Not just a cargo receptor for large cargoes; an emerging role of TANGO1 as an organizer of ER exit sites
Author(s) -
Kota Saito,
Miharu Maeda
Publication year - 2019
Publication title -
the journal of biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 115
eISSN - 1756-2651
pISSN - 0021-924X
DOI - 10.1093/jb/mvz036
Subject(s) - copii , endoplasmic reticulum , golgi apparatus , copi , microbiology and biotechnology , secretion , vesicle , receptor , vesicular transport protein , transport protein , biology , secretory pathway , chemistry , biochemistry , membrane
Proteins synthesized within the endoplasmic reticulum (ER) are exported from ER exit sites via coat protein complex II (COPII)-coated vesicles. Although the mechanisms of COPII-vesicle formation at the ER exit sites are highly conserved among species, vertebrate cells secrete a wide range of materials, including collagens and chylomicrons, which form bulky structures within the ER that are too large to fit into conventional carriers. Transport ANd Golgi Organization 1 (TANGO1) was initially identified as a cargo receptor for collagens but has been recently rediscovered as an organizer of ER exit sites. We would like to review recent advances in the mechanism of large cargo secretion and organization of ER exit sites through the function of TANGO1.
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