Journal
JOURNAL OF CELL SCIENCE
Volume 122, Issue 16, Pages 2866-2876Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.047423
Keywords
P-type ATPase; Aminophospholipid translocase; Acrosome biogenesis; Phospholipid asymmetry; Spermatogenesis
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Funding
- National Key Project for Basic Science Research of China [2009CB941100, 2007CB947903, 2005CB522701]
- National Natural Science Foundation of China [30871411, 30771077, 30500276]
- Robert Bosch Foundation
- Deutsche Forschungsgemeinschaft [Po748-4]
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P4-ATPases are transmembrane proteins unique to eukaryotes that play a fundamental role in vesicular transport. They have been proposed to act as phospholipid flippases thereby regulating lipid topology in cellular membranes. We cloned and characterized a novel murine P4-ATPase that is specifically expressed in testis, and named it FetA (flippase expressed in testis splicing form A). When expressed in Saccharomyces cerevisiae, FetA localizes partially to the plasma membrane resulting in increased internalization of NBD-labeled phosphatidylethanolamine and phosphatidylcholine, supporting a role for FetA in the inward lipid translocation across cellular membranes. In mouse testis, FetA protein is detected in gamete cells, from pachytene spermatocytes to mature sperms, and its intracellular localization is tightly related with acrosome formation, a process that involves intensive intracellular vesicle formation and fusion. Furthermore, loss-of-function of FetA by RNA interference in mastocytoma P815 cells profoundly perturbs the structural organization of the Golgi complex and causes loss of constitutive secretion at lower temperature. Our findings point to an essential role of FetA in Golgi morphology and secretory function, suggesting a crucial role for this novel murine P4-ATPase in spermatogenesis.
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