C2CD2L, also known as TMEM24 or DLNB23, is an endoplasmic reticulum (ER) protein that localizes on sites of contact between the endoplasmic reticulum and the cell membrane. The reversible localization is regulated by phosphorylation and dephosphorylation in response to oscillations in cytosolic calcium. TMEM24 protein plays a key role in the coordination of Ca2+ and phosphoinositide signaling. Molecular analysis of TMEM24 identifies it as a pancreatic islet enriched protein that plays a key role in regulating glucose-sensitive insulin release from the reserve pool of granules.
|Basic Information of C2CD2L|
|Protein Name||Phospholipid transfer protein C2CD2L|
|Organism||Homo sapiens (Human)|
TMEM24 is reversibly located on the sites of contact between the endoplasmic reticulum and the cell membrane, tethering the two bilayers. It plays a key role in the coordination of Ca2+ and phosphoinositide signaling. It can transport phosphatidylinositol from its site of synthesis in the endoplasmic reticulum to the cell membrane. In response to increase of cytosolic Ca2+, TMEM24 is phosphorylated and separated from the cell membrane, thereby disrupting the transport of phosphatidylinositol to the cell membrane. In insulin-secreting cells, TMEM24 positively regulates insulin secretion in response to glucose by coordinating Ca2+ and phosphoinositide signaling.
Fig.1 TMEM24 activity cycle at ER-PM contacts. (Lees, 2017)
This article demonstrates that TMEM24 participates in regulating insulin secretion by coordinating Ca2+ and phosphoinositide signaling pathways in insulin-secreting cells.
This study reveals that TMEM24 is abundant in neurons compared with glial cells and its levels increase as neuronal differentiation.
This investigation demonstrates that TMEM24 is involved in the glucose-stimulated insulin secretion from a reserve pool of granules and provides an insulin-secreting pathway within cells.
This article is the first report on identification and characterization of the TMEM24 family.
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