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J. Biol. Chem., Vol. 278, Issue 14, 12175-12181, April 4, 2003

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A New Member of the LIM Protein Family Binds to Filamin B and Localizes at Stress Fibers^*

Toshiro Takafuta^§¶, Mari Saeki^¶, Tetsuro-Takahiro Fujimoto, Kingo Fujimura, and Sandor S. Shapiro^**

From the  Department of Medicine, Cardeza Foundation for Hematologic Research, Jefferson Medical College, Philadelphia, Pennsylvania 19041, the ^§ Department of Clinical and Laboratory Medicine, Yamanashi Medical University, Yamanashi 409-3898, Japan, and the  Department of Clinical Pharmaceutical Science, Graduate School of Medicine, Hiroshima University, Hiroshima 734-8551, Japan

Human filamins are 280-kDa proteins containing an N-terminal actin-binding domain followed by 24 characteristic repeats. They also interact with a number of other cellular proteins. All of those identified to date, with the exception of actin, bind to the C-terminal third of a filamin. In a yeast two-hybrid search of a human placental library, using as bait repeats 10-18 of filamin B, we isolated a cDNA coding for a novel 374 amino acid protein containing a proline-rich domain near its N terminus and two LIM domains at its C terminus. We term this protein filamin-binding LIM protein-1, FBLP-1. Yeast two-hybrid studies with deletion mutants localized the areas of interaction in FBLP-1 to its N-terminal domain and in filamin B to repeats 10-13. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. We also have identified two FBLP-1 variants. Both contain three C-terminal LIM domains, but one lacks the N-terminal proline-rich domain. Transfection of FBLP-1 into 293A cells promoted stress fiber formation, and both FBLP-1 and filamin B localized to stress fibers in the transfected cells. The association between filamin B and FBLP-1 may play a hitherto unknown role in cytoskeletal function, cell adhesion, and cell motility.

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