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REVIEW the Mammalian START Domain Protein Family in Lipid 257 REVIEW The mammalian START domain protein family in lipid transport in health and disease Barbara J Clark Department of Biochemistry and Molecular Biology, and the Center for Genetics and Molecular Medicine, School of Medicine, University of Louisville, Louisville, Kentucky 40292, USA (Correspondence should be addressed to B J Clark; Email: [email protected]) Abstract Lipid transfer proteins of the steroidogenic acute regulatory START domain protein family are not well established. protein-related lipid transfer (START) domain family are Recent research has focused on characterizing the cell-type defined by the presence of a conserved w210 amino acid distribution and regulation of the START proteins, examin- sequence that folds into an a/b helix-grip structure forming a ing the specificity and directionality of lipid transport, and hydrophobic pocket for ligand binding. The mammalian identifying disease states associated with dysregulation of START proteins bind diverse ligands, such as cholesterol, START protein expression. This review summarizes the oxysterols, phospholipids, sphingolipids, and possibly fatty current concepts of the proposed physiological and patho- acids, and have putative roles in non-vesicular lipid transport, logical roles for the mammalian START domain proteins in thioesterase enzymatic activity, and tumor suppression. cholesterol and lipid trafficking. However, the biological functions of many members of the Journal of Endocrinology (2012) 212, 257–275 Introduction organized membrane region for signaling and other functions (Lingwood & Simons 2010). Changes in ER membrane Lipid transport proteins play an important role in non- cholesterol levels signal for changes in gene expression leading vesicular trafficking of cholesterol, phospholipids, and to altered cholesterol metabolism while transport of sphingolipids between biological membranes to help maintain cholesterol to mitochondria is required for production of the proper cholesterol:phospholipid:sphingolipid distribution steroid hormones and bile acids. Thus, it has long been (reviewed in Prinz (2007) and Lev (2010)). Cholesterol appreciated that maintaining proper cholesterol distribution content is maintained at relatively low levels within the within the cell is important for cholesterol homeostasis and endoplasmic reticulum (ER) and mitochondrial membranes membrane function (Qin et al. 2006, Maxfield & van Meer compared with the plasma membrane (PM; Mesmin & 2010). There are two major gene families for lipid transfer Maxfield 2009). The source of PM cholesterol is from both proteins with specificity for sterols: the steroidogenic acute de novo synthesis in the ER and cellular uptake of low-density regulatory protein (StAR)-related lipid-transfer (START) lipoprotein (LDL)-derived cholesterol. De novo-synthesized domain family and the oxysterol-binding protein (OSBP) cholesterol is rapidly transferred to the PM by non-vesicular family, which includes the OSBP-related proteins (ORPs). trafficking mechanism(s), implicating a role for soluble sterol This review focuses on the role of the mammalian START transport proteins (Maxfield & van Meer 2010). Receptor- domain family in lipid trafficking and the implications for mediated endocytosis of LDL delivers lipoproteins to the late dysregulation of START protein expression in disease states. endosomes/lysosomes where free cholesterol is hydrolyzed The OSBP/ORP family has been reviewed by others (Prinz from cholesterol esters (Goldstein & Brown 2009). The free 2007, Ngo et al. 2010). cholesterol is recycled back to the PM or transported to the ER. In the PM, cholesterol can be found clustered with sphingolipids into detergent-resistant protein–lipid micro- The START domain protein family domains referred to as lipid rafts (Danielsen & Hansen 2003, Rajendran & Simons 2005, Hanzal-Bayer & Hancock The START domain is defined by a conserved sequence of 2007). Functionally, lipid rafts are proposed to provide an w210 amino acids that folds into an a/b helix-grip structure Journal of Endocrinology (2012) 212, 257–275 DOI: 10.1530/JOE-11-0313 0022–0795/12/0212–257 q 2012 Society for Endocrinology Printed in Great Britain Online version via http://www.endocrinology-journals.org Downloaded from Bioscientifica.com at 09/28/2021 06:46:29AM via free access 258 B J CLARK . Mammalian START protein functions forming a hydrophobic pocket for binding sterols and other mechanisms for cholesterol absorption/desorption have been lipids (Ponting & Aravind 1999, Iyer et al. 2001). The helix- reviewed elsewhere (Alpy & Tomasetto 2005, Miller 2007, grip fold is used to define a large superfamily of proteins Lavigne et al. 2010). that bind hydrophobic lipids, classified as the SRPBCC protein superfamily on NCBI’s Conserved Domain Data- base (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC, Cholesterol trafficking and homeostasis cl14643 NCBI; Marchler-Bauer et al. 2009). BLASTP searches have identified START domains in genomes from Intracellular cholesterol levels are tightly regulated by plants, bacteria, protists, and animals, but not in archaea or controlling biosynthetic and degradation pathways. There yeast (Schrick et al. 2004). START domains are relatively rare are several excellent reviews on cholesterol homeostasis and in bacteria and protist genomes, and to date, there is no cholesterol trafficking (Russell 2003, Soccio & Breslow 2004, evidence that these proteins are expressed. Proteins Prinz 2007, Brown & Goldstein 2009, Mesmin & Maxfield containing the START domain are most abundant in plants 2009, Maxfield & van Meer 2010, Wollam & Antebi 2011), and are highly represented in proteins that contain a and only a brief overview of these topics is provided to set the homeodomain, suggesting a role in transcription (Schrick cellular context for START protein function(s). The major et al. 2004). The homeodomain–START domain structure regulatory step for cholesterol biosynthesis is the expression has only been found in plant proteins. Coupling the START and activation of the enzyme HMG-CoA reductase domain with other motifs is, however, a common theme as (HMGR). HMGR transcription is controlled by sterol START domains in other phyla are found in multi-domain regulatory element-binding protein-2 (SREBP2), a member proteins that provide additional functions such as protein of the basic helix–loop–helix–leucine zipper (bHLH-Zip) localization, enzymatic activity, or signaling (Ponting & transcription factor family that is encoded by the SREBP2 Aravind 1999, Iyer et al. 2001). gene (Hua et al. 1993, Yokoyama et al. 1993, Sakai & Rawson The mammalian START domain protein family is well 2001). SREBP2, however, is a proteolytic fragment of a larger characterized and is composed of 15 members that group into transmembrane protein of the ER that forms a protein six subfamilies based on the sequence and ligand similarities complex composed of SREBP, SREBP-cleavage-activating (Ponting & Aravind 1999, Soccio et al. 2002; Table 1). In very protein (SCAP), and insulin-induced genes 1 and 2 (INSIGs) general terms, the subfamilies can be classified into that functions as a cellular cholesterol sensor. When ER cholesterol- and oxysterol binding proteins (STARD1/D3 cholesterol levels decline below some threshold level, and STARD4/D5/D6 subfamilies), the phospholipid- and SREBP-SCAP dissociates from INSIGs and moves to the sphingolipid-binding proteins (STARD2 (phosphatidyl- Golgi apparatus where two proteolytic cleavages releases a choline transfer protein, PCTP)/D7/D10/D11 subfamily), w50 kDa N-terminal fragment that translocates to the the multi-domain proteins containing either putative Rho- nucleus and activates target gene transcription (Anderson GTPase signaling function (STARD8/12/13 subfamily) or 2003; Fig. 1). Major target genes induced by SREBP2 in the thioesterase activity (STARD14/15 subfamily), and the liver are within the cholesterol biosynthetic pathway STARD9 subfamily composed of a single member of including HMGR and the LDL receptor (LDLR) (Horton unknown function that is not further discussed (Soccio et al. et al. 2003). A resulting increase in cholesterol synthesis 2002, Soccio & Breslow 2003, Alpy & Tomasetto 2005). The (HMGR) and uptake (LDLR) increases intracellular choles- crystal structures for the START domains of hSTARD3/ terol levels. The resulting increase in ER cholesterol stabilizes metastatic axillary lymph node 64 kDa protein (MLN64) and the INSIG-SCAP-SREBP2 complex within the ER and mSTARD4 were the first to be solved and showed an a/b thereby suppresses SREBP2 processing and subsequent helix-grip fold with a nine-stranded anti-parallel b-sheet transcriptional function(s). Cholesterol is also converted to forming a U-shaped hydrophobic cleft that binds the ligand cholesterol esters by acyl-CoA:cholesterol acyl transferase and is flanked by amino- and carboxyl-terminal a helices activity (ACAT), an enzyme localized to the ER. An increase (Tsujishita & Hurley 2000, Romanowski et al. 2002). The in ER cholesterol levels activates ACAT leading to increased carboxyl-terminal a helix is proposed to serve as a ‘cap’ to the cholesterol ester synthesis. ligand-binding site, with lipid access to the binding pocket Cholesterol metabolism to bile acids in the liver represents requiring a conformational change in the START domain the major route for cholesterol clearance. There are two and movement of the C-terminal helix (Baker et al. 2005, pathways for bile acid biosynthesis, the classical pathway that Bose et al. 2008a,b). To
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