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.
Highlights
The steroidogenic acute regulatory protein-related lipid transfer (START) Domain Protein FamilyLipids are currently recognized as versatile and dynamic regulators of various cellular processes such as growth, development, survival, intracellular signaling, and membrane trafficking
Synthesis and secretion after StarD7 silencing is consistent with the finding that high hCG production and secretion are associated with several pathological alterations in syncytiotrophoblast function [92,93]. These results indicate that dysregulation of StarD7 expression could result in altered trophoblast function or differentiation, leading to an increased risk of placental disorders
StarD7 is a member of the START domain superfamily, which is involved in various physiological processes such as lipid transfer, metabolism, and modulation of signaling pathways
Summary
Lipids are currently recognized as versatile and dynamic regulators of various cellular processes such as growth, development, survival, intracellular signaling, and membrane trafficking. The typical START domain folds into a helix-grip structure with α-helices at the amino and carboxy termini separated by 9 β-sheets and 2 α-helices forming a hydrophobic pocket for binding sterols and other lipids [6,11]. Based on their phylogenetic relationships, the 15 well-characterized mammalian START domain-containing proteins are grouped into six subfamilies [3,12]. The first member of the family to be reported was the steroidogenic acute regulatory protein (StAR/StarD1), which transfers cholesterol to the mitochondria in steroid-producing cells [13]. We summarize the current state of knowledge in StarD7 research, focusing on the molecular characteristics, protein-lipid interactions, and mechanisms that regulate StarD7 expression
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