The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization
The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization
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.
Amino Acid Sequence, Antigens, Differentiation, B-Lymphocyte, Brefeldin A, Cell Membrane, Cyclopentanes, Cytoplasm, DNA, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Golgi Apparatus, HeLa Cells, Histocompatibility Antigens Class II, Humans, Microscopy, Electron, Microscopy, Fluorescence, Molecular Sequence Data, N-Acetyllactosamine Synthase, Transfection, Journal Article, Research Support, Non-U.S. Gov't
3567-75
Nilsson, T
dc04eed0-7d32-4e19-aad5-f563a273d3da
Lucocq, J M
f56b463d-3280-46ab-89b8-3cdf95fcab24
Mackay, D
588a653e-9785-4a00-be71-4e547850ee4a
Warren, Graham
b333359b-629a-4a98-8fc4-24566215d10a
December 1991
Nilsson, T
dc04eed0-7d32-4e19-aad5-f563a273d3da
Lucocq, J M
f56b463d-3280-46ab-89b8-3cdf95fcab24
Mackay, D
588a653e-9785-4a00-be71-4e547850ee4a
Warren, Graham
b333359b-629a-4a98-8fc4-24566215d10a
Nilsson, T, Lucocq, J M, Mackay, D and Warren, Graham
(1991)
The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization.
The EMBO Journal, 10 (12), .
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.
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Published date: December 1991
Keywords:
Amino Acid Sequence, Antigens, Differentiation, B-Lymphocyte, Brefeldin A, Cell Membrane, Cyclopentanes, Cytoplasm, DNA, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Golgi Apparatus, HeLa Cells, Histocompatibility Antigens Class II, Humans, Microscopy, Electron, Microscopy, Fluorescence, Molecular Sequence Data, N-Acetyllactosamine Synthase, Transfection, Journal Article, Research Support, Non-U.S. Gov't
Identifiers
Local EPrints ID: 418318
URI: http://eprints.soton.ac.uk/id/eprint/418318
ISSN: 0261-4189
PURE UUID: 51d44af1-6a83-41cb-ae8f-5cadc5f14e2c
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Date deposited: 28 Feb 2018 17:30
Last modified: 16 Mar 2024 03:05
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Author:
T Nilsson
Author:
J M Lucocq
Author:
Graham Warren
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