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J Biol Chem, Vol. 274, Issue 38, 27083-27091, September 17, 1999
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From the We have cloned and characterized a novel isoform
of the skeletal muscle LIM protein 1 (SLIM1), designated SLIMMER. SLIM1
contains an N-terminal single zinc finger followed by four LIM domains. SLIMMER is identical to SLIM1 over the first three LIM domains but
contains a novel C-terminal 96 amino acids with three potential bipartite nuclear localization signals, a putative nuclear export sequence, and 27 amino acids identical to the RBP-J binding region of
KyoT2, a murine isoform of SLIM1. SLIM1 localized to the cytosol of
Sol8 myoblasts and myotubes. SLIMMER was detected in the nucleus of
myoblasts and, following differentiation into myotubes, was exclusively
cytosolic. Recombinant green fluorescent protein-SLIM1 localized to the
cytoplasm and associated with focal adhesions and actin filaments in
COS-7 cells, while green fluorescent protein-SLIMMER was predominantly
nuclear. SLIMMER truncation mutants revealed that the first nuclear
localization signal mediates nuclear localization. The addition of the
proposed nuclear export sequence decreased the level of exclusively
nuclear expression and increased cytosolic SLIMMER expression in COS-7
cells. The leucine-rich nuclear export signal was required for the
export of SLIMMER from the nucleus of myoblasts to the cytoplasm of
myotubes. Collectively, these results suggest distinct roles for SLIM1
and SLIMMER in focal adhesions and nuclear-cytoplasmic communication.
Department of Biochemistry and Molecular
Biology, Monash University, Clayton, Victoria, Australia 3168 and the
¶ Department of Anatomy and Cell Biology, SUNY Health Science
Center, Syracuse, New York 13210
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