What is it about?
Several glycolytic enzymes and their isoforms have been found to be important in cell signaling unrelated to glycolysis. The involvement of parafusin (PFUS), a member of the phosphoglucomutase (PGM) superfamily with no phosphoglucomutase activity, in Ca2+-dependent exocytosis has been controversial
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Why is it important?
Earlier work showed that parafusin is a secretory vesicle scaffold component with unusual post-translational modifications (cyclic phosphorylation and phosphoglucosylation) coupled to stages in the exocytic process. Using RNAi, we demonstrate that parafusin synthesis can be reversibly blocked, with minor or no effect on other PGM isoforms. PFUS knockdown produces an inhibition of dense core secretory vesicle (DCSV) synthesis leading to an exo− phenotype.
Perspectives
We conclude that PFUS and its orthologs are necessary for proper scaffold maturation. Because of this association, parafusin is an important signaling component for regulatory control of the secretory pathway.
Professor Elzbieta Wyroba
Nencki Institute of Experimental Biology
Read the Original
This page is a summary of: RNAi knockdown of parafusin inhibits the secretory pathway, European Journal of Cell Biology, October 2011, Elsevier,
DOI: 10.1016/j.ejcb.2011.06.002.
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