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Papers In Press, published online ahead of print December 20, 2002
Cardeza Foundation, Department of Medicine, Jefferson Medical College, Philadelphia, PA 19107
Corresponding Author: Sandor.Shapiro{at}mail.tju.edu
Human filamins are 280 kD proteins containing an N-terminal actin-binding domain followed by 24 characteristic repeats. They also interact with a number of other cellular proteins. All those identified to date, except actin, bind to the C-terminal half 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 (PRD) 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.
J. Biol. Chem, 10.1074/jbc.M209339200
Submitted on September 11, 2002
Revised on December 6, 2002
Accepted on December 20, 2002
A new member of the LIM protein family binds to filamin B and localizes at stress fibers
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