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Fmn2 mutant mice develop accelerated age-associated memory decline that is further increased in the presence of additional risk factors and is mechanistically linked to a loss of transcriptional homeostasis.
FMN2 promotes cell survival by limiting nuclear envelope damage & DNA double-strand breaks; FMN2 is upregulated in human melanomas & disruption of FMN2 in mouse melanoma cells inhibits their extravasation & metastasis to the lung; FMN2 generates a perinuclear actin/focal adhesion system that protects the nucleus and DNA from damage to promote cell survival during confined migration & thus promote cancer metastasis.
This DNA damage-induced nuclear actin assembly requires two biologically and physically linked nucleation factors: Formin-2 and Spire-1 (show SPIRE1 ELISA Kits)/Spire-2.
We therefore characterized co-expressed Spir-2 (show SPIRE1 ELISA Kits) and Fmn-2 fluorescent protein fusions . The data corroborate a model according to which Spir-2 (show SPIRE1 ELISA Kits) exists in two different states, a cytosolic monomeric conformation and a membrane-bound state
FMN2 mutations link intellectual disability either directly or indirectly to the regulation of actin-mediated synaptic spine density.
miR-335 regulates the expression of at least five formin family members, three of which are validated, FMNL3, FMN2 and DAAM2.
FMN2 is a crucial protein involved in the control of p21 (show CDKN1A ELISA Kits).
results identify FMN2 as a crucial component in the regulation of p21 (show CDKN1A ELISA Kits) and consequent oncogene (show RAB1A ELISA Kits)/stress-induced cell-cycle arrest in human cells.
analysis of the molecular basis of the Spir1/formin-2 interaction
FMN2 was characterized at human chromosome 1q43.
Fmn2 as a mediator of actin bundle integrity, enabling efficient force transmission to the adhesion sites.
Data suggest formin homology domain (FH2) of Fmn2 binds actin at filament barbed end as weak capper and plays a role in displacing WASP homology domain 2 (WH2) domains of Spire-1 from actin; competitive binding of Fmn2 vs Spire-1 aids actin assembly.
Spire recruits Fmn2 and facilitates its association with actin filaments barbed ends.
Results suggest that the regulation of microtubule acetylation is likely a general formin (show FMN1 ELISA Kits) activity.
Spire1 (show SPIRE1 ELISA Kits) and Spire2 cooperate with Formin-2 (Fmn2) to nucleate actin filaments in mouse oocytes.
High formin 2 levels at meiosis I entry induce meshwork maintenance, leading to equal forces being exerted on the chromosomes, preventing spindle migration.
Gene profiling of Fmn2 in Graffi murine leukemia virus-induced lymphoid leukemias suggest its important role in leukemogenesis.
Formin homology (FH) domain proteins (see FMN1\; MIM 136535) play a role in cytoskeletal organization and/or establishment of cell polarity.