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SFB3  -  Sfb3p

Saccharomyces cerevisiae S288c

Synonyms: LST1, Lethal with SEC13 protein 1, SEC24-related protein 3, SED5-binding protein 3, YHR098C
 
 
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High impact information on SFB3

  • We show that the same site is conserved as a cargo-interaction domain on the Sec24p homolog Lst1p, which only packages a subset of the cargoes recognized by Sec24p [1].
  • Furthermore, unlike Sec24p, Lst1p fails to bind to Bet1p in vitro, indicating a direct correlation between cargo binding and recruitment into vesicles [2].
  • We show that Lst1p can function as a COPII subunit independently of Sec24p on native ER membranes and on synthetic liposomes [2].
  • A tagged version of Lst1p was purified and eluted as a heterodimer complexed with Sec23p comparable to the Sec23/24p heterodimer [3].
  • Furthermore, Pma1p coimmunoprecipitated with Lst1p and Sec24p from vesicles [3].
 

Anatomical context of SFB3

 

Associations of SFB3 with chemical compounds

  • Surprisingly, monomeric Pma1p present in ceramide-deficient membranes can be exported from the ER in COPII vesicles in a reaction that is stimulated by Lst1p [5].
 

Other interactions of SFB3

  • Vesicles formed with a mixture of Sec23/Lst1p and Sec23/24p were similar morphologically and in their buoyant density, but larger than normal COPII vesicles (87-nm vs. 75-nm diameter) [3].
  • We investigated the role of Lst1p, a Sec24p homologue, in cargo recruitment into COPII vesicles in Saccharomyces cerevisiae [3].
  • Supplementation of mutant cytosol with purified Sec23/Lst1p restored Pma1p packaging into the vesicles [3].
  • Sec24p and its two nonessential homologues Sfb2p and Sfb3p have been suggested to serve in cargo selection [6].

References

  1. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Miller, E.A., Beilharz, T.H., Malkus, P.N., Lee, M.C., Hamamoto, S., Orci, L., Schekman, R. Cell (2003) [Pubmed]
  2. Cargo selection into COPII vesicles is driven by the Sec24p subunit. Miller, E., Antonny, B., Hamamoto, S., Schekman, R. EMBO J. (2002) [Pubmed]
  3. 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]
  4. LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. Roberg, K.J., Crotwell, M., Espenshade, P., Gimeno, R., Kaiser, C.A. J. Cell Biol. (1999) [Pubmed]
  5. Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum. Lee, M.C., Hamamoto, S., Schekman, R. J. Biol. Chem. (2002) [Pubmed]
  6. Endoplasmic reticulum exit of a secretory glycoprotein in the absence of sec24p family proteins in yeast. Karhinen, L., Bastos, R.N., Jokitalo, E., Makarow, M. Traffic (2005) [Pubmed]
 
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