Skip to main content
Log in

1H, 13C, and 15N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5)

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

Steroidogenic acute regulatory (StAR)—related lipid transfer proteins possess a START (steroidogenic acute regulatory-related lipid transfer) domain. START domains are conserved protein modules involved in the non-vesicular intracellular transport of lipids and cholesterol in mammals. Fifteen mammalian proteins, divided in five subfamilies, are reported to possess a START domain. Members of the STARD4 subfamily, i.e. STARD4, 5 and 6 are essentially single START domains and are thought to be involved in the intracellular transport of cholesterol. No structure of a cholesterol-bound START domain from this family has been resolved yet. The determination of the structure of such a complex would contribute to a better understanding of the mechanism of ligand binding and transport by START domains, two unresolved aspects of their structural biology. In this context, we have undertaken the structure determination of a ligand-bound form of STARD5 by NMR. Here, we report the 1H, 13C and 15N backbone resonance assignments of the ligand-free STARD5.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1

Similar content being viewed by others

References

  • Alpy F, Tomasetto C (2005) Give lipids a START: the StAR-related lipid transfer (START) domain in mammals. J Cell Sci 118:2791–2801

    Article  Google Scholar 

  • Clark BJ, Wells J, King SR, Stocco DM (1994) The purification, cloning, and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 mouse Leydig tumor cells. Characterization of the steroidogenic acute regulatory protein (StAR). J Biol Chem 269:28314–28322

    Google Scholar 

  • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293

    Article  Google Scholar 

  • Gardner KH, Rosen MK, Kay LE (1997) Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry 36:1389–1401

    Google Scholar 

  • Kudo N, Kumagai K, Matsubara R, Kobayashi S, Hanada K, Wakatsuki S, Kato R (2010) Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer. J Mol Biol 396:245–251

    Article  Google Scholar 

  • Lavigne P, Najmanovich R, LeHoux JG (2010) Mammalian StAR-related lipid transfer (START) domains with specificity for cholesterol: structural conservation and mechanism of reversible binding. Subcell Biochem 51:425–437

    Article  Google Scholar 

  • LeHoux JG, Mathieu A, Lavigne P, Fleury A (2003) Adrenocorticotropin regulation of steroidogenic acute regulatory protein. Microsc Res Tech 61:288–299

    Article  Google Scholar 

  • Mathieu AP, Fleury A, Ducharme L, Lavigne P, LeHoux JG (2002) Insights into steroidogenic acute regulatory protein (StAR)-dependent cholesterol transfer in mitochondria: evidence from molecular modeling and structure-based thermodynamics supporting the existence of partially unfolded states of StAR. J Mol Endocrinol 29:327–345

    Article  Google Scholar 

  • Roderick SL, Chan WW, Agate DS, Olsen LR, Vetting MW, Rajashankar KR, Cohen DE (2002) Structure of human phosphatidylcholine transfer protein in complex with its ligand. Nat Struct Biol 9:507–511

    Google Scholar 

  • Rodriguez-Agudo D, Ren S, Hylemon PB, Redford K, Natarajan R, Del Castillo A, Gil G, Pandak WM (2005) Human STARD5, a cytosolic StAR-related lipid binding protein. J Lipid Res 46:1615–1623

    Article  Google Scholar 

  • Romanowski MJ, Soccio RE, Breslow JL, Burley SK (2002) Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (STARD4) containing a StAR-related lipid transfer domain. Proc Natl Acad Sci USA 99:6949–6954

    Article  ADS  Google Scholar 

  • Soccio RE, Adams RM, Romanowski MJ, Sehayek E, Burley SK, Breslow JL (2002) The cholesterol-regulated STARD4 gene encodes a StAR-related lipid transfer protein with two closely related homologues, STARD5 and STARD6. Proc Natl Acad Sci USA 99:6943–6948

    Article  ADS  Google Scholar 

  • Thorsell AG, Lee WH, Persson C, Siponen MI, Nilsson M, Busam RD, Kotenyova T, Schüler H, Lethiö L (2011) Comparative Structural Analysis of Lipid Binding START Domains. PLoS ONE 6:e19521

    Article  ADS  Google Scholar 

  • Tsujishita Y, Hurley JH (2000) Structure and lipid transport mechanism of a StAR-related domain. Nat Struct Biol 7:408–414

    Article  Google Scholar 

  • Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59:687–696

    Article  Google Scholar 

  • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180

    Article  Google Scholar 

Download references

Acknowledgments

This work supported by a grant (MT-10983) to JGL and PL from the Canadian Institutes of Health Research. This work was also supported by the Regroupement Stratégique sur la Structure, la Fonction et l’Ingénierie des Protéines (PROTEO) and NSERC (PL). We would like to thank Dr Lari Lehtiö (Åbo Akademi University, Turku, Finland) for kindly providing us with the STARD5 cDNA.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Pierre Lavigne.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Lorin, A., Létourneau, D., Lefebvre, A. et al. 1H, 13C, and 15N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5). Biomol NMR Assign 7, 21–24 (2013). https://doi.org/10.1007/s12104-012-9368-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-012-9368-z

Keywords

Navigation