Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast.

The EMBO journal | Feb 1, 2001

http://www.ncbi.nlm.nih.gov/pubmed/11157748

The role of protein phosphorylation in secretion is not well understood. Here we show that yeast lacking the Snc1,2 v-SNAREs, or bearing a temperature-sensitive mutation in the Sso2 t-SNARE, are rescued at restrictive conditions by the addition of ceramide precursors and analogs to the growth medium. Rescue results from dephosphorylation of the Sso t-SNAREs by a ceramide-activated type 2A protein phosphatase (Sit4) involved in cell cycle control. Sso t-SNARE dephosphorylation correlated with its assembly into complexes with the Sec9 t-SNARE, both in vitro and in vivo, and with an increase in protein trafficking and secretion in cells. SNARE complexes isolated under these conditions contained only Sso and Sec9, suggesting that a t-t-SNARE fusion complex is sufficient to confer exocytosis. Mutation of a single PKA site (Ser79 to Ala79) in Sso1 resulted in a decrease in phosphorylation and was sufficient to confer growth to snc cells at restrictive conditions. Thus, modulation of t-SNARE phosphorylation regulates SNARE complex assembly and membrane fusion in vivo.

Pubmed ID: 11157748 RIS Download

Mesh terms: Exocytosis | Fungal Proteins | Membrane Fusion | Membrane Proteins | Models, Biological | Mutagenesis, Site-Directed | Mutation | Phosphoprotein Phosphatases | Phosphorylation | Qa-SNARE Proteins | SNARE Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Sphingosine | Temperature | Vesicular Transport Proteins