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_32
Snippet: The disruption of the RER1 gene showed various effects on the chimeric proteins (see Fig. 4 , Table II ). The three constructs, DSSm, DSDm, and SSDm, which contain the Sec12p TMD, secreted significant amounts of a-factor in the Arerl cells like SSSm. This indicates that Rerlp is very important for the retention of these proteins in the early compartments. In contrast, the secretion of a-factor by SDSm or SDDm was not markedly affected by the RER1.....
Document: The disruption of the RER1 gene showed various effects on the chimeric proteins (see Fig. 4 , Table II ). The three constructs, DSSm, DSDm, and SSDm, which contain the Sec12p TMD, secreted significant amounts of a-factor in the Arerl cells like SSSm. This indicates that Rerlp is very important for the retention of these proteins in the early compartments. In contrast, the secretion of a-factor by SDSm or SDDm was not markedly affected by the RER1 disruption. In the case of SDDm, the amount of the secreted a-factor was about 35-38% (12-13% if corrected) of that of DDDm, regardless of RER1 ÷ or Arerl. In other words, a significant amount of the molecule is still retained in the early compartments independent of the Rerlp function.
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