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Vol. 9, Issue 1, 131-141, January 1998
Physiologisch-chemisches Institut der Universität
Tübingen, 72076 Tübingen, Germany
Cdc48p from Saccharomyces cerevisiae and its highly
conserved mammalian homologue VCP (valosin-containing protein) are
ATPases with essential functions in cell division and homotypic fusion of endoplasmic reticulum vesicles. Both are mainly attached to the
endoplasmic reticulum, but relocalize in a cell cycle-dependent manner:
Cdc48p enters the nucleus during late G1; VCP aggregates at the
centrosome during mitosis. The nuclear import signal sequence of Cdc48p
was localized near the amino terminus and its function demonstrated by
mutagenesis. The nuclear import is regulated by a cell cycle-dependent
phosphorylation of a tyrosine residue near the carboxy terminus.
Two-hybrid studies indicate that the phosphorylation results in a
conformational change of the protein, exposing the nuclear import
signal sequence previously masked by a stretch of acidic residues.
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