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Gene Review

MSO1  -  Mso1p

Saccharomyces cerevisiae S288c

Synonyms: N3457, Protein MSO1, YNR049C
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High impact information on MSO1

  • We further found that Mso1p interacts with Sec1p both in vitro and in the two-hybrid system [1].
  • Cells that lack MSO1 are viable, but they accumulate secretory vesicles in the bud, indicating that the terminal step in secretion is partially impaired [1].
  • These results position Mso1p in the interface of the exocyst complex, Sec4p, and the SNARE machinery, and reveal a novel layer of molecular conservation in the exocytosis machinery [2].
  • Green fluorescent protein-tagged Mso1p localizes to the sites of exocytosis and at the site of prospore membrane formation [2].
  • In this study, we have analyzed the association of the Sec1p interacting protein Mso1p with the membrane fusion machinery in yeast [2].

Biological context of MSO1

  • A point mutation, T47A, within the Sec1p-binding domain abolishes Mso1p functionality in vivo, and mso1T47A mutant cells display specific genetic interactions with sec1 mutants [2].
  • As a proof of principle, we produced a set of plasmid constructions encoding both C- and N-terminally truncated variants of yeast Mso1p and mapped its Sec1p-interacting region [3].

Anatomical context of MSO1

  • Mso1 localized primarily to the plasma membrane of the bud when SNARE complex formation was not impaired but was mostly in the cytoplasm when assembly was prevented [4].

Regulatory relationships of MSO1

  • Overexpression of Mso1 lacking this domain (Mso1-(1-193)) inhibited the growth of cells bearing an attenuated Sec4 GTPase [4].

Other interactions of MSO1

  • These findings suggest that Mso1p is a component of the secretory vesicle docking complex whose function is closely associated with that of Sec1p [1].

Analytical, diagnostic and therapeutic context of MSO1

  • The mutant proteins were unable to interact with the Sec1p-interacting proteins Mso1p and Sso2p in the two-hybrid assay, even at the permissive temperature [5].


  1. Mso1p: a yeast protein that functions in secretion and interacts physically and genetically with Sec1p. Aalto, M.K., Jäntti, J., Ostling, J., Keränen, S., Ronne, H. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. Molecular interactions position Mso1p, a novel PTB domain homologue, in the interface of the exocyst complex and the exocytic SNARE machinery in yeast. Knop, M., Miller, K.J., Mazza, M., Feng, D., Weber, M., Keränen, S., Jäntti, J. Mol. Biol. Cell (2005) [Pubmed]
  3. A gene truncation strategy generating N- and C-terminal deletion variants of proteins for functional studies: mapping of the Sec1p binding domain in yeast Mso1p by a Mu in vitro transposition-based approach. Poussu, E., Jäntti, J., Savilahti, H. Nucleic Acids Res. (2005) [Pubmed]
  4. Mso1 is a novel component of the yeast exocytic SNARE complex. Castillo-Flores, A., Weinberger, A., Robinson, M., Gerst, J.E. J. Biol. Chem. (2005) [Pubmed]
  5. Characterization of the sec1-1 and sec1-11 mutations. Brummer, M.H., Kivinen, K.J., Jäntti, J., Toikkanen, J., Söderlund, H., Keränen, S. Yeast (2001) [Pubmed]
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