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Published 19 August 2002. doi:10.1083/jcb.200203086
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© The Rockefeller University Press, 0021-9525/2002/8/639 $5.00
The Journal of Cell Biology, Volume 158, Number 4, August 19, 2002 639-646

Article

A survival pathway for Caenorhabditis elegans with a blocked unfolded protein response



Fumihiko Urano1, Marcella Calfon1, Takunari Yoneda1, Chi Yun1, Moni Kiraly2, Scott G. Clark1 and David Ron1

1 Skirball Institute, New York University School of Medicine, New York, NY 10016
2 Department of Developmental Biology and Genetics, Stanford University Medical School, Stanford, CA 94305

Address correspondence to David Ron, Skirball Institute of Biomolecular Medicine, Room 3-10, 540 First Avenue, New York, NY 10016. Tel.: (212) 263-7786. Fax: (212) 263-8951. E-mail: ron{at}saturn.med.nyu.edu

The unfolded protein response (UPR) counteracts stress caused by unprocessed ER client proteins. A genome-wide survey showed impaired induction of many UPR target genes in xbp-1 mutant Caenorhabditis elegans that are unable to signal in the highly conserved IRE1-dependent UPR pathway. However a family of genes, abu (activated in blocked UPR), was induced to higher levels in ER-stressed xbp-1 mutant animals than in ER-stressed wild-type animals. RNA-mediated interference (RNAi) inactivation of a representative abu family member, abu-1 (AC3.3), activated the ER stress marker hsp-4::gfp in otherwise normal animals and killed 50% of ER-stressed ire-1 and xbp-1 mutant animals. Abu-1(RNAi) also enhanced the effect of inactivation of sel-1, an ER-associated protein degradation gene. The nine abu genes encode highly related type I transmembrane proteins whose lumenal domains have sequence similarity to a mammalian cell surface scavenger receptor of endothelial cells that binds chemically modified extracellular proteins and directs their lysosomal degradation. Our findings that ABU-1 is an intracellular protein located within the endomembrane system that is induced by ER stress in xbp-1 mutant animals suggest that ABU proteins may interact with abnormal ER client proteins and this function may be particularly important in animals with an impaired UPR.

Key Words: chaperone; protein folding; protein degradation; gene expression; functional genomics


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