Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation.

@article{Weinberger2005ControlOG,
  title={Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation.},
  author={Adina Weinberger and Faustin Kamena and Rachel Kama and Anne Spang and Jeffrey E Gerst},
  journal={Molecular biology of the cell},
  year={2005},
  volume={16 10},
  pages={
          4918-30
        }
}
Previously, we demonstrated that the phosphorylation of t-SNAREs by protein kinase A (PKA) affects their ability to participate in SNARE complexes and to confer endocytosis and exocytosis in yeast. Here, we show that the presumed phosphorylation of a conserved membrane-proximal PKA consensus site (serine-317) in the Sed5 t-SNARE regulates endoplasmic reticulum (ER)-Golgi transport, as well as Golgi morphology. Sed5 is a phosphoprotein, and both alanine and aspartate substitutions in serine-317… CONTINUE READING

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