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. 2022 May 23;10(5):1201. doi: 10.3390/biomedicines10051201

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Cholesterol and phosphatidylinositol 4-phosphate (PI4P) are transported between the endoplasmic reticulum (ER) and the Golgi apparatus. To maintain PI4P levels associated with cholesterol transport, phosphatidylinositol (PI) is transferred through phosphatidylinositol transport protein β (PITPβ), while the OxySterol Binding Protein (OSBP)-Related Domain (ORD motif) of Oxysterol Binding Protein (OSBP) transports cholesterol from the ER to the Golgi membrane and reciprocal transport of PI4P from Golgi membrane to the ER. Association of these two membrane structures is achieved by the interaction of the two phenylalanines (FF) in an acidic tract (FFAT)-like motif of OSBP with vesicle-associated membrane protein-associated protein (VAP) in the ER, and pleckstrin homology domain (PH domain) from OSBP, which binds to PI4P at the Golgi.