5TOD
Transmembrane protein 24 SMP domain
Summary for 5TOD
| Entry DOI | 10.2210/pdb5tod/pdb |
| Descriptor | Transmembrane protein 24 (1 entity in total) |
| Functional Keywords | lipid transfer protein, smp, membrane contact sites, lipid transport |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 6 |
| Total formula weight | 126355.56 |
| Authors | Lees, J.A.,Reinisch, K.M. (deposition date: 2016-10-17, release date: 2017-03-01, Last modification date: 2024-11-13) |
| Primary citation | Lees, J.A.,Messa, M.,Sun, E.W.,Wheeler, H.,Torta, F.,Wenk, M.R.,De Camilli, P.,Reinisch, K.M. Lipid transport by TMEM24 at ER-plasma membrane contacts regulates pulsatile insulin secretion. Science, 355:-, 2017 Cited by PubMed Abstract: 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)P] precursor phosphatidylinositol between bilayers, allowing replenishment of PI(4,5)P 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. PubMed: 28209843DOI: 10.1126/science.aah6171 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.96 Å) |
Structure validation
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