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Vol. 11, Issue 1, 23-38, January 2000
and
*Medical Research Council Laboratory of Molecular Biology,
Cambridge CB2 2QH, United Kingdom; and Many endocytosed proteins in yeast travel to the vacuole, but some
are recycled to the plasma membrane. We have investigated the recycling
of chimeras containing green fluorescent protein (GFP) and the exocytic
SNARE Snc1p. GFP-Snc1p moves from the cell surface to internal
structures when Golgi function or exocytosis is blocked, suggesting
continuous recycling via the Golgi. Internalization is mediated by a
conserved cytoplasmic signal, whereas diversion from the vacuolar
pathway requires sequences within and adjacent to the transmembrane
domain. Delivery from the Golgi to the surface is also influenced by
the transmembrane domain, but the requirements are much less specific.
Recycling requires the syntaxins Tlg1p and Tlg2p but not Pep12p or
proteins such as Vps4p and Vps5p that have been implicated in late
endosome-Golgi traffic. Subtle changes to the recycling signal cause
GFP-Snc1p to accumulate preferentially in punctate internal structures,
although it continues to recycle to the surface. The internal GFP-Snc1p
colocalizes with Tlg1p, and immunofluorescence and immunoelectron
microscopy reveal structures that contain Tlg1p, Tlg2p, and Kex2p but
lack Pep12p and Sec7p. We propose that these represent early endosomes
in which sorting of Snc1p and late Golgi proteins occurs, and that
transport can occur directly from them to the Golgi apparatus.
Biozentrum of the
University of Basel, CH-4056 Basel, Switzerland
Present address: Cell Biology and
Metabolism Branch, National Institute of Child Health and Human
Development, National Institutes of Health, Bethesda, MD 20892.
§
Corresponding author. E-mail address:
hp{at}mrc-lmb.cam.ac.uk.
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