Sphingomyelin is sorted at the trans Golgi network into a distinct class of secretory vesicle
Author(s) -
Yongqiang Deng,
Félix Rivera-Molina,
Derek Toomre,
Christopher G. Burd
Publication year - 2016
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1602875113
Subject(s) - sphingomyelin , golgi apparatus , organelle , microbiology and biotechnology , secretory pathway , sphingolipid , vesicle , ceramide , biology , secretory vesicle , vesicular transport protein , vesicular transport proteins , chemistry , biochemistry , membrane , endoplasmic reticulum , endosome , vacuolar protein sorting , intracellular , apoptosis
Significance The biochemical reactions that drive cellular life are housed in distinct membrane enclosed compartments known as organelles. Whereas proteins targeting to different organelles are well developed, little is known regarding how lipids are sorted to different organelles. We engineered a protein from a marine organism into a fluorescent “biosensor” of sphingomyelin (SM), a sphingolipid that is produced in the Golgi apparatus but is a major component of the plasma membrane. By monitoring SM dynamics in live cells, we discovered that SM is transported from its site of synthesis in the Golgi to the plasma membrane in a distinct type of secretory transport carrier. Our findings show that vesicle-based trafficking pathways are specialized to transport distinct types of lipids, in addition to proteins.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom