StAR-related lipid transfer protein 3

Definition:

Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes. Creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB. Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes. May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane. However, such results need additional experimental evidences; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes. Does not activate transcriptional cholesterol sensing. Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina.

References:

[1]. Maarit Hölttä-Vuori, et al. MLN64 is involved in actin-mediated dynamics of late endocytic organelles. Mol Biol Cell. 2005 Aug;16(8):3873-86. [Content Brief]

[2]. Mei Zhang, et al. MLN64 mediates mobilization of lysosomal cholesterol to steroidogenic mitochondria. J Biol Chem. 2002 Sep 6;277(36):33300-10. [Content Brief]

[3]. Binxing Li, et al. Identification of StARD3 as a lutein-binding protein in the macula of the primate retina. Biochemistry. 2011 Apr 5;50(13):2541-9. [Content Brief]

[4]. Fabien Alpy, et al. STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER. J Cell Sci. 2013 Dec 1;126(Pt 23):5500-12. [Content Brief]

[5]. Anastasia Liapis, et al. MLN64 transport to the late endosome is regulated by binding to 14-3-3 via a non-canonical binding site. PLoS One. 2012;7(4):e34424. [Content Brief]

[6]. F Alpy, et al. The steroidogenic acute regulatory protein homolog MLN64, a late endosomal cholesterol-binding protein. J Biol Chem. 2001 Feb 9;276(6):4261-9. [Content Brief]

[7]. Léa P Wilhelm, et al. STARD3 mediates endoplasmic reticulum-to-endosome cholesterol transport at membrane contact sites. EMBO J. 2017 May 15;36(10):1412-1433. [Content Brief]

[8]. Mark Charman, et al. MLN64 mediates egress of cholesterol from endosomes to mitochondria in the absence of functional Niemann-Pick Type C1 protein. J Lipid Res. 2010 May;51(5):1023-34. [Content Brief]

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