Please use this identifier to cite or link to this item: https://doi.org/10.1126/science.aah6171
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dc.titleLipid transport by TMEM24 at ER-plasma membrane contacts regulates pulsatile insulin secretion
dc.contributor.authorLees, Joshua A
dc.contributor.authorMessa, Mirko
dc.contributor.authorSun, Elizabeth Wen
dc.contributor.authorWheeler, Heather
dc.contributor.authorTorta, Federico
dc.contributor.authorWenk, Markus R
dc.contributor.authorDe Camilli, Pietro
dc.contributor.authorReinisch, Karin M
dc.date.accessioned2020-08-21T04:58:49Z
dc.date.available2020-08-21T04:58:49Z
dc.date.issued2017-02-17
dc.identifier.citationLees, Joshua A, Messa, Mirko, Sun, Elizabeth Wen, Wheeler, Heather, Torta, Federico, Wenk, Markus R, De Camilli, Pietro, Reinisch, Karin M (2017-02-17). Lipid transport by TMEM24 at ER-plasma membrane contacts regulates pulsatile insulin secretion. SCIENCE 355 (6326). ScholarBank@NUS Repository. https://doi.org/10.1126/science.aah6171
dc.identifier.issn00368075
dc.identifier.issn10959203
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/173253
dc.description.abstractCopyright 2016 by the American Association for the Advancement of Science; all rights reserved. Insulin is released by β cells in pulses regulated by calcium and phosphoinositide signaling. Here, we describe how transmembrane protein 24 (TMEM24) helps coordinate these signaling events. We showed that TMEM24 is an endoplasmic reticulum (ER)-anchored membrane protein whose reversible localization to ER-plasma membrane (PM) contacts is governed by phosphorylation and dephosphorylation in response to oscillations in cytosolic calcium. A lipid-binding module in TMEM24 transports the phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] precursor phosphatidylinositol between bilayers, allowing replenishment of PI(4,5)P2 hydrolyzed during signaling. In the absence of TMEM24, calcium oscillations are abolished, leading to a defect in triggered insulin release. Our findings implicate direct lipid transport between the ER and the PM in the control of insulin secretion, a process impaired in patients with type II diabetes.
dc.language.isoen
dc.publisherAMER ASSOC ADVANCEMENT SCIENCE
dc.sourceElements
dc.subjectScience & Technology
dc.subjectMultidisciplinary Sciences
dc.subjectScience & Technology - Other Topics
dc.subjectBINDING PROTEINS
dc.subjectPHOSPHATIDYLSERINE TRANSPORT
dc.subjectCALCIUM OSCILLATIONS
dc.subjectTULIP SUPERFAMILY
dc.subjectSMP DOMAINS
dc.subjectEXCHANGE
dc.subjectPHOSPHOLIPIDS
dc.subjectSITES
dc.subjectPHOSPHORYLATION
dc.subjectIDENTIFICATION
dc.typeArticle
dc.date.updated2020-06-17T03:31:22Z
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.description.doi10.1126/science.aah6171
dc.description.sourcetitleSCIENCE
dc.description.volume355
dc.description.issue6326
dc.published.statePublished
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