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Vol. 11, Issue 7, 2445-2457, July 2000
and
*Department of Biology, University of Rochester, Rochester NY,
14627; and Vac8p is a vacuolar membrane protein that is required for efficient
vacuole inheritance and fusion, cytosol-to-vacuole targeting, and
sporulation. By analogy to other armadillo domain proteins, including
Department of Molecular Biology and
Microbiology, Case Western Reserve University, School of Medicine,
Cleveland, OH 44106
-catenin and importin 
, we hypothesize that Vac8p docks various
factors at the vacuole membrane. Two-hybrid and copurfication assays
demonstrated that Vac8p does form complexes with multiple binding
partners, including Apg13p, Vab2p, and Nvj1p. Here we describe the
surprising role of Vac8p-Nvj1p complexes in the formation of
nucleus-vacuole (NV) junctions. Nvj1p is an integral membrane protein
of the nuclear envelope and interacts with Vac8p in the cytosol through
its C-terminal 40-60 amino acids (aa). Nvj1p green fluorescent protein
(GFP) concentrated in small patches or rafts at sites of close contact
between the nucleus and one or more vacuoles. Previously, we showed
that Vac8p-GFP concentrated in intervacuole rafts, where is it likely
to facilitate vacuole-vacuole fusion, and in "orphan" rafts at the
edges of vacuole clusters. Orphan rafts of Vac8p red-sifted GFP (YFP)
colocalize at sites of NV junctions with Nvj1p blue-sifted GFP (CFP).
GFP-tagged nuclear pore complexes (NPCs) were excluded from NV
junctions. In vac8-
cells, Nvj1p-GFP generally failed
to concentrate into rafts and, instead, encircled the nucleus. NV
junctions were absent in both nvj1- and
vac8- cells. Overexpression of Nvj1p caused the
profound proliferation of NV junctions. We conclude that Vac8p and
Nvj1p are necessary components of a novel interorganelle junction apparatus.
Corresponding author. E-mail address:
dasg{at}uhura.cc.rochester.edu.
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