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Vol. 10, Issue 7, 2221-2233, July 1999
with HLH-Zip
and
§
*Department of Anatomy and Cell Biology, The sterol regulatory element-binding protein-2 (SREBP-2) is
produced as a large precursor molecule attached to the endoplasmic reticulum membrane. In response to the sterol depletion, the N-terminal segment of the precursor, which contains a basic
helix-loop-helix-leucine zipper domain, is released by two sequential
cleavages and is translocated to the nucleus, where it activates the
transcription of target genes. The data herein show that released
SREBP-2 uses a distinct nuclear transport pathway, which is mediated by
importin Laboratory of Biochemistry and Molecular Biology,Institute for Molecular and Cellular Biology,
. The mature form of SREBP-2 is actively transported into
the nucleus when injected into the cell cytoplasm. SREBP-2 binds
directly to importin in the absence of importin 
. Ran-GTP but
not Ran-GDP causes the dissociation of the SREBP-2-importin complex. G19VRan-GTP inhibits the nuclear import of SREBP-2 in living
cells. In the permeabilized cell in vitro transport system, nuclear
import of SREBP-2 is reconstituted only by importin in conjunction
with Ran and its interacting protein p10/NTF2. We further demonstrate that the helix-loop-helix-leucine zipper motif of SREBP-2 contains a
novel type of nuclear localization signal, which binds directly to
importin .
§
Corresponding author: E-mail address:
yyoneda{at}anat3.med.osaka-u.ac.jp.
Molecular Biology of the Cell
Vol. 10, 2221-2233, July 1999
Copyright © 1999 by The American Society for Cell Biology
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