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(Received for publication, September 16, 1996, and in revised form, November 7, 1996)
From the UBC6 is a C-terminal membrane-anchored (type IV)
protein, native to Saccharomyces cerevisiae, where it is
found in the endoplasmic reticulum. When expressed in mammalian cells,
this novel ubiquitin-conjugating enzyme also localizes to the
endoplasmic reticulum. UBC6 lacks a lumenal domain and contains no
known endoplasmic reticulum retention signals. Analysis of chimeric
proteins in which the cytosolic domain of UBC is linked to a
heterologous transmembrane domain, or in which the UBC6 transmembrane
domain is appended to an unrelated soluble protein, led to the
determination that the transmembrane domain of UBC6 plays a dominant
role in its compartmental localization. The basis for the transmembrane
domain-mediated subcellular targeting of UBC6 was evaluated by
lengthening the wild type UBC6 hydrophobic segment from 17 to 21 amino
acids, which resulted in re-targeting to the Golgi complex. A further
increase in length to 26 amino acids allowed this modified protein to
traverse the secretory pathway and gain expression at the plasma
membrane. These findings are consistent with models in which, in the
absence of dominant cytosolic or lumenal targeting determinants,
proteins may be sorted within the secretory pathway based on
interactions between their transmembrane domains and the surrounding
lipid bilayer.
Volume 272, Number 3,
Issue of January 17, 1997
pp. 1970-1975
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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Laboratory of Immune Cell Biology,
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