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The protein encoded by FMNL3 contains a formin homology 2 domain and has high sequence identity to the mouse Wbp3 protein.
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Activated FMNL3 triggers microtubule stabilization and is required for this alignment in vascular endothelial cells during angiogenesis.
FMNL3, the target gene of miR (zeige MLXIP ELISA Kits)-127, is upregulated and acting as an oncogene (zeige RAB1A ELISA Kits) in ESCC
we use a simple cellular system to examine fundamental features of formin (zeige FMN1 ELISA Kits)-mediated filopodial assembly, using constitutively active constructs of the formins mDia2 and FMNL3
FMNL3 interacts with Cdc42 and RhoJ, two Rho family GTPases known to be required for lumen formation. FMNL3 and RhoJ are concentrated at the early apical surface, or AMIS, and regulate the formation of radiating actin cables from this site.
FMNL3 functions in assembly of actin-based protrusions that are specialized for cell-cell adhesion.
FMNL3 plays an important role in the progression and metastasis of colorectal carcinoma and may be a novel potential prognostic predictor in colorectal carcinoma.
miR-335 regulates the expression of at least five formin family members, three of which are validated, FMNL3, FMN2 and DAAM2.
Formin-like 3 (FMNL3) is a crucial regulator of endothelial cell elongation during angiogenesis.
Protein N-myristoylation plays critical roles in the cellular morphological changes induced by FMNL2 (zeige FMNL2 ELISA Kits) and FMNL3.
Data suggest that the FH2 domain of FRL2 possesses properties not shared by FRL1 that allow it to generate filopodia.
3.4-A structure of FMNL3 FH2 dimer in complex with tetramethylrhodamine-actin uncovers details of formin (zeige FMN1 ELISA Kits)-regulated actin elongation; structure provides details for FH2-mediated filament elongation by processive capping and supports a model in which C-terminal non-FH2 residues of FMNL3 are required to stabilize the filament nucleus
The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends.
The protein encoded by this gene contains a formin homology 2 domain and has high sequence identity to the mouse Wbp3 protein. Two alternative transcripts encoding different isoforms have been described.
, WW domain binding protein 3
, WW domain-binding protein 3
, formin homology 2 domain-containing protein 3
, formin-like protein 3
, formin-like 3 protein