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Vol. 10, Issue 10, 3357-3372, October 1999


Departments of *Cell Biology and ¶Biological Sciences,
University of Alberta, Edmonton, AB, T6G 2H7, Canada;
A panel of mAbs was elicited against intracellular membrane
fractions from rat pancreas. One of the antibodies reacted with a
95-kDa protein that localizes primarily to the Golgi complex or the
endoplasmic reticulum (ER), depending on cell type. The corresponding
cDNA was cloned and sequenced and found to encode a protein of 97.6 kDa
that we call GERp95 (Golgi ER protein 95 kDa). The
protein copurifies with intracellular membranes but does not contain
hydrophobic regions that could function as signal peptides or
transmembrane domains. Biochemical analysis suggests that GERp95 is a
cytoplasmically exposed peripheral membrane protein that exists in a
protease-resistant complex. GERp95 belongs to a family of highly
conserved proteins in metazoans and Schizosaccharomyces pombe. It has recently been determined that plant and
Drosophila homologues of GERp95 are important for
controlling the differentiation of stem cells (Bohmert et
al., 1998; Cox et al., 1998; Moussian et
al., 1998). In Caenorhabditis elegans, there are
at least 20 members of this protein family. To this end, we have used
RNA interference to show that the GERp95 orthologue in C.
elegans is important for maturation of germ-line stem cells in
the gonad. GERp95 and related proteins are an emerging new family of
proteins that have important roles in metazoan development. The present study suggests that these proteins may exert their effects on cell
differentiation from the level of intracellular membranes.
Biological Process Sciences, SmithKline Beecham
Pharmaceuticals, King of Prussia, Pennsylvania 19406; and
London Regional Cancer Centre, London, Ontario N6A 4L6
Canada
Corresponding author. E-mail address:
thobman{at}anat.med.ualberta.ca.
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