Gene Symbol: SNA3
Description: Sna3p
Alias: Sna3p
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Stawiecka Mirota M, Pokrzywa W, Morvan J, Zoladek T, Haguenauer Tsapis R, Urban Grimal D, et al. Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation. Traffic. 2007;8:1280-96 pubmed
    ..b>Sna3p is a membrane protein previously described as an Ub-independent MVB cargo, but proteomic studies have since shown ..
  2. Reggiori F, Pelham H. Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting. EMBO J. 2001;20:5176-86 pubmed
    ..a polyphosphatase (Phm5p), a presumptive haem oxygenase (Ylr205p/Hmx1p) and a protein of unknown function (Yjl151p/Sna3p). All are membrane proteins, and appear to be cargo molecules rather than part of the vesicle-forming machinery...
  3. Kim H, Steffen A, Oldham M, Chen J, Huibregtse J. Structure and function of a HECT domain ubiquitin-binding site. EMBO Rep. 2011;12:334-41 pubmed publisher
    ..Our results support a model in which the N-lobe-binding site acts to localize and orient the distal end of the ubiquitin chain to promote conjugation of the next ubiquitin molecule. ..
  4. MacDonald C, Stringer D, Piper R. Sna3 is an Rsp5 adaptor protein that relies on ubiquitination for its MVB sorting. Traffic. 2012;13:586-98 pubmed publisher
    ..To better understand this process, we have further characterized the membrane protein Sna3, the prototypical Ub-independent cargo protein sorted through the MVB pathway in yeast...
  5. Oestreich A, Aboian M, Lee J, Azmi I, Payne J, Issaka R, et al. Characterization of multiple multivesicular body sorting determinants within Sna3: a role for the ubiquitin ligase Rsp5. Mol Biol Cell. 2007;18:707-20 pubmed
    ..identify additional MVB sorting signals, we examined the previously described ubiquitination-independent MVB cargo Sna3. Although Sna3 ubiquitination is not essential, Sna3 MVB sorting is positively modulated by its ubiquitination...
  6. McNatt M, McKittrick I, West M, Odorizzi G. Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway. Mol Biol Cell. 2007;18:697-706 pubmed
    ..However, Ub is not required for sorting of Sna3, an MVB vesicle cargo protein in yeast...
  7. Kim H, Huibregtse J. Polyubiquitination by HECT E3s and the determinants of chain type specificity. Mol Cell Biol. 2009;29:3307-18 pubmed publisher
    ..Our results are also consistent with a simple sequential-addition mechanism for polyubiquitination by Rsp5, rather than a mechanism involving the formation of either E2- or E3-linked polyubiquitin chain transfers. ..
  8. Watson H, Bonifacino J. Direct binding to Rsp5p regulates ubiquitination-independent vacuolar transport of Sna3p. Mol Biol Cell. 2007;18:1781-9 pubmed
    ..An exception is Sna3p, which does not require ubiquitination for entry into MVBs...
  9. Kamadurai H, Qiu Y, Deng A, Harrison J, MacDonald C, Actis M, et al. Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3. elife. 2013;2:e00828 pubmed publisher

More Information


  1. Shetty A, Swaminathan A, Lopes J. Transcription regulation of a yeast gene from a downstream location. J Mol Biol. 2013;425:457-65 pubmed publisher
    ..This study focused on inositol-mediated regulation of the tandem gene pair SNA3-INO1...
  2. De Block J, Szopinska A, Guerriat B, Dodzian J, Villers J, Hochstenbach J, et al. Yeast Pmp3p has an important role in plasma membrane organization. J Cell Sci. 2015;128:3646-59 pubmed publisher
    ..and it belongs to the sensitive to Na(+) (SNA)-protein family, which comprises four members--Pmp3p/Sna1p, Sna2p, Sna3p and Sna4p...
  3. Lee J, Oestreich A, Payne J, Gunawan M, Norgan A, Katzmann D. The HECT domain of the ubiquitin ligase Rsp5 contributes to substrate recognition. J Biol Chem. 2009;284:32126-37 pubmed publisher
    ..These results highlight the ability of Rsp5 to interact with substrates via multiple modalities, suggesting additional mechanisms of regulating this interaction and relevant outcomes. ..
  4. Jarmoszewicz K, Łukasiak K, Riezman H, Kaminska J. Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants. PLoS ONE. 2012;7:e39582 pubmed publisher
    ..Additionally, Rsp5 and Sla1 proteins were found by co-immunoprecipitation in a complex containing COPI subunits. Together, our results show that Rsp5 ligase plays a role in regulating retrograde Golgi-to-ER trafficking. ..
  5. Matsumoto R, Suzuki K, Ohya Y. Organelle acidification is important for localisation of vacuolar proteins in Saccharomyces cerevisiae. Protoplasma. 2013;250:1283-93 pubmed publisher
    ..These results suggest that many alterations in the localisation of vacuolar proteins occur after loss of the acidification of acidic compartments. ..
  6. Hiraki T, Abe F. Overexpression of Sna3 stabilizes tryptophan permease Tat2, potentially competing for the WW domain of Rsp5 ubiquitin ligase with its binding protein Bul1. FEBS Lett. 2010;584:55-60 pubmed publisher
    ..Overexpression of SNA3 encoding an endosomal/vacuolar protein possessing the PPAY motif allowed growth at 25 MPa, which was potentiated by ..
  7. Leon S, Erpapazoglou Z, Haguenauer Tsapis R. Ear1p and Ssh4p are new adaptors of the ubiquitin ligase Rsp5p for cargo ubiquitylation and sorting at multivesicular bodies. Mol Biol Cell. 2008;19:2379-88 pubmed publisher
    ..Therefore, Ear1p/Ssh4p recruit Rsp5p and assist it in its function at MVBs by directing the ubiquitylation of specific cargoes. ..
  8. Epple U, Eskelinen E, Thumm M. Intravacuolar membrane lysis in Saccharomyces cerevisiae. Does vacuolar targeting of Cvt17/Aut5p affect its function?. J Biol Chem. 2003;278:7810-21 pubmed
    ..These findings suggest that similar to Sna3p sorting of Cvt17/Aut5p to MVB vesicles is independent of ubiquitination...
  9. MacDonald C, Payne J, Aboian M, Smith W, Katzmann D, Piper R. A family of tetraspans organizes cargo for sorting into multivesicular bodies. Dev Cell. 2015;33:328-42 pubmed publisher
    ..Expression of these proteins increases during nutrient stress through an NAD(+)/Sir2-dependent mechanism that in turn accelerates the downregulation of a broad range of cell-surface proteins. ..