Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP

@article{Miki1998InductionOF,
  title={Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP},
  author={Hiroaki Miki and Takuya Sasaki and Yoshimi Takai and Tadaomi Takenawa},
  journal={Nature},
  year={1998},
  volume={391},
  pages={93-96}
}
Cdc42 is a small GTPase of the Rho family which regulates the formation of actin filaments to generate filopodia,. Although there are several proteins such as PAK, ACK and WASP (Wiskott–Aldrich syndrome protein) that bind Cdc42 directly, none of these can account for the filopodium formation induced by Cdc42. Here we demonstrate that before it can induce filopodium formation, Cdc42 must bind a WASP-related protein, N-WASP, that is richest in neural tissues but is expressed ubiquitously. N-WASP… 
WIP regulates N-WASP-mediated actin polymerization and filopodium formation
TLDR
It is shown that WASP-interacting protein (WIP) interacts directly with N-WASP and actin, which is consistent with their role in actin-tail formation in cells infected with vaccinia virus or Shigella.
Comment How WASP Regulates Actin Polymerization
TLDR
The isolated native WASP from thymus is isolated and shown that it is indeed inactive until stimulated, and the known binding of N-WASP’s COOH terminus by its NH 2 terminus has now been shown to inhibit the ability of the COOh terminus to activate actin nucleation, illuminating the molecular basis of this regulation.
WASP family members and formin proteins coordinate regulation of cell protrusions in carcinoma cells
TLDR
Data show that coordinate regulation between the WASP family and mDia proteins controls the balance between lamellar and lamellipodial protrusion activity.
Cytoskeletal alterations in Dictyostelium induced by expression of human cdc42.
TLDR
Human cdc42 has various effects on the Dictyostelium actin cytoskeleton consistent with a conserved role of small GTPases in control of the cytos skeleton.
Regulation of actin cytoskeleton by mDab1 through N-WASP and ubiquitination of mDab1.
TLDR
It is shown that mDab1 associates with N-WASP (neuronal Wiskott-Aldrich syndrome protein) in vitro and in brains of embryonic mice, which suggests that m Dab1 regulates the actin cytoskeleton through N-wASP, which is negatively regulated by phosphorylation-mediated ubiquitination of mDAb1.
The Toca-1-N-WASP Complex Links Filopodial Formation to Endocytosis
TLDR
It is reported that Toca-1 induces filopodia and neurites as does N-WASP in N1E115 neuroblastoma cells, and three inhibitors of endocytosis, Dynamin-K44A, Eps15Δ95/295, and clathrin heavy chain RNA interference, block TOCA-1-induced Filopodial formation.
The Cdc42 Effector IRSp53 Generates Filopodia by Coupling Membrane Protrusion with Actin Dynamics*
TLDR
It is proposed that IRSp53 generates filopodia by coupling membrane protrusion through its I-BAR domain with actin dynamics through SH3 domain binding partners, including N-WASP and Mena.
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References

SHOWING 1-10 OF 16 REFERENCES
The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
TLDR
It is shown that microinjection of the related human Cdc42Hs into Swiss 3T3 fibroblasts induced the formation of peripheral actin microspikes, determined by staining with phalloidin, and that Cdc 42Hs plays an important role in determining mammalian cell morphology.
N‐WASP, a novel actin‐depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2‐dependent manner downstream of tyrosine kinases.
TLDR
It is concluded that N‐WASP transmits signals from tyrosine kinases to cause a polarized rearrangement of cortical actin filaments dependent on PIP2.
The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia
TLDR
Results suggest that n-chimaerin acts synergistically with Rac1 and Cdc42Hs to induce actin-based morphological changes and that GAPs may have morphological functions in addition to downregulation of GTPases.
Identification, Characterization, and Intracellular Distribution of Cofilin in Dictyostelium discoideum(*)
TLDR
The results suggest that cofilin may be involved in dynamic reorganization of membranous actin cytoskeletons in vegetative cells under starvation stress.
How profilin promotes actin filament assembly in the presence of thymosin β4
A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42
TLDR
The findings indicate that there may be a regulatory mechanism that sustains the GTP-bound active form of Cdc42Hs and which is directly linked to a tyrosine phosphorylation pathway.
Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin.
TLDR
Cofilin was found to inhibit the superprecipitation of actin-myosin mixtures as well as the act in-activated myosin ATPase and the nucleation assay suggested that cofilin shortens the actin filaments and hence increases the filament number.
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