Clustered hydrophobic amino acids in amphipathic helices mediate erlin1/2 complex assembly

Biochemical and Biophysical Research Communications

Volumn 415, Issue 1, 2011, Pages 135-140

  Pednekar, Deepa ^a   Wang, Yuan ^a   Fedotova, Tatyana V ^a   Wojcikiewicz, Richard J H ^a  

^a State University of New York Upstate Medical University: College of Medicine   (United States)

Author keywords

Amphipathic helix; Assembly; Crosslinking; Erlin1; Erlin2

Indexed keywords

AMINO ACID; ERLIN1 PROTEIN; ERLIN2 PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CROSS LINKING; FEMALE; HUMAN; HUMAN CELL; HYDROPHOBICITY; MOLECULAR MODEL; MUTAGENESIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; HELA CELLS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MEMBRANE PROTEINS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY;

EID: 80755175760     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.10.032     Document Type: Article

References (27)

1. Browman D.T., Hoegg M.B., Robbins S.M. The SPFH domain-containing proteins: more than lipid raft markers. Trends Cell Biol. 2007, 17:394-402.
2. Tavernarakis N., Driscoll M., Kyrpides N.C. The SPFH domain: implicated in regulating targeted protein turnover in stomatins and other membrane-associated proteins. Trends Biochem. Sci. 1999, 24:425-427.
3. Morrow I.C., Parton R.G. Flotillins and the PHB domain family proteins: rafts, worms and anaesthetics. Traffic 2005, 6:725-740.
4. L. Lapatsina, J. Brand, K. Poole, et al., Stomatin-domain proteins, Eur. J. Cell Biol. (2011) in press.
5. Merkwirth C., Langer T. Prohibitin function within mitochondria: essential roles for cell proliferation and cristae morphogenesis. Biochim. Biophys. Acta 2009, 1793:27-32.
6. Pearce M.M.P., Wormer D.B., Wilkens S., et al. An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. J. Biol. Chem. 2009, 284:10433-10445.
7. Wojcikiewicz R.J.H., Pearce M.M.P., Sliter D.A., et al. When worlds collide: IP3 receptors and the ERAD pathway. Cell Calcium 2009, 46:147-153.
8. Vembar S.S., Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 2008, 9:944-957.
9. Wang Y., Pearce M.M.P., Sliter D.A., et al. SPFH1 and SPFH2 mediate the ubiquitination and degradation of inositol 1,4,5-trisphosphate receptors in muscarinic receptor-expressing HeLa cells. Biochim. Biophys. Acta 2009, 1793:1710-1718.
10. Lu J.P., Wang Y., Sliter D.A., et al. RNF170, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. J. Biol. Chem. 2011, 286:24426-24433.
11. Jo Y., Sguigna P.V., DeBose-Boyd R.A. Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 2011, 286:15022-15031.
12. Hoegg M.B., Browman D.T., Resek M.E., et al. Distinct regions within the erlins are required for oligomerization and association with high molecular weight complexes. J. Biol. Chem. 2009, 284:7766-7776.
13. Snyers L., Umlauf E., Prohaska R. Oligomeric nature of the integral membrane protein stomatin. J. Biol. Chem. 1998, 273:17221-17226.
14. Umlauf E., Mairhofer M., Prohaska R. Characterization of the stomatin domain involved in homo-oligomerization and lipid raft association. J. Biol. Chem. 2006, 281:23349-23356.
15. Back J.W., Artal Sanz M., De Jong L., et al. A structure for the yeast prohibitin complex: structure prediction and evidence from chemical crosslinking and mass spectrometry. Protein Sci. 2002, 11:2471-2478.
16. Tatsuta T., Model K., Langer T. Formation of membrane-bound ring complexes by prohibitins in mitochondria. Mol. Biol. Cell 2005, 16:248-259.
17. Salzer U., Prohaska R. Stomatin, flotillin-1 and flotillin-2 are major integral proteins of erythrocyte lipid rafts. Blood 2001, 97:1141-1143.
18. Sliter D.A., Kubota K., Kirkpatrick D.S., et al. Mass spectral analysis of type I inositol 1,4,5-trisphosphate receptor ubiquitination. J. Biol. Chem. 2008, 283:35319-35328.
19. Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157:105-132.
20. Krause F. Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (membrane) protein complexes and supercomplexes. Electrophoresis 2006, 27:2759-2781.
21. Pace C.N., Scholtz J.M. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 1998, 75:422-427.
22. Solis G.P., Hoegg M., Munderloh C., et al. Reggie/flotillin proteins are organized into stable tetramers in membrane microdomains. Biochem. J. 2007, 403:313-322.
23. Yokoyama H., Fujii S., Matsui I. Crystal structure of a core domain of stomatin from Pyrococcus horikoshii illustrates a novel trimeric and coiled-coil fold. J. Mol. Biol. 2008, 376:868-878.
24. Keskin O., Gursoy A., Ma B., et al. Principles of protein-protein interactions: what are the preferred ways for proteins to interact?. Chem. Rev. 2008, 108:1225-1244.
25. Chelli R., Gervasio L., Procacci P., et al. Stacking and T-shape competition in aromatic-aromatic amino acid interactions. J. Am. Chem. Soc. 2002, 124:6133-6143.
26. Lanzarotti E., Biekofsky R.R., Estrin D.A., et al. Aromatic-aromatic interactions in proteins: beyond the dimer. J. Chem. Inf. Model. 2011, 51:1623-1633.
27. Yildirim Y., Orhan E.K., Iseri S.A.U., et al. A frameshift mutation of ERLIN2 in recessive intellectual disability, motor dysfunction and multiple joint contactures. Hum. Mol. Genet. 2011, 20:1886-1892.