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|Author:||Bandyopadhyay Aditi A|
J Cell Sci
Functional differences between kindlin-1 and kindlin-2 in keratinocytes.
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FBLIM1, also known as CAL, Mig-2-interacting protein or Migfilin, is a cytoplasmic protein that belongs to the LIM superfamily. FBLIM1 is a protein found in cell-cell and cell-ECM connections where it co-localizes with FLNA/C and FLNB. FBLIM1 was found to bind directly to FLNA/C and to be an important regulator of cell shape and motility. FBLIM1 exerts its influence on cellular functions by interacting with various binding partners; FLN via its N- terminal domain, VASP and Src via its proline-rich region, and kindlin-2 and the cardiac transcription factor, CSX/NKX2-5 via its C-terminal LIM domains. Three isoforms exist for FBLIM1 due to alternative splicing events, namely FBLP-1A, FBLP-1 and FBLP-1B. FBLIM1 serves as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. It is associated with actin stress fiber at cell-ECM focal adhesion sites. FBLP-1A and FBLP-1B are recruited and localized at actin stress fibers and clustered at cell-EMC adhesion sites through interaction with PLEKHC1. FBLP-1 is localized at actin stress fibers. FBLIM1 is implicated in cell shape modulation (spreading) and motility. FBLIM1 participate in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. It may also regulate the assembly of filamin-containing signaling complexes that control actin assembly. In addition, FBLIM1 is capable of translocating to the nucleus and regulating gene expression. This antibody is a rabbit polyclonal antibody raised against full length human FBLIM1 antigen.