PMID:1935889

Citation	Nilsson, T, Lucocq, JM, Mackay, D and Warren, G (1991) The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization. EMBO J. 10:3567-75
Abstract	Chimeric cDNAs were constructed so as to generate hybrid proteins in which different parts of the N-terminal domain of the human invariant chain were replaced by equivalent sequences from the trans Golgi resident enzyme, beta-1,4-galactosyltransferase. The cytoplasmic and membrane spanning domains of galactosyltransferase were found to be sufficient to retain all of the hybrid invariant chain in trans Golgi cisternae as judged by indirect immunofluorescence, treatment with brefeldin A and immuno-electron microscopy. As few as ten amino acids corresponding to the lumenal half of the membrane spanning domain of the Golgi enzyme sufficed to localize most of the hybrid invariant chain to the trans cisternae. A cytoplasmic domain was necessary for complete retention as assessed by flow cytofluorometry but could be provided either by galactosyltransferase or by invariant chain. This suggests that the cytoplasmic domain plays a role accessory to the membrane spanning domain, the latter mediating compartmental specificity.
Links	PubMed PMC453088
Keywords	Amino Acid Sequence; Antigens, Differentiation, B-Lymphocyte; Brefeldin A; Cell Membrane/enzymology; Cyclopentanes/pharmacology; Cytoplasm/enzymology; DNA/genetics; Electrophoresis, Polyacrylamide Gel; Flow Cytometry; Golgi Apparatus/enzymology; HeLa Cells/ultrastructure; Histocompatibility Antigens Class II/metabolism; Humans; Microscopy, Electron; Microscopy, Fluorescence; Molecular Sequence Data; N-Acetyllactosamine Synthase/genetics; N-Acetyllactosamine Synthase/metabolism; Transfection
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HUMAN:B4GT7		GO:0000138: Golgi trans cisterna	ECO:0000314:		C		Figure 7E	complete CACAO 10434

References

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