Selected article for: "domain interaction and Golgi complex"
Title: Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha 1,2-mannosyltransferase to a medial-Golgi compartment
  • Document date: 1995_11_2
    • ID: q1jx0n0l_60
    Snippet: It has been postulated that the targeting of glycosyltransferases carrying a TMD sorting signal could be due to interactions between the membrane-spanning domain and compartment specific membrane lipids (Pelham and Munro, 1993) . There is no evidence that Kre2p is retained by such a mechanism, since in the series of constructs we have devised, the Kre2p TMD is not implicated in retention. In this lipid interaction model, the length of the membran.....
    Document: It has been postulated that the targeting of glycosyltransferases carrying a TMD sorting signal could be due to interactions between the membrane-spanning domain and compartment specific membrane lipids (Pelham and Munro, 1993) . There is no evidence that Kre2p is retained by such a mechanism, since in the series of constructs we have devised, the Kre2p TMD is not implicated in retention. In this lipid interaction model, the length of the membranespanning domain is important for the proper sorting of animal glycosyltransferases (Munro, 1991; Pelham and Munro, 1993) . In the case of KDKK the TMD of DPAP B is three amino acid residues shorter than the Kre2p TMD, and in the case of KPKK the TMD of Pho8p is seven amino acid residues longer than the Kre2p TMD, yet both are retained in the Golgi complex.

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