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Figure 7. Proposed model describing the role of the cyclic phosphorylation of Sec5 in an engagement-disengagement cycle between the exocyst and its upstream G protein. From: The Function of the Exocyst is Regulated by Effector Phosphorylation.
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Figure 2. The RalA-interacting exocyst subunit Sec5 undergoes hormone-stimulated phosphorylation in its effector domain. From: The Function of the Exocyst is Regulated by Effector Phosphorylation.
Figure 6. Sec5 phosphorylation contributes to cellular organization and organism development. From: The Function of the Exocyst is Regulated by Effector Phosphorylation.
Figure 3. Sec5 effector domain phosphorylation disengages the G protein RalA during vesicle targeting. From: The Function of the Exocyst is Regulated by Effector Phosphorylation.
Figure 1. RalA promotes exocyst function independently of GTP hydrolysis. From: The Function of the Exocyst is Regulated by Effector Phosphorylation.
Figure 4. Protein Kinase C (PKC) catalyzes Sec5 effector domain phosphorylation that negatively regulates RalA interaction. From: The Function of the Exocyst is Regulated by Effector Phosphorylation.
Figure 5. Sec5 phosphorylation contributes to a cyclic regulatory loop upon recognition by RalA. From: The Function of the Exocyst is Regulated by Effector Phosphorylation.
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