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The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles

Nature Structural & Molecular Biology volume 13, pages 555–556 (2006)Cite this article

Abstract

The exocyst is a conserved protein complex essential for trafficking secretory vesicles to the plasma membrane. The structure of the C-terminal domain of the exocyst subunit Sec6p reveals multiple helical bundles, which are structurally and topologically similar to Exo70p and the C-terminal domains of Exo84p and Sec15, despite <10% sequence identity. The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins.

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Figure 1: Structure of the Sec6p C-terminal domain.
Figure 2: Sec6CT2 contains a similar helical-bundle motif to those of Exo70p, Exo84CT and Sec15CT.

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References

  1. Bonifacino, J.S. & Glick, B.S. Cell 116, 153–166 (2004).

    Article  CAS  Google Scholar 

  2. TerBush, D.R., Maurice, T., Roth, D. & Novick, P. EMBO J. 15, 6483–6494 (1996).

    Article  CAS  Google Scholar 

  3. Hsu, S.C. et al. Neuron 17, 1209–1219 (1996).

    Article  CAS  Google Scholar 

  4. Sivaram, M.V., Saporita, J.A., Furgason, M.L., Boettcher, A.J. & Munson, M. Biochemistry 44, 6302–6311 (2005).

    Article  CAS  Google Scholar 

  5. Guo, W., Roth, D., Walch-Solimena, C. & Novick, P. EMBO J. 18, 1071–1080 (1999).

    Article  CAS  Google Scholar 

  6. Vega, I.E. & Hsu, S.C. J. Neurosci. 21, 3839–3848 (2001).

    Article  CAS  Google Scholar 

  7. Matern, H.T., Yeaman, C., Nelson, W.J. & Scheller, R.H. Proc Natl. Acad. Sci. USA 98, 9648–9653 (2001).

    Article  CAS  Google Scholar 

  8. Dong, G., Hutagalung, A.H., Fu, C., Novick, P. & Reinisch, K.M. Nat. Struct. Mol. Biol. 12, 1094–1100 (2005).

    Article  CAS  Google Scholar 

  9. Lamping, E. et al. Gene 361, 57–66 (2005).

    Article  CAS  Google Scholar 

  10. Novick, P., Field, C. & Schekman, R. Cell 21, 205–215 (1980).

    Article  CAS  Google Scholar 

  11. Wu, S., Mehta, S.Q., Pichaud, F., Bellen, H.J. & Quiocho, F.A. Nat. Struct. Mol. Biol. 12, 879–885 (2005).

    Article  CAS  Google Scholar 

  12. Hamburger, Z.A., Hamburger, A.E., West, A.P. & Weis, W.I. J. Mol. Biol. 356, 9–21 (2006).

    Article  CAS  Google Scholar 

  13. Hsu, S.C. et al. Neuron 20, 1111–1122 (1998).

    Article  CAS  Google Scholar 

  14. Whyte, J.R. & Munro, S. J. Cell Sci. 115, 2627–2637 (2002).

    CAS  Google Scholar 

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Acknowledgements

We are grateful to S. Ryder, W. Royer, W. Kobertz and R. Gilmore for critical reading of this manuscript and discussions. Thanks to the staff at the X25 and X29 beamlines at the National Synchrotron Light Source and to D. Lambright, B. van den Berg, S. Eathiraj and members of the Lambright laboratory for help with structure determination. This work was supported by US National Institutes of Health grant GM068803 to M.M. and an American Heart Association award to M.V.S.S.

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  1. Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, 01605, Massachusetts, USA

    Mylavarapu V S Sivaram, Melonnie L M Furgason, Daniel N Brewer & Mary Munson

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  1. Mylavarapu V S Sivaram
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  2. Melonnie L M Furgason
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  3. Daniel N Brewer
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  4. Mary Munson
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Correspondence to Mary Munson.

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Supplementary information

Supplementary Fig. 1

The C-terminal domain of Sec6p is essential and binds Exo70p and Sec10p (PDF 2246 kb)

Supplementary Fig. 2

Final model and electron density map (PDF 1866 kb)

Supplementary Fig. 3

Packing of Sec6CT2 in the crystal (PDF 1100 kb)

Supplementary Fig. 4

Structure-based sequence alignment of Sec6CT2 (PDF 415 kb)

Supplementary Fig. 5

Sec6CT2, Exo70p, Exo84CT and Sec15CT have distinct surface features (PDF 2657 kb)

Supplementary Fig. 6

Secondary structure prediction profiles (PDF 29 kb)

Supplementary Table 1

Data collection and refinement statistics (PDF 96 kb)

Supplementary Methods (PDF 125 kb)

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Sivaram, M., Furgason, M., Brewer, D. et al. The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles. Nat Struct Mol Biol 13, 555–556 (2006). https://doi.org/10.1038/nsmb1096

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