Caldesmon suppresses cancer cell invasion by regulating podosome/invadopodium formation.
The podosome and invadopodium are dynamic cell-adhesion structures that degrade the extracellular matrix (ECM) and promote cell invasion. We recently reported that the actin-binding protein caldesmon is a pivotal regulator of podosome formation. Here, we analyzed the caldesmon's involvement in podosome/invadopodium-mediated invasion by transformed and cancer cells. The ectopic expression of caldesmon reduced the number of podosomes/invadopodia and decreased the ECM degradation activity, resulting in the suppression of cell invasion. Conversely, the depletion of caldesmon facilitated the formation of podosomes/invadopodia and cell invasion. Taken together, our results indicate that caldesmon acts as a potent repressor of cancer cell invasion.
Yoshio
T
T
Department of Neuroscience (D13), Osaka University Graduate School of Medicine, Osaka 565-0871, Japan.
Morita
T
T
Kimura
Y
Y
Tsujii
M
M
Hayashi
N
N
Sobue
K
K
D000818:Animals; D001943:Breast Neoplasms / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D002277:Carcinoma / Q000378:metabolism; D002461:Cell Line, Transformed; D045744:Cell Line, Tumor; D022081:Cell Surface Extensions / Q000378:metabolism*; D002472:Cell Transformation, Viral; D002999:Clone Cells; D003110:Colonic Neoplasms / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D019085:Fluorescent Antibody Technique, Direct; D006801:Humans; D009361:Neoplasm Invasiveness; D009374:Neoplasms, Experimental / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D052736:Rous sarcoma virus / Q000378:metabolism; D014162:Transfection
D002148:Calmodulin-Binding Proteins