Connecting vesicular transport with lipid synthesis: FAPP2
| العنوان: | Connecting vesicular transport with lipid synthesis: FAPP2 |
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| المؤلفون: | Giovanni D'Angelo, Laura Rita Rega, GIOVANNI DANGELO, Maria Antonietta De Matteis |
| المساهمون: | D'Angelo, Giovanni, Rega, Laura Rita, DE MATTEIS, Maria Antonietta |
| المصدر: | Biochimica et Biophysica Acta Biochimica et biophysica acta. Molecular cell research 1821 (2012): 1089–-1095. doi:10.1016/j.bbalip.2012.01.003 info:cnr-pdr/source/autori:Giovanni D'Angelo, Laura Rita Rega, Maria Antonietta De Matteis/titolo:Connecting vesicular transport with lipid synthesis: FAPP2/doi:10.1016%2Fj.bbalip.2012.01.003/rivista:Biochimica et biophysica acta. Molecular cell research/anno:2012/pagina_da:1089/pagina_a:-1095/intervallo_pagine:1089–-1095/volume:1821 |
| بيانات النشر: | Elsevier BV, 2012. |
| سنة النشر: | 2012 |
| مصطلحات موضوعية: | Lipid transfer protein, Molecular Sequence Data, FAPP2, Golgi complex, Glycosphingolipid, Transport carrier, Gene Expression, Review, Biology, Glycosphingolipids, Cell membrane, symbols.namesake, medicine, Animals, Humans, Amino Acid Sequence, Transport Vesicles, Molecular Biology, Lipid raft, Secretory pathway, Adaptor Proteins, Signal Transducing, Animal, Cell Membrane, Biological Transport, Lipid metabolism, Cell Biology, Lipid, Golgi apparatus, Lipid Metabolism, Lipids, Membrane contact site, Protein Structure, Tertiary, Cell biology, Transport protein, Vesicular transport protein, medicine.anatomical_structure, Transport Vesicle, symbols, lipids (amino acids, peptides, and proteins), Sequence Alignment, Human, trans-Golgi Network |
| الوصف: | Next to the protein-based machineries composed of small G-proteins, coat complexes, SNAREs and tethering factors, the lipid-based machineries are emerging as important players in membrane trafficking. As a component of these machineries, lipid transfer proteins have recently attracted the attention of cell biologists for their involvement in trafficking along different segments of the secretory pathway. Among these, the four-phosphate adaptor protein 2 (FAPP2) was discovered as a protein that localizes dynamically with the trans-Golgi network and regulates the transport of proteins from the Golgi complex to the cell surface. Later studies have highlighted a role for FAPP2 as lipid transfer protein involved in glycosphingolipid metabolism at the Golgi complex. Here we discuss the available evidence on the function of FAPP2 in both membrane trafficking and lipid metabolism and propose a mechanism of action of FAPP2 that integrates its activities in membrane trafficking and in lipid transfer. This article is part of a Special Issue entitled Lipids and Vesicular Transport. Highlights ► FAPP2 contains a PtdIns4P (and ARF1) binding PH domain and a GLTP (Glycolipid Transfer Protein) domain. ► The FAPP2-PH domain targets the protein to the trans-Golgi network and has membrane bending activity. ► Via the GLTP domain FAPP2 transfers glucosylceramide and fosters complex glycolipid synthesis at the Golgi complex. ► FAPP2 controls TGN-to-plasma membrane vesicular trafficking by assisting the formation of post-Golgi carriers. ► The lipid-transfer activity of FAPP2 is required for its role in membrane trafficking. |
| تدمد: | 1388-1981 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1331b460548ad541d9256d7d97ab97c6Test https://doi.org/10.1016/j.bbalip.2012.01.003Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....1331b460548ad541d9256d7d97ab97c6 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 13881981 |
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