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Vol. 15, Issue 6, 2758-2770, June 2004

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Deficiencies in the Endoplasmic Reticulum (ER)-Membrane Protein Gab1p Perturb Transfer of Glycosylphosphatidylinositol to Proteins and Cause Perinuclear ER-associated Actin Bar Formation

Stephen J. Grimme ^* , Xiang-Dong Gao  , Paul S. Martin , Kim Tu , Serguei E. Tcheperegine , Kathleen Corrado  ^||, Anne E. Farewell  ^¶, Peter Orlean ^*, and Erfei Bi  ^#

^* Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801; Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104; Department of Biology, University of Michigan, Ann Arbor, Michigan 48109; ^|| Onondaga County Center for Forensic Sciences, Syracuse, New York 13210; and ^¶ Department of General and Marine Microbiology, Lundberg Laboratory, Göteborg University, S-405 30 Göteborg, Sweden

Submitted January 15, 2004; Revised March 5, 2004; Accepted March 26, 2004
Monitoring Editor: Reid Gilmore

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.

These authors contributed equally to this work.

^# Corresponding author. E-mail address: ebi{at}mail.med.upenn.edu.

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