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Gene Review

SEC16  -  Sec16p

Saccharomyces cerevisiae S288c

Synonyms: COPII coat assembly protein SEC16, LPF1W, Protein transport protein SEC16, YPL085W
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High impact information on SEC16

  • SEC16 encodes a 240-kD hydrophilic protein that is required for transport vesicle budding from the ER in Saccharomyces cerevisiae [1].
  • We propose that Sec16p nucleates a Sar1-GTP-dependent initiation of COPII assembly and serves to stabilize the coat to premature disassembly after Sar1p hydrolyzes GTP [1].
  • Sec16p is tightly and peripherally bound to ER membranes, hence it is not one of the cytosolic proteins required to reconstitute transport vesicle budding in a cell-free reaction [1].
  • Although COPII vesicle budding is promoted by GTP or a nonhydrolyzable analogue, guanylimide diphosphate (GMP-PNP), Sec16p stimulation is dependent on GTP in the reaction [1].
  • Details of coat protein assembly and Sec16p-stimulated vesicle budding were explored with synthetic liposomes composed of a mixture of lipids, including acidic phospholipids (major-minor mix), or a simple binary mixture of phosphatidylcholine (PC) and phosphatidylethanolamine (PE) [1].

Biological context of SEC16


Anatomical context of SEC16


Associations of SEC16 with chemical compounds

  • Sec16p is released from this particulate fraction by high salt, but not by nonionic detergents or urea [5].

Physical interactions of SEC16

  • Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p [5].
  • Second, we show that a truncation mutant of Sec31p specifically defective for Sec16p binding is unable to complement a sec31Delta mutant and cannot rescue the secretion defect of a temperature-sensitive sec31 mutant at nonpermissive temperatures [6].
  • Here we use two-hybrid and coprecipitation assays to demonstrate that the essential COPII protein Sec24p binds to the central region of Sec16p [7].

Regulatory relationships of SEC16

  • Sec16p binds to major-minor mix liposomes and facilitates the recruitment of COPII proteins and vesicle budding in a reaction that is stimulated by Sar1p and GMP-PNP [1].

Other interactions of SEC16

  • In a screen to find functionally related genes, we isolated SED4 as a dosage-dependent suppressor of temperature-sensitive SEC16 mutations [3].
  • In the delta(sed4) background, the suppression activity of SAR1 towards sec12 and sec16 is lost [8].
  • First, we map onto Sec31p binding regions for Sec16p, Sec23p, Sec24p, and Sec13p [6].
  • They also suppressed yeast sec12 and sec16 temperature-sensitive mutations as yeast SAR1 does [9].
  • These findings indicate that Sec16p associates with Sec23p as part of the transport vesicle coat structure [5].

Analytical, diagnostic and therapeutic context of SEC16


  1. Sec16p potentiates the action of COPII proteins to bud transport vesicles. Supek, F., Madden, D.T., Hamamoto, S., Orci, L., Schekman, R. J. Cell Biol. (2002) [Pubmed]
  2. 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]
  3. SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation. Gimeno, R.E., Espenshade, P., Kaiser, C.A. J. Cell Biol. (1995) [Pubmed]
  4. Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Campbell, J.L., Schekman, R. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  5. Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. Espenshade, P., Gimeno, R.E., Holzmacher, E., Teung, P., Kaiser, C.A. J. Cell Biol. (1995) [Pubmed]
  6. COPII subunit interactions in the assembly of the vesicle coat. Shaywitz, D.A., Espenshade, P.J., Gimeno, R.E., Kaiser, C.A. J. Biol. Chem. (1997) [Pubmed]
  7. COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent regions of Sec16p. Gimeno, R.E., Espenshade, P., Kaiser, C.A. Mol. Biol. Cell (1996) [Pubmed]
  8. Sed4p functions as a positive regulator of Sar1p probably through inhibition of the GTPase activation by Sec23p. Saito-Nakano, Y., Nakano, A. Genes Cells (2000) [Pubmed]
  9. Isolation of a tobacco cDNA encoding Sar1 GTPase and analysis of its dominant mutations in vesicular traffic using a yeast complementation system. Takeuchi, M., Tada, M., Saito, C., Yashiroda, H., Nakano, A. Plant Cell Physiol. (1998) [Pubmed]
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