Title : MARCKS protein is phosphorylated and regulates calcium mobilization during human acrosomal exocytosis.

Pub. Date : 2013

PMID : 23704996






3 Functional Relationships(s)
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1 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. adenophostin A myristoylated alanine rich protein kinase C substrate Homo sapiens
2 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. adenophostin A myristoylated alanine rich protein kinase C substrate Homo sapiens
3 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. adenophostin A myristoylated alanine rich protein kinase C substrate Homo sapiens