Please use this identifier to cite or link to this item: https://doi.org/10.7554/eLife.51401
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dc.titleMovement of accessible plasma membrane cholesterol by GRAMD1 lipid transfer protein complex
dc.contributor.authorNaito, T
dc.contributor.authorErcan, B
dc.contributor.authorKrshnan, L
dc.contributor.authorTriebl, A
dc.contributor.authorKoh, DHZ
dc.contributor.authorWei, FY
dc.contributor.authorTomizawa, K
dc.contributor.authorTorta, FT
dc.contributor.authorWenk, MR
dc.contributor.authorSaheki, Y
dc.date.accessioned2020-06-18T04:53:47Z
dc.date.available2020-06-18T04:53:47Z
dc.date.issued2019-11-01
dc.identifier.citationNaito, T, Ercan, B, Krshnan, L, Triebl, A, Koh, DHZ, Wei, FY, Tomizawa, K, Torta, FT, Wenk, MR, Saheki, Y (2019-11-01). Movement of accessible plasma membrane cholesterol by GRAMD1 lipid transfer protein complex. eLife 8. ScholarBank@NUS Repository. https://doi.org/10.7554/eLife.51401
dc.identifier.issn2050084X
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/170366
dc.description.abstract© 2019, eLife Sciences Publications Ltd. All rights reserved. Cholesterol is a major structural component of the plasma membrane (PM). The majority of PM cholesterol forms complexes with other PM lipids, making it inaccessible for intracellular transport. Transition of PM cholesterol between accessible and inaccessible pools maintains cellular homeostasis, but how cells monitor PM cholesterol accessibility remains unclear. We show that endoplasmic reticulum (ER)-anchored lipid transfer proteins, the GRAMD1s, sense and transport accessible PM cholesterol to the ER. GRAMD1s bind one another and populate at ER-PM contacts by sensing a transient expansion of the accessible pool of PM cholesterol via GRAM domains and facilitate its transport via StART-like domains. Cells lacking all three GRAMD1s exhibit striking expansion of the accessible pool of PM cholesterol due to less efficient PM to ER transport of accessible cholesterol. Thus, GRAMD1s facilitate movement of accessible PM cholesterol to the ER in order to counteract acute increase of PM cholesterol, activating non-vesicular cholesterol transport.
dc.publishereLife Sciences Publications, Ltd
dc.sourceElements
dc.subjectGRAM domain
dc.subjectStART-like domain
dc.subjectbiochemistry
dc.subjectcell biology
dc.subjectchemical biology
dc.subjectcholesterol
dc.subjecthuman
dc.subjectmembrane contact sites
dc.subjectnon-vesicular lipid transport
dc.subjectplasma membrane
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBiological Transport
dc.subjectCOS Cells
dc.subjectCarrier Proteins
dc.subjectCell Membrane
dc.subjectChlorocebus aethiops
dc.subjectCholesterol
dc.subjectEndoplasmic Reticulum
dc.subjectHeLa Cells
dc.subjectHumans
dc.subjectMultiprotein Complexes
dc.subjectMutant Proteins
dc.subjectProtein Binding
dc.subjectProtein Domains
dc.subjectSirolimus
dc.subjectSphingomyelins
dc.typeArticle
dc.date.updated2020-06-17T04:02:16Z
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.7554/eLife.51401
dc.description.sourcetitleeLife
dc.description.volume8
dc.published.statePublished
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