High impact information on SYT6

• Protein kinase C-mediated phosphorylation of the two polybasic regions of synaptotagmin VI regulates their function in acrosomal exocytosis [1].
• Aided by a streptolysin-O permeabilization protocol developed in our laboratory, we have previously demonstrated requirements for Rab3A, NSF, and synaptotagmin VI in the human sperm acrosome reaction [2].
• Synaptotagmin VI participates in the acrosome reaction of human spermatozoa [3].
• Rab3A-promoted exocytosis was inhibited by the cytosolic domain of synaptotagmin VI and by the anti-synaptotagmin VI antibody, indicating that synaptotagmin is also necessary for Rab-mediated acrosomal content release [3].

Biological context of SYT6

• Calcium-triggered acrosomal exocytosis in permeabilized sperm cells was abrogated by a specific anti-synaptotagmin VI antibody, indicating that the protein is required for the process [3].

Associations of SYT6 with chemical compounds

• Moreover, a recombinant fusion protein between glutathione S-transferase and the two calcium and phospholipid binding domains of synaptotagmin VI completely inhibited calcium-triggered exocytosis [3].

Analytical, diagnostic and therapeutic context of SYT6

• The ubiquitous synaptotagmin VI isoform was found in human sperm cells by Western blot analysis [3].

References