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Study provides evidence that WIP and WIRE contribute to breast cancer cell invasiveness through coordinated roles. WIP seems necessary for the assembly of invasive protrusions, whereas WIRE regulates their maturation, which leads to matrix degradation.
conclude that tyrosine phosphorylation of WIP is a crucial regulator of WASP stability and function as an actin-nucleation-promoting factor
WIP was shown to interact with various binding partners, including the signaling proteins Nck (show NCK1 ELISA Kits), CrkL (show CRKL ELISA Kits) and cortactin (show CTTN ELISA Kits).
Data indicate the WASp-interacting protein (WIP)-Wiskott-Aldrich syndrome protein (WASp) interaction in the regulation of actin-dependent processes.
These findings reveal WIP as a previously unreported regulator of neuronal maturation and synaptic activity
These findings indicate that WIP deficiency should be suspected in patients with features of WAS in whom WAS sequence and mRNA levels are normal.
The results suggest that some of the mutations in the WH1 domain cause the Wiskott-Aldrich syndrome (show WASL ELISA Kits) syndrome in humans by perturbing the WASP (show WASL ELISA Kits)-WIP complex formation.
show that the N-WASP (show WASL ELISA Kits) EVH1 domain specifically binds a 25 residue motif from the WASP Interacting Protein (WIP)
X-linked thrombocytopenia caused by a mutation in the WAS gene that disrupts interaction with the (WASP)-interacting protein (WIP).
interactions of WASP (show WASL ELISA Kits) and WIP are affected by two novel mutations that change the conformation of WASP (show WASL ELISA Kits) and disrupt hydrogen bonding
These experiments identify WIP as a member of a signaling cascade comprised of Abl (show ABL1 ELISA Kits) family kinases, mTORC1 and S6K (show RPS6KB1 ELISA Kits), which regulates neuron development and specifically, neuritic branching and complexity.
WIP is a link between membrane lipid composition and actin cytoskeleton at dendritic spines.
WIPf1 deficiency results in defective B cell function. By regulating the cortical actin cytoskeleton, WIPf1 influences the function of CD19 (show CD19 ELISA Kits) as a general hub for PI3K signaling.
WIP binding to actin, independently of its binding to Wiskott-Aldrich syndrome protein, is critical for the integrity of the actin cytoskeleton in T cells and for their migration into tissues.
Results show that WIP is a novel regulator of focal adhesion assembly and cell adhesion.
Data indicate the involvement of WIP (WASP Interacting Protein) in the control of migratory persistence in both mesenchymal (fibroblast) and amoeboid (B lymphocytes) motility.
Using mouse embryonic fibroblasts lacking Nck, WIP, or N-WASP, this study investigated whether an interaction of Nck with both WIP and N-WASP is required for their recruitment to vaccinia during Arp2/3-dependent actin assembly.
These data highlight similar pathogenic strategies shared by EPEC and vaccinia virus by demonstrating a requirement for both Nck and N-WASP, but not WIP or WIP family members in pathogen-induced actin assembly.
This study implicates WIP in enteropathogenic Escherichia coli-mediated actin polymerization and pedestal elongation.
These findings identify a novel role for mAbp1 (show DBNL ELISA Kits) in growth factor-induced dorsal ruffle formation through its interaction with WIP.
This gene encodes a protein that plays an important role in the organization of the actin cytoskeleton. The encoded protein binds to a region of Wiskott-Aldrich syndrome protein that is frequently mutated in Wiskott-Aldrich syndrome, an X-linked recessive disorder. Impairment of the interaction between these two proteins may contribute to the disease. Two transcript variants encoding the same protein have been identified for this gene.
WAS/WASL interacting protein family, member 1
, WAS/WASL-interacting protein family member 1
, Wiskott-Aldrich syndrome protein interacting protein
, WASP interacting protein
, WASP-interacting protein
, protein PRPL-2
, wiskott-Aldrich syndrome protein-interacting protein