Title: trans-Golgi retention of a plasma membrane protein: mutations in the cytoplasmic domain of the asialoglycoprotein receptor subunit H1 result in trans-Golgi retention Document date: 1995_7_2
ID: tedj3xxz_4
Snippet: As part of these studies, an H1 mutant lacking most of the cytoplasmic domain (residues 4-33) was constructed (Geffen et al., 1993) . Although this mutant protein exits the ER, it is not detectable at the cell surface. Here we show that it accumulates specifically in a trans-Golgi compartment. The sequence requirement for retention or exit to the plasma membrane was investigated by further mutagenesis. The results indicate that the size of the cy.....
Document: As part of these studies, an H1 mutant lacking most of the cytoplasmic domain (residues 4-33) was constructed (Geffen et al., 1993) . Although this mutant protein exits the ER, it is not detectable at the cell surface. Here we show that it accumulates specifically in a trans-Golgi compartment. The sequence requirement for retention or exit to the plasma membrane was investigated by further mutagenesis. The results indicate that the size of the cytoplasmic domain determines the fate of the protein and modulates an intrinsic ability of the transmembrane and/or exoplasmic portion of H1 to interact with component(s) resident in the trans-Golgi. Such a mechanism may be functional also for other trans-Golgi/plasma membrane proteins.
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