STARD10 binds LPCAT1 and PC

Stable Identifier
R-HSA-8873923
Type
Reaction [binding]
Species
Homo sapiens
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The steroidogenic acute regulatory (StAR) protein-related lipid transfer (START) domain proteins constitute a family of evolutionarily conserved and widely expressed proteins that have been implicated in lipid transport, metabolism, and signaling. Human PCTP-like protein (STARD10) (Olayioye et al. 2005) is thought to be a dual specificity lipid transfer protein capable of shuttling phosphatidylcholine (PC) (and phosphatidylethanolamine (PE), not shown here) between intracellular membranes, especially to lamellar body membranes. Saturated PC is a major component of pulmonary surfactant, a mixture of proteins and phospholipids that plays an important role in facilitating gas exchange by maintaining alveolar stability. After synthesis in the endoplasmic reticulum, saturated PC is transported to lamellar bodies (LBs) for storage prior to secretion. Lysophosphatidylcholine acyltransferase 1 (LPCAT1) mediated reacylation is a final step in saturated PC synthesis prior to transport and LPCAT1 is proposed to form a complex with STARD10 at the ER membrane to facilitate the synthesis then transport of saturated PC to LBs (Lin et al. 2015).

Literature References
PubMed ID Title Journal Year
15911624 StarD10, a START domain protein overexpressed in breast cancer, functions as a phospholipid transfer protein

Olayioye, MA, Vehring, S, Müller, P, Herrmann, A, Schiller, J, Thiele, C, Lindeman, GJ, Visvader, JE, Pomorski, T

J. Biol. Chem. 2005
26048993 Lysophosphatidylcholine Acyltransferase 1 (LPCAT1) Specifically Interacts with Phospholipid Transfer Protein StarD10 to Facilitate Surfactant Phospholipid Trafficking in Alveolar Type II Cells

Lin, S, Ikegami, M, Moon, C, Naren, AP, Shannon, JM

J. Biol. Chem. 2015
17561512 Phosphorylation of StarD10 on serine 284 by casein kinase II modulates its lipid transfer activity

Olayioye, MA, Buchholz, M, Schmid, S, Schoffler, P, Hoffmann, P, Pomorski, T

J. Biol. Chem. 2007
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