Regulating filopodial dynamics through actin-depolymerizing factor/cofilin.
The regulation of filopodial dynamics by neurotrophins and other guidance cues plays an integral role in growth cone pathfinding. Filopodia are F-actin-based structures that explore the local environment, generate forces and play a role in growth cone translocation. Here, we review recent research showing that the actin-depolymerizing factor (ADF)/cofilin family of proteins mediates changes in the length and number of growth cone filopodia in response to brain-derived neurotrophic factor (BDNF). Although inhibition of myosin contractility also causes filopodial elongation, the elongation in response to BDNF does not occur through a myosin-dependent pathway. Active ADF/cofilin increases the rate of cycling between the monomer and polymer pools and is critical for the BDNF-induced changes. Thus, we discuss potential mechanisms by which ADF/cofilin may affect filopodial initiation and length change via its effects on F-actin dynamics in light of past research on actin and myosin function in growth cones.
Fass
Joseph
J
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870, USA.
Gehler
Scott
S
Sarmiere
Patrick
P
Letourneau
Paul
P
Bamburg
James R
JR
D051339:Actin Depolymerizing Factors; D000818:Animals; D045744:Cell Line, Tumor; D051345:Destrin; D020439:Growth Cones / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D051379:Mice; D008840:Microfilament Proteins / Q000378:metabolism* / Q000648:ultrastructure; D009419:Nerve Tissue Proteins / Q000378:metabolism* / Q000648:ultrastructure
D051339:Actin Depolymerizing Factors; C495824:DSTN protein, human; D051345:Destrin; C495825:Dstn protein, mouse; D008840:Microfilament Proteins; D009419:Nerve Tissue Proteins