Filling gaps in signaling to actin cytoskeletal remodeling.
A recent publication in the April 4 issue of Cell advances our understanding of stimulus response coupling leading to actin remodeling. It describes the identification of a novel membrane component Mig-2 that engages filamin A through a new intermediary, migfilin, to stimulate actin assembly and cell spreading on a substrate of extracellular matrix.
Stossel
Thomas P
TP
Hematology Division, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Avenue, Boston, MA 02115, USA.
Hartwig
John H
JH
D000199:Actins / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D003285:Contractile Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000378:metabolism*; D005109:Extracellular Matrix / Q000378:metabolism*; D064448:Filamins; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism; D011485:Protein Binding / Q000235:genetics; D015398:Signal Transduction / Q000235:genetics; D020744:rac GTP-Binding Proteins / Q000378:metabolism
D000199:Actins; D029742:Caenorhabditis elegans Proteins; D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; C442327:Mig-2 protein, C elegans; D020744:rac GTP-Binding Proteins