SFB3

Summary

Gene Symbol: SFB3
Description: Sfb3p
Alias: LST1, Sfb3p
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Cohen M, Stutz F, Dargemont C. Deubiquitination, a new player in Golgi to endoplasmic reticulum retrograde transport. J Biol Chem. 2003;278:51989-92 pubmed
    ..Bre5p complex. All together, our results indicate that the Ubp3p.Bre5p deubiquitination complex co-regulates anterograde and retrograde transports between endoplasmic reticulum and Golgi compartments. ..
  2. Roberg K, Bickel S, Rowley N, Kaiser C. Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8. Genetics. 1997;147:1569-84 pubmed
    ..The LST7 gene encodes a novel protein. Together, these data indicate that SEC13, LST4, LST7, and LST8 function in the regulated delivery of Gap1p to the cell surface, perhaps as components of a post-Golgi secretory-vesicle coat. ..
  3. Roberg K, Crotwell M, Espenshade P, Gimeno R, Kaiser C. LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol. 1999;145:659-72 pubmed
    ..b>LST1 showed synthetic-lethal interactions with the complete set of COPII genes, indicating that LST1 encodes a new COPII ..
  4. Peng R, De Antoni A, Gallwitz D. Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem. 2000;275:11521-8 pubmed
    ..cerevisiae expresses two non-essential Sec24p-related proteins, termed Sfb2p (product of YNL049c) and Sfb3p/Lst1p (product of YHR098c)...
  5. Shimoni Y, Kurihara T, Ravazzola M, Amherdt M, Orci L, Schekman R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol. 2000;151:973-84 pubmed
    ..We found that cytosol from an lst1-null strain supported the packaging of alpha-factor precursor into COPII vesicles but was deficient in the ..
  6. Miller E, Beilharz T, Malkus P, Lee M, Hamamoto S, Orci L, et al. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell. 2003;114:497-509 pubmed
    ..Together, our data support a model whereby Sec24p proteins contain multiple independent cargo binding domains that allow for recognition of a diverse set of sorting signals...
  7. Bhandari D, Zhang J, Menon S, Lord C, Chen S, Helm J, et al. Sit4p/PP6 regulates ER-to-Golgi traffic by controlling the dephosphorylation of COPII coat subunits. Mol Biol Cell. 2013;24:2727-38 pubmed publisher
    ..In vitro, Sit4p dephosphorylates COPII coat subunits. Consistent with a role in coat recycling, Sit4p and its mammalian orthologue, PP6, regulate traffic from the ER to the Golgi complex. ..
  8. D Arcangelo J, Crissman J, Pagant S, Čopič A, Latham C, Snapp E, et al. Traffic of p24 Proteins and COPII Coat Composition Mutually Influence Membrane Scaffolding. Curr Biol. 2015;25:1296-305 pubmed publisher
    ..Vesicles that contain such cargoes are also more dependent on scaffolding by Sec13p, and may serve as a model for large carrier formation in other systems. ..
  9. Miller E, Antonny B, Hamamoto S, Schekman R. Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J. 2002;21:6105-13 pubmed
    ..Our data suggest that the principle role of Sec24p is to discriminate cargo molecules for incorporation into COPII vesicles...

More Information

Publications11

  1. Behnia R, Barr F, Flanagan J, Barlowe C, Munro S. The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic. J Cell Biol. 2007;176:255-61 pubmed
  2. Kodera C, Yorimitsu T, Sato K. Sec23 homolog Nel1 is a novel GTPase-activating protein for Sar1 but does not function as a subunit of the coat protein complex II (COPII) coat. J Biol Chem. 2014;289:21423-32 pubmed publisher
    ..In contrast to Sec23, which is predominantly localized at ER exit sites on the ER membrane, a major proportion of Nel1 is localized throughout the cytosol. Our findings highlight a possible role of Nel1 as a novel GAP for Sar1. ..