Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 38, Pages 15846-15851Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1109101108
Keywords
cholera toxin; endocytosis
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Funding
- Core Research for Evolutional Science and Technology, Japan Science and Technology Agency
- Program for Promotion of Basic and Applied Research for Innovations in Bio-Oriented Industry
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Senri Life Science Foundation
- [20370045]
- [18050019]
- Grants-in-Aid for Scientific Research [21200075, 23227004] Funding Source: KAKEN
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Phosphatidylserine (PS) is a relatively minor constituent of biological membranes. Despite its low abundance, PS in the plasma membrane (PM) plays key roles in various phenomena such as the coagulation cascade, clearance of apoptotic cells, and recruitment of signaling molecules. PS also localizes in endocytic organelles, but how this relates to its cellular functions remains unknown. Here we report that PS is essential for retrograde membrane traffic at recycling endosomes (REs). PS was most concentrated in REs among intracellular organelles, and evectin-2 (evt-2), a protein of previously unknown function, was targeted to REs by the binding of its pleckstrin homology (PH) domain to PS. X-ray analysis supported the specificity of the binding of PS to the PH domain. Depletion of evt-2 or masking of intracellular PS suppressed membrane traffic from REs to the Golgi. These findings uncover the molecular basis that controls the RE-to-Golgi transport and identify a unique PH domain that specifically recognizes PS but not polyphosphoinositides.
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