Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 25, Issue 19, Pages 8693-8702Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.25.19.8693-8702.2005
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Funding
- NIGMS NIH HHS [GM 56827, R01 GM056827] Funding Source: Medline
- NIMH NIH HHS [R01 MH061876, MH61876] Funding Source: Medline
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Synaptotagmin (syt) I is thought to act as a Ca2+ sensor that regulates neuronal exocytosis. Fifteen additional isoforms of syt have been identified, but their functions are less well understood. Here, we used PC 12 cells to test the idea that different isoforms of syt impart cells with distinct metal (i.e., Ca2+, Ba2+, and Sr2+) requirements for secretion. These cells express syt's I and IX (syt IX sometimes referred to as syt V), which have low apparent metal affinities, at much higher levels than syt VII, which we show has a relatively high apparent affinity for metals. We found that syt I and VII partially colocalize on large dense core vesicles and that upregulation of syt VII produces a concomitant increase in the divalent cation sensitivity of catecholamine release from PC12 cells. Furthermore, RNA interference-mediated knockdown of endogenous syt VII reduced the metal sensitivity of release. These data support the hypothesis that the complement of syt's expressed by a cell, in conjunction with their metal affinity, determines the divalent cation sensitivity of exocytosis.
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