A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans
Summary: Vitellogenin is thought to share a common ancestor with human apolipoprotein B (ApoB) for systemic lipid transport. In Caenorhabditis elegans, although a general route for inter-tissue vitellogenin transport has been described, the full mechanism that underlies its intracellular trafficking...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-02-01
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| Series: | iScience |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004225001208 |
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| author | Jimmy H. Mo Chao Zhai Kwangsek Jung Yan Li Yonghong Yan Meng-Qiu Dong Ho Yi Mak |
| author_facet | Jimmy H. Mo Chao Zhai Kwangsek Jung Yan Li Yonghong Yan Meng-Qiu Dong Ho Yi Mak |
| author_sort | Jimmy H. Mo |
| collection | DOAJ |
| description | Summary: Vitellogenin is thought to share a common ancestor with human apolipoprotein B (ApoB) for systemic lipid transport. In Caenorhabditis elegans, although a general route for inter-tissue vitellogenin transport has been described, the full mechanism that underlies its intracellular trafficking within the intestine remains obscure. In humans, the TANGO1 family of proteins generates membrane carriers to accommodate bulky ApoB-containing lipoprotein particles for their endoplasmic reticulum (ER) export. TANGO1 orthologs have hitherto been discovered in most metazoans, except nematodes. Here, we report the C. elegans TNGL-1 as a mediator of vitellogenin export from the ER. Depletion of TNGL-1 causes the retention of vitellogenin in the ER lumen. Furthermore, the TNGL-1 C-terminal unstructured domain and its luminal globular domain are required for its proper localization and cargo engagement, respectively. Our findings support TNGL-1 as a distant TANGO1 family member and point to the universal requirement of TANGO1-based mechanisms for the secretion of specific metazoan proteins. |
| format | Article |
| id | doaj-art-fb875c6fadf2435c87723be666258f8f |
| institution | Kabale University |
| issn | 2589-0042 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj-art-fb875c6fadf2435c87723be666258f8f2025-02-02T05:29:10ZengElsevieriScience2589-00422025-02-01282111860A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegansJimmy H. Mo0Chao Zhai1Kwangsek Jung2Yan Li3Yonghong Yan4Meng-Qiu Dong5Ho Yi Mak6Division of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, ChinaNational Institute of Biological Sciences, Beijing, China; Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing 100084, ChinaDivision of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, ChinaDivision of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, ChinaNational Institute of Biological Sciences, Beijing, China; Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing 100084, ChinaNational Institute of Biological Sciences, Beijing, China; Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University, Beijing 100084, ChinaDivision of Life Science, The Hong Kong University of Science and Technology, Hong Kong SAR, China; Corresponding authorSummary: Vitellogenin is thought to share a common ancestor with human apolipoprotein B (ApoB) for systemic lipid transport. In Caenorhabditis elegans, although a general route for inter-tissue vitellogenin transport has been described, the full mechanism that underlies its intracellular trafficking within the intestine remains obscure. In humans, the TANGO1 family of proteins generates membrane carriers to accommodate bulky ApoB-containing lipoprotein particles for their endoplasmic reticulum (ER) export. TANGO1 orthologs have hitherto been discovered in most metazoans, except nematodes. Here, we report the C. elegans TNGL-1 as a mediator of vitellogenin export from the ER. Depletion of TNGL-1 causes the retention of vitellogenin in the ER lumen. Furthermore, the TNGL-1 C-terminal unstructured domain and its luminal globular domain are required for its proper localization and cargo engagement, respectively. Our findings support TNGL-1 as a distant TANGO1 family member and point to the universal requirement of TANGO1-based mechanisms for the secretion of specific metazoan proteins.http://www.sciencedirect.com/science/article/pii/S2589004225001208cell biologyfunctional aspects of cell biology |
| spellingShingle | Jimmy H. Mo Chao Zhai Kwangsek Jung Yan Li Yonghong Yan Meng-Qiu Dong Ho Yi Mak A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans iScience cell biology functional aspects of cell biology |
| title | A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans |
| title_full | A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans |
| title_fullStr | A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans |
| title_full_unstemmed | A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans |
| title_short | A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans |
| title_sort | distant tango1 family member promotes vitellogenin export from the er in c elegans |
| topic | cell biology functional aspects of cell biology |
| url | http://www.sciencedirect.com/science/article/pii/S2589004225001208 |
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