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A more recent version of this article appeared on June 1, 2004
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Submitted on January 15, 2004
Revised on March 5, 2004
Accepted on March 26, 2004
1 Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
2 Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA
3 Department of Biology, University of Michigan, Ann Arbor, MI 48109, USA; Onondaga County Center for Forensic Sciences, Syracuse, NY 13210, USA
4 Department of Biology, University of Michigan, Ann Arbor, MI 48109, USA; Department of General and Marine Microbiology, Lundberg Laboratory, Göteborg University, S-405 30 Göteborg, Sweden
* Corresponding author. E-mail address: ebi{at}mail.med.upenn.edu.
The essential GAB1 gene, which encodes an endoplasmic reticulum (ER)-membrane protein, was identified in a screen for mutants defective in cellular morphogenesis. A temperature-sensitive gab1 mutant accumulates complete glycosylphosphatidylinositol (GPI) precursors, and its temperature sensitivity is suppressed differentially by overexpression of different subunits of the GPI transamidase, from strong suppression by Gpi8p and Gpi17p, to weak suppression by Gaa1p, and to no suppression by Gpi16p. In addition, both Gab1p and Gpi17p localize to the ER and are in the same protein complex in vivo. These findings suggest that Gab1p is a subunit of the GPI transamidase with distinct relationships to other subunits in the same complex. We also show that depletion of Gab1p or Gpi8p, but not Gpi17p, Gpi16p, or Gaa1p causes accumulation of cofilin-decorated actin bars that are closely associated with the perinuclear ER, which highlights a functional interaction between the ER network and the actin cytoskeleton.
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