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].

References