Not just a cargo receptor for large cargoes; an emerging role of TANGO1 as an organizer of ER exit sites
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 materia...
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| Published in | Journal of biochemistry (Tokyo) Vol. 166; no. 2; pp. 115 - 119 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
England
01.08.2019
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| Subjects | |
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| Abstract | 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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| AbstractList | Abstract
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. 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. |
| Author | Maeda, Miharu Saito, Kota |
| Author_xml | – sequence: 1 givenname: Kota surname: Saito fullname: Saito, Kota organization: Department of Biological Informatics and Experimental Therapeutics, Graduate School of Medicine, Akita University, 1-1-1 Hondo, Akita 010-8543, Japan – sequence: 2 givenname: Miharu surname: Maeda fullname: Maeda, Miharu organization: Department of Biological Informatics and Experimental Therapeutics, Graduate School of Medicine, Akita University, 1-1-1 Hondo, Akita 010-8543, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31098622$$D View this record in MEDLINE/PubMed |
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| Keywords | collagen COPII secretion ER TANGO1 |
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