Selected article for: "ER retention and mutant protein"
Title: Endoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain
  • Document date: 1996_7_2
    • ID: 45x96b5d_64
    Snippet: We have also tried to determine which part of the cytoplasmic domain of Sec12p is important for the ER retention by a systematic deletion analysis. However, most of the constructed mutant proteins are unstable in the yeast cells, and we have been unable to narrow down the region that is ascribed to for the retention mechanism. The cytoplasmic domain of Secl2p contains the catalytic site of the protein that functions as the guanine-nucleotide exch.....
    Document: We have also tried to determine which part of the cytoplasmic domain of Sec12p is important for the ER retention by a systematic deletion analysis. However, most of the constructed mutant proteins are unstable in the yeast cells, and we have been unable to narrow down the region that is ascribed to for the retention mechanism. The cytoplasmic domain of Secl2p contains the catalytic site of the protein that functions as the guanine-nucleotide exchange factor toward the Sarl GTPase (Barlowe and Schekman, 1993) . Mutations in this region may hamper the interaction with Sarlp and other molecules that are essential for vesicle budding and thus accelerate the degradation of the mutant protein. It is also conceivable that the interaction of the cytoplasmic domain of Secl2p with other component(s) of the budding machinery may be the mechanism of the static retention. If so, the signal in this domain may require its overall conformation rather than particular residues.

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