Structural insights into nonvesicular lipid transport by the oxysterol binding protein homologue family
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- 作者：Junsen Tong ; Mohammad Kawsar Manik ; Huiseon Yang ; Young Jun Im ; imyoungjun@jnu.ac.kr" class="auth_mail" title="E-mail the corresponding author
- 关键词：CERT ; ceramide transfer protein ; ER ; endoplasmic reticulum ; FFAT ; two phenylalanines in an acidic tract ; LE ; late endosome ; LTP ; lipid transfer protein ; MCS ; membrane contact site ; OSBP ; oxysterol-binding protein ; ORP ; OSBP-related protein ; ORD ; OSBP-related domain ; PC ; phosphatidylcholine ; PH ; pleckstrin homology ; PI ; phosphatidylinositol ; PM ; plasma membrane ; PI(4)P ; phosphatidylinositol 4-phosphate ; PS ; phosphatidylserine ; VAP ; vesicle-associated membrane protein (VAMP)-binding protein
- 刊名：Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids
- 出版年：2016
- 出版时间：August 2016
- 年：2016
- 卷：1861
- 期：8
- 页码：928-939
- 全文大小：1689 K
文摘
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Oxysterol-binding protein (OSBP) family proteins are involved in intracellular lipid transport and cell signaling.
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Significant advances have been made in understanding the structure and function of this protein family.
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The structures of OSBPs are composed of a conserved lipid-binding domain and additional targeting modules.
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The unique structural features of ORPs correlate with the PI(4)P-coupled lipid transport optimized in membrane contact sites.