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First published online 14 September 2004
doi: 10.1242/jcs.01372

Journal of Cell Science 117, 4959-4968 (2004)
Published by The Company of Biologists 2004
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Research Article

Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae

Erik Kvam and David S. Goldfarb*

Department of Biology, University of Rochester, 436 Hutchison Hall, Rochester, New York, NY 14627, USA

* Author for correspondence (e-mail: dasg{at}mail.rochester.edu)

Accepted 21 June 2004

OSH1 belongs to a seven-member gene family in yeast that is related to mammalian oxysterol-binding protein (OSBP). Here, we investigate the targeting of Osh1p to nucleus-vacuole (NV) junctions in Saccharomyces cerevisiae. NV junctions are interorganelle interfaces mediated by Nvj1p in the nuclear envelope and Vac8p on the vacuole membrane. Together, Nvj1p and Vac8p form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by a process termed piecemeal microautophagy of the nucleus (PMN). Osh1p is targeted to NV junctions proportional to NVJ1 expression through a physical association with Nvj1p. NV junctions per se are not required for this targeting because Osh1p colocalizes with Nvj1p in the absence of Vac8p. NV-junction-associated Osh1p is also a substrate for PMN degradation. Although OSH1 is not required for NV-junction formation or PMN, PMN is defective in cells lacking the yeast OSBP family (Osh1p to Osh7p). By contrast, the vesicular targeting of aminopeptidase I to the vacuole by macroautophagy is not dependent on the Osh protein family. We conclude the formation of nuclear PMN vesicles requires the overlapping activities of Osh1p and other Osh family members.

Key words: Nucleus-vacuole junction, Oxysterol-binding protein, Autophagy


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© The Company of Biologists Ltd 2004