Int. J. Mol. Sci. 2013, 14(3), 6170-6186; doi:10.3390/ijms14036170

The Lipid Transfer Protein StarD7: Structure, Function, and Regulation

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Received: 7 December 2012; in revised form: 17 February 2013 / Accepted: 22 February 2013 / Published: 18 March 2013
(This article belongs to the Special Issue Phospholipids: Molecular Sciences 2012)
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Abstract: 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. The 15 well-characterized mammalian START domain-containing proteins are grouped into six subfamilies. The START domain containing 7 mRNA encodes StarD7, a member of the StarD2/phosphatidylcholine transfer protein (PCTP) subfamily, which was first identified as a gene overexpressed in a choriocarcinoma cell line. Recent studies show that the StarD7 protein facilitates the delivery of phosphatidylcholine to the mitochondria. This review summarizes the latest advances in StarD7 research, focusing on the structural and biochemical features, protein-lipid interactions, and mechanisms that regulate StarD7 expression. The implications of the role of StarD7 in cell proliferation, migration, and differentiation are also discussed.
Keywords: StarD7; START domain; SF-1; b-catenin; ABCG2; cell migration; cell proliferation
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MDPI and ACS Style

Flores-Martin, J.; Rena, V.; Angeletti, S.; Panzetta-Dutari, G.M.; Genti-Raimondi, S. The Lipid Transfer Protein StarD7: Structure, Function, and Regulation. Int. J. Mol. Sci. 2013, 14, 6170-6186.

AMA Style

Flores-Martin J, Rena V, Angeletti S, Panzetta-Dutari GM, Genti-Raimondi S. The Lipid Transfer Protein StarD7: Structure, Function, and Regulation. International Journal of Molecular Sciences. 2013; 14(3):6170-6186.

Chicago/Turabian Style

Flores-Martin, Jésica; Rena, Viviana; Angeletti, Sofía; Panzetta-Dutari, Graciela M.; Genti-Raimondi, Susana. 2013. "The Lipid Transfer Protein StarD7: Structure, Function, and Regulation." Int. J. Mol. Sci. 14, no. 3: 6170-6186.

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