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SEC13  -  GTPase-activating protein SEC13

Saccharomyces cerevisiae S288c

Synonyms: ANU3, L8167.4, Protein transport protein SEC13, YLR208W
 
 
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Disease relevance of SEC13

  • Sec13 was expressed in Escherichia coli as a hexa-His-tagged protein (H6Sec13) and purified to homogeneity [1].
  • Antibodies raised against a C-terminal portion of Sec31A co-precipitate Sec13 and inhibit ER-Golgi transport of temperature-arrested vesicular stomatitis G protein in a semi-intact cell assay [2].
 

High impact information on SEC13

  • The five core COPII proteins (Sar1p, Sec23/24p, and Sec13/31p) act in concert to capture cargo proteins and sculpt the ER membrane into vesicles of defined geometry [3].
  • Thus, the Nup84p complex in conjunction with Sec13-type proteins is required for correct nuclear pore biogenesis [4].
  • COPII-coated vesicles form on the endoplasmic reticulum by the stepwise recruitment of three cytosolic components: Sar1-GTP to initiate coat formation, Sec23/24 heterodimer to select SNARE and cargo molecules, and Sec13/31 to induce coat polymerization and membrane deformation [5].
  • We show that a pool of green fluorescent protein-tagged Sec13p localizes to the nuclear pores in vivo, and identify sec13 mutant alleles that are synthetically lethal with nup85Delta and affect the localization of a green fluorescent protein-Nup49p reporter protein [6].
  • In the electron microscope, sec13 mutants exhibit structural defects in nuclear pore complex (NPC) and nuclear envelope organization [6].
 

Biological context of SEC13

  • The blockage of autophagy in these mutants was not dependent on transport from endoplasmic reticulum-to-Golgi, because mutations in two other COPII genes, SEC13 and SEC31, did not affect autophagy [7].
  • The SEC13 gene was originally identified by temperature-sensitive mutations that block all protein transport from the ER to the Golgi [8].
  • The SEC17 and SAR1 genes contain introns at the same relative positions in both P. pastoris and S. cerevisiae, whereas the SEC13 gene contains an intron in P. pastoris but not in S. cerevisiae [9].
  • The SEC13 gene of Saccharomyces cerevisiae is required in vesicle biogenesis at a step before or concurrent with the release of transport vesicles from the ER membrane [10].
  • Expression of SEC13 on a multicopy plasmid resulted in overproduction of a monomeric form of Sec13p, suggesting that another member of the complex becomes limiting when Sec13p is overproduced [10].
 

Anatomical context of SEC13

 

Associations of SEC13 with chemical compounds

  • Our finding, both in Gbeta and in Sec13, that no mutation of the conserved Asp entirely prevents folding suggests that there is no obligatory folding order for each repeat and that the folding order is probably not the same for different WD repeat proteins, or even necessarily constant for the same protein [12].
  • Folding a WD repeat propeller. Role of highly conserved aspartic acid residues in the G protein beta subunit and Sec13 [12].
  • We mutated each of these conserved Asp residues to Gly individually and in pairs in Gbeta and in Sec13, a yeast WD repeat protein involved in vesicular traffic, and then analyzed the ability of the mutant proteins to fold in vitro and in COS-7 cells [12].
  • In addition, cells expressing exogenous Sec13 showed giant nuclei compared to endogenous ones in the absence of nocodazole [15].
 

Physical interactions of SEC13

  • Recombinant production in baculovirus-infected insect cells and purification of the mammalian Sec13/Sec31 complex [16].
 

Other interactions of SEC13

  • Different alleles of SEC13 exhibit different relative effects on protein transport from the ER to the Golgi, or on Gap1p activity, indicating distinct requirements for SEC13 function at two different steps in the secretory pathway [8].
  • Sar1p GTPase activity was activated by the Sec23/24p GTPase-activating protein (GAP), and further accelerated 10-fold by Sec13/31p [17].
  • NO348 shows similarity with YCW2, TUP1 and SEC13 [18].
  • Formation of ER-derived protein transport vesicles requires three cytosolic components, a small GTPase, Sar1p, and two heterodimeric complexes, Sec23/24p and Sec13/31p, which comprise the COPII coat [19].
  • Deletion of PEP12, a gene required for vesicular transport from the Golgi to the prevacuolar compartment, counteracts the effect of the sec13 mutation and partially restores Gap1p transport to the plasma membrane [11].
 

Analytical, diagnostic and therapeutic context of SEC13

References

  1. Analysis of the physical properties and molecular modeling of Sec13: A WD repeat protein involved in vesicular traffic. Saxena, K., Gaitatzes, C., Walsh, M.T., Eck, M., Neer, E.J., Smith, T.F. Biochemistry (1996) [Pubmed]
  2. Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport. Tang, B.L., Zhang, T., Low, D.Y., Wong, E.T., Horstmann, H., Hong, W. J. Biol. Chem. (2000) [Pubmed]
  3. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Lee, M.C., Orci, L., Hamamoto, S., Futai, E., Ravazzola, M., Schekman, R. Cell (2005) [Pubmed]
  4. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Siniossoglou, S., Wimmer, C., Rieger, M., Doye, V., Tekotte, H., Weise, C., Emig, S., Segref, A., Hurt, E.C. Cell (1996) [Pubmed]
  5. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Bi, X., Corpina, R.A., Goldberg, J. Nature (2002) [Pubmed]
  6. Structure and assembly of the Nup84p complex. Siniossoglou, S., Lutzmann, M., Santos-Rosa, H., Leonard, K., Mueller, S., Aebi, U., Hurt, E. J. Cell Biol. (2000) [Pubmed]
  7. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Ishihara, N., Hamasaki, M., Yokota, S., Suzuki, K., Kamada, Y., Kihara, A., Yoshimori, T., Noda, T., Ohsumi, Y. Mol. Biol. Cell (2001) [Pubmed]
  8. Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8. Roberg, K.J., Bickel, S., Rowley, N., Kaiser, C.A. Genetics (1997) [Pubmed]
  9. Isolation of Pichia pastoris genes involved in ER-to-Golgi transport. Payne, W.E., Kaiser, C.A., Bevis, B.J., Soderholm, J., Fu, D., Sears, I.B., Glick, B.S. Yeast (2000) [Pubmed]
  10. Cytosolic Sec13p complex is required for vesicle formation from the endoplasmic reticulum in vitro. Pryer, N.K., Salama, N.R., Schekman, R., Kaiser, C.A. J. Cell Biol. (1993) [Pubmed]
  11. Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. Roberg, K.J., Rowley, N., Kaiser, C.A. J. Cell Biol. (1997) [Pubmed]
  12. Folding a WD repeat propeller. Role of highly conserved aspartic acid residues in the G protein beta subunit and Sec13. Garcia-Higuera, I., Gaitatzes, C., Smith, T.F., Neer, E.J. J. Biol. Chem. (1998) [Pubmed]
  13. COPII: a membrane coat that forms endoplasmic reticulum-derived vesicles. Barlowe, C. FEBS Lett. (1995) [Pubmed]
  14. A family of mammalian proteins homologous to yeast Sec24p. Tang, B.L., Kausalya, J., Low, D.Y., Lock, M.L., Hong, W. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  15. Sec13 induces genomic instability in U2OS cells. Sihn, C.R., Suh, E.J., Lee, K.H., Kim, S.H. Exp. Mol. Med. (2005) [Pubmed]
  16. Recombinant production in baculovirus-infected insect cells and purification of the mammalian Sec13/Sec31 complex. Gurkan, C., Balch, W.E. Meth. Enzymol. (2005) [Pubmed]
  17. Purification and functional properties of yeast Sec12 GEF. Futai, E., Schekman, R. Meth. Enzymol. (2005) [Pubmed]
  18. Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV identifies six known genes, a new member of the hexose transporter family and ten new open reading frames. Maftahi, M., Nicaud, J.M., Levesque, H., Gaillardin, C. Yeast (1995) [Pubmed]
  19. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. Shimoni, Y., Kurihara, T., Ravazzola, M., Amherdt, M., Orci, L., Schekman, R. J. Cell Biol. (2000) [Pubmed]
  20. A membrane protein enriched in endoplasmic reticulum exit sites interacts with COPII. Tang, B.L., Ong, Y.S., Huang, B., Wei, S., Wong, E.T., Qi, R., Horstmann, H., Hong, W. J. Biol. Chem. (2001) [Pubmed]
 
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