mediated membrane recruitment in EGF-stimulated cells, owing to its binding to PI 3,4-P2. centaurin-α2 prevents ARF6 translocation to, and cortical actin formation at, the plasma membrane, which are phenotypic indications for ARF6 activation in EGF-stimulated cells. Moreover, the constitutively active mutant of ARF6 reverses the effect of centaurin-α2 on cortical actin formation. The membrane targeted centaurin-α2 is constitutively active. Together, these studies indicate that centaurin-α2 is recruited in a sustained manner to the plasma membrane through binding to PI 3,4-P2 and thereby regulates actin reorganisation via ARF6.</jats:p> |
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| author | Venkateswarlu, Kanamarlapudi, Brandom, Kevin G., Yun, Hongruo |
| author_facet | Venkateswarlu, Kanamarlapudi, Brandom, Kevin G., Yun, Hongruo, Venkateswarlu, Kanamarlapudi, Brandom, Kevin G., Yun, Hongruo |
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| description | <jats:p>GTPase activating proteins (GAPs) of the centaurin family regulate the actin cytoskeleton and vesicle trafficking through inactivation of the ADP-ribosylation factor (ARF) family of small GTP-binding proteins. We report the functional characterisation of centaurin-α2, which is structurally related to the centaurin-α1 ARF6 GAP. centaurin-α2 contains an N-terminal GAP domain followed by two pleckstrin homology (PH) domains (N-PH and C-PH). In vitro, GFP-centaurin-α2 specifically binds the phosphatidylinositol (PI) 3-kinase lipid products, PI 3,4-P2 and PI 3,4,5-P3 (PIP3), through its C-terminal PH domain. In agreement with this observation, GFP-centaurin-α2 was recruited to the plasma membrane from the cytosol in EGF-stimulated cells in a PI-3-kinase-dependent manner. Moreover, the C-PH domain is sufficient and necessary for membrane recruitment of centaurin-α2. centaurin-α2 shows sustained kinetics of PI-3-kinase-mediated membrane recruitment in EGF-stimulated cells, owing to its binding to PI 3,4-P2. centaurin-α2 prevents ARF6 translocation to, and cortical actin formation at, the plasma membrane, which are phenotypic indications for ARF6 activation in EGF-stimulated cells. Moreover, the constitutively active mutant of ARF6 reverses the effect of centaurin-α2 on cortical actin formation. The membrane targeted centaurin-α2 is constitutively active. Together, these studies indicate that centaurin-α2 is recruited in a sustained manner to the plasma membrane through binding to PI 3,4-P2 and thereby regulates actin reorganisation via ARF6.</jats:p> |
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| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| spelling | Venkateswarlu, Kanamarlapudi Brandom, Kevin G. Yun, Hongruo 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.03373 <jats:p>GTPase activating proteins (GAPs) of the centaurin family regulate the actin cytoskeleton and vesicle trafficking through inactivation of the ADP-ribosylation factor (ARF) family of small GTP-binding proteins. We report the functional characterisation of centaurin-α2, which is structurally related to the centaurin-α1 ARF6 GAP. centaurin-α2 contains an N-terminal GAP domain followed by two pleckstrin homology (PH) domains (N-PH and C-PH). In vitro, GFP-centaurin-α2 specifically binds the phosphatidylinositol (PI) 3-kinase lipid products, PI 3,4-P2 and PI 3,4,5-P3 (PIP3), through its C-terminal PH domain. In agreement with this observation, GFP-centaurin-α2 was recruited to the plasma membrane from the cytosol in EGF-stimulated cells in a PI-3-kinase-dependent manner. Moreover, the C-PH domain is sufficient and necessary for membrane recruitment of centaurin-α2. centaurin-α2 shows sustained kinetics of PI-3-kinase-mediated membrane recruitment in EGF-stimulated cells, owing to its binding to PI 3,4-P2. centaurin-α2 prevents ARF6 translocation to, and cortical actin formation at, the plasma membrane, which are phenotypic indications for ARF6 activation in EGF-stimulated cells. Moreover, the constitutively active mutant of ARF6 reverses the effect of centaurin-α2 on cortical actin formation. The membrane targeted centaurin-α2 is constitutively active. Together, these studies indicate that centaurin-α2 is recruited in a sustained manner to the plasma membrane through binding to PI 3,4-P2 and thereby regulates actin reorganisation via ARF6.</jats:p> PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation Journal of Cell Science |
| spellingShingle | Venkateswarlu, Kanamarlapudi, Brandom, Kevin G., Yun, Hongruo, Journal of Cell Science, PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation, Cell Biology |
| title | PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_full | PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_fullStr | PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_full_unstemmed | PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_short | PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| title_sort | pi-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on arf6-mediated actin cytoskeleton reorganisation |
| title_unstemmed | PI-3-kinase-dependent membrane recruitment of centaurin-α2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.03373 |