High impact information on FBLIM1

• Loss of Mig-2 or migfilin impairs cell shape modulation [1].
• Together, Mig-2, migfilin and filamin define a connection between cell matrix adhesions and the actin cytoskeleton and participate in the orchestration of actin assembly and cell shape modulation [1].
• We show here that migfilin, a LIM-containing protein, localizes to cell-matrix adhesions, associates with actin filaments, and is essential for cell shape modulation [1].
• Functionally, migfilin facilitates VASP localization to cell-matrix adhesions [2].
• Loss of migfilin impairs cell migration [2].

Biological context of FBLIM1

• The association between filamin B and FBLP-1 may play a hitherto unknown role in cytoskeletal function, cell adhesion, and cell motility [3].
• 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 [3].
• Migfilin also travels from the cytoplasm into the nucleus, a process that is regulated by RNA splicing and calcium signaling [4].

Anatomical context of FBLIM1

• Migfilin therefore functions as an important scaffold at cell-matrix adhesions [1].
• FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells [3].
• Finally, siRNA-mediated depletion of migfilin compromised the organization of adherens junctions and weakened cell-cell association [5].
• Immunoelectron microscopic analyses reveal that migfilin is closely associated with beta-catenin, but not desmosomes, at cell-cell junctions [5].

Associations of FBLIM1 with chemical compounds

• The interaction is mediated by the VASP EVH1 domain and a single L(104)PPPPP site located within the migfilin proline-rich domain [2].
• In this specific case, displacement of integrin tails from filamin by migfilin may provide a mechanism for switching between different integrin-cytoskeleton linkages [6].

Other interactions of FBLIM1

• 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 [3].
• We report here that migfilin, a recently identified component of cell-extracellular matrix adhesions, is recruited to cell-cell junctions in response to cadherin-mediated cell-cell adhesions [5].

References