Sec16A defines the site for vesicle budding from the endoplasmic reticulum on exit from mitosis

Journal of Cell Science

Volumn 123, Issue 23, 2010, Pages 4032-4038

  Hughes, Helen ^a   Stephens, David J ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

COPII; Golgi; Mitosis

Indexed keywords

PROTEIN; SEC16A PROTEIN; UNCLASSIFIED DRUG;

ANAPHASE; ARTICLE; CELL BUDDING; CELL VACUOLE; CONTROLLED STUDY; CYTOSOL; ENDOPLASMIC RETICULUM; FEMALE; GOLGI COMPLEX; HUMAN; HUMAN CELL; METAPHASE; MITOSIS; MOLECULAR IMAGING; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; TELOPHASE;

CYTOPLASMIC VESICLES; ENDOPLASMIC RETICULUM; GOLGI APPARATUS; HEK293 CELLS; HELA CELLS; HUMANS; MITOSIS; PROTEIN TRANSPORT; VESICULAR TRANSPORT PROTEINS;

EID: 78649742451     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.076000     Document Type: Article

References (35)

1. Altan-Bonnet, N., Sougrat, R., Liu, W., Snapp, E. L., Ward, T. and Lippincott-Schwartz, J. (2006). Golgi inheritance in mammalian cells is mediated through endoplasmic reticulum export activities. Mol. Biol. Cell 17, 990-1005.
2. Bartz, R., Sun, L. P., Bisel, B., Wei, J. H. and Seemann, J. (2008). Spatial separation of Golgi and ER during mitosis protects SREBP from unregulated activation. EMBO J. 27, 948-955.
3. Bhattacharyya, D. and Glick, B. S. (2007). Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization. Mol. Biol. Cell 18, 839-849.
4. Connerly, P. L., Esaki, M., Montegna, E. A., Strongin, D. E., Levi, S., Soderholm, J. and Glick, B. S. (2005). Sec16 is a determinant of transitional ER organization. Curr. Biol. 15, 1439-1447.
5. Corthesy-Theulaz, I., Pauloin, A. and Pfeffer, S. R. (1992). Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol. 118, 1333-1345.
6. Farmaki, T., Ponnambalam, S., Prescott, A. R., Clausen, H., Tang, B. L., Hong, W. and Lucocq, J. M. (1999). Forward and retrograde trafficking in mitotic animal cells. ER-Golgi transport arrest restricts protein export from the ER into COPII-coated structures. J. Cell Sci. 112, 589-600.
7. Hammond, A. T. and Glick, B. S. (2000). Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell 11, 3013-3030.
8. He, C. Y., Pypaert, M. and Warren, G. (2005). Golgi duplication in Trypanosoma brucei requires Centrin2. Science 310, 1196-1198.
9. Heinzer, S., Worz, S., Kalla, C., Rohr, K. and Weiss, M. (2008). A model for the self-organization of exit sites in the endoplasmic reticulum. J. Cell Sci. 121, 55-64.
10. Henderson, M. C., Shaw, Y. J., Wang, H., Han, H., Hurley, L. H., Flynn, G., Dorr, R. T. and Von Hoff, D. D. (2009). UA62784, a novel inhibitor of centromere protein E kinesin-like protein. Mol. Cancer Ther. 8, 36-44.
11. Ho, W. C., Allan, V. J., van Meer, G., Berger, E. G. and Kreis, T. E. (1989). Reclustering of scattered Golgi elements occurs along microtubules. Eur. J. Cell Biol. 48, 250-263.
12. Hughes, H. and Stephens, D. J. (2008). Assembly, organization, and function of the COPII coat. Histochem. Cell Biol. 129, 129-151.
13. Hughes, H., Budnik, A., Schmidt, K., Palmer, K. J., Mantell, J., Noakes, C., Johnson, A., Carter, D. A., Verkade, P., Watson, P. et al. (2009). Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER. J. Cell Sci. 122, 2924-2934.
14. Iinuma, T., Shiga, A., Nakamoto, K., O'Brien, M. B., Aridor, M., Arimitsu, N., Tagaya, M. and Tani, K. (2007). Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum. J. Biol. Chem. 282, 17632-17639.
15. Ivan, V., de Voer, G., Xanthakis, D., Spoorendonk, K. M., Kondylis, V. and Rabouille, C. (2008). Drosophila Sec16 mediates the biogenesis of tER sites upstream of Sar1 through an arginine-rich motif. Mol. Biol. Cell 19, 4352-4365.
16. Kredel, S., Oswald, F., Nienhaus, K., Deuschle, K., Rocker, C., Wolff, M., Heilker, R., Nienhaus, G. U. and Wiedenmann, J. (2009). mRuby, a bright monomeric red fluorescent protein for labeling of subcellular structures. PLoS ONE 4, e4391.
17. Kuge, O., Dascher, C., Orci, L., Rowe, T., Amherdt, M., Plutner, H., Ravazzola, M., Tanigawa, G., Rothman, J. E. and Balch, W. E. (1994). Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. J. Cell Biol. 125, 51-65.
18. Lucocq, J. M. and Warren, G. (1987). Fragmentation and partitioning of the Golgi apparatus during mitosis in HeLa cells. EMBO J. 6, 3239-3246.
19. Mayer, T. U., Kapoor, T. M., Haggarty, S. J., King, R. W., Schreiber, S. L. and Mitchison, T. J. (1999). Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 286, 971-974.
20. Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K. and Miyawaki, A. (2002). A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90.
21. Palmer, K. J., Hughes, H. and Stephens, D. J. (2009). Specificity of cytoplasmic dynein subunits in discrete membrane-trafficking steps. Mol. Biol. Cell 20, 2885-2899.
22. Prescott, A. R., Farmaki, T., Thomson, C., James, J., Paccaud, J. P., Tang, B. L., Hong, W., Quinn, M., Ponnambalam, S. and Lucocq, J. (2001). Evidence for prebudding arrest of ER export in animal cell mitosis and its role in generating Golgi partitioning intermediates. Traffic 2, 321-335.
23. Seemann, J., Pypaert, M., Taguchi, T., Malsam, J. and Warren, G. (2002). Partitioning of the matrix fraction of the Golgi apparatus during mitosis in animal cells. Science 295, 848-851.
24. Shima, D. T., Haldar, K., Pepperkok, R., Watson, R. and Warren, G. (1997). Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J. Cell Biol. 137, 1211-1228.
25. Souter, E., Pypaert, M. and Warren, G. (1993). The Golgi stack reassembles during telophase before arrival of proteins transported from the endoplasmic reticulum. J. Cell Biol. 122, 533-540.
26. Steegmaier, M., Hoffmann, M., Baum, A., Lenart, P., Petronczki, M., Krssak, M., Gurtler, U., Garin-Chesa, P., Lieb, S., Quant, J. et al. (2007). BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo. Curr. Biol. 17, 316-322.
27. Stephens, D. J. (2003). De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites. EMBO rep. 4, 210-217.
28. Storrie, B., White, J., Rottger, S., Stelzer, E. H., Suganuma, T. and Nilsson, T. (1998). Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 143, 1505-1521.
29. Supek, F., Madden, D. T., Hamamoto, S., Orci, L. and Schekman, R. (2002). Sec16p potentiates the action of COPII proteins to bud transport vesicles. J. Cell Biol. 158, 1029-1038.
30. Townley, A. K., Feng, Y., Schmidt, K., Carter, D. A., Porter, R., Verkade, P. and Stephens, D. J. (2008). Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development. J. Cell Sci. 121, 3025-3034.
31. Ward, T. H., Polishchuk, R. S., Caplan, S., Hirschberg, K. and Lippincott-Schwartz, J. (2001). Maintenance of Golgi structure and function depends on the integrity of ER export. J. Cell Biol. 155, 557-570.
32. Watson, P., Forster, R., Palmer, K. J., Pepperkok, R. and Stephens, D. J. (2005). Coupling of ER exit to microtubules through direct interaction of COPII with dynactin. Nat. Cell Biol. 7, 48-55.
33. Watson, P., Townley, A. K., Koka, P., Palmer, K. J. and Stephens, D. J. (2006). Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7, 1678-1687.
34. Wei, J. H. and Seemann, J. (2009). Mitotic division of the mammalian Golgi apparatus. Semin. Cell Dev. Biol. 20, 810-816.
35. Zaal, K. J., Smith, C. L., Polishchuk, R. S., Altan, N., Cole, N. B., Ellenberg, J., Hirschberg, K., Presley, J. F., Roberts, T. H., Siggia, E. et al. (1999). Golgi membranes are absorbed into and reemerge from the ER during mitosis. Cell 99, 589-601.