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Recruitment of Paxillin (show PXN Proteins), Cdc42 (show CDC42 Proteins) and N-WASP is necessary for cell adhesion, migration and invasion induced by Estradiol in breast cancer cells.
Results suggest that local invasiveness of ameloblastoma is dependent upon the migratory potential of its tumour cells as defined by their distribution of cortactin, N-WASP and WIP in correlation with F-actin cytoskeletal dynamics.
A Treg-specific role for WASP is required for prevention of Th2 effector cell differentiation and allergic sensitization to dietary antigens.
WASP and SCAR drive pseudopod formation and are conserved in actin-filled pseudopod-based motility.
Authors show that knock-down of WASp or expression of Y102F mutant of WASp decreases colony formation and in vivo tumor growth. Results show that WASp is a novel substrate of ALK and has a critical role in regulating invasiveness and oncogenesis of ALCL.
this study describes an Iranian boy with Wiskott-Aldrich syndrome with a novel WASP mutation
The inducible recruitment of WASp to the TCR-CD3 (show CD3 Proteins) complex is partially dependent of tyrosine phosphorylation of Cd3e (show CD3E Proteins).
This suggests that TOCA1 binding to Cdc42 is an early step in the Cdc42-dependent pathways that govern actin dynamics, and the differential binding affinities of the effectors facilitate a handover from TOCA1 to N-WASP, which can then drive recruitment of the actin-modifying machinery.
the Cdc42 (show CDC42 Proteins)/Nwasp/stress fibers/YAP (show YAP1 Proteins) signal pathway may potentially play an important role in regulating podocyte apoptosis. Maintaining necessary Cdc42 (show CDC42 Proteins) would be one potent way to prevent proteinuria kidney diseases.
Low GAS7C increases cancer cell motility by promoting N-WASP/FAK (show PTK2 Proteins)/F-actin cytoskeleton dynamics. It also enhances beta-catenin (show CTNNB1 Proteins) stability via hnRNP U (show HNRNPU Proteins)/beta-TrCP (show BTRC Proteins) complex formation.
Myogenic differentiation depends on the expression regulation patterns of Grb2 (show GRB2 Proteins) and N-WASP.
DOCK8 and WASp are in the same signaling pathway that links T-cell receptors (TCRs) to the actin cytoskeleton in TCR-driven actin assembly.
the dendritic cell actin cytoskeleton organized into recognizable synaptic structures, formed Wiskott-Aldrich syndrome protein-dependent podosomes within this area.
N-WASP expression in B lymphocytes is required for the development of autoimmunity of WAS (Wiskott-Aldrich syndrome) and may represent a novel therapeutic target in WAS.
Data (including data from studies in knockout mice) suggest that Cnr1 (cannabinoid receptor 1 (show CNR1 Proteins)) activation impacts actin cytoskeleton polymerization/stability via Wasl in growth cones of developing neurons and in synaptic spines of mature neurons.
Platelet actin nodule formation is dependent on WASp and the ARP2 (show AICDA Proteins)/3 complex. WASp(-/-) mouse blood displays impaired platelet aggregate formation at arteriolar shear rates.
Our data suggests that the N-WASP-Arp2/3 actin polymerization machinery generates branched-actin arrays at an advanced stage of blood-testis barrier remodeling.
Findings suggest that Wiskott-Aldrich syndrome protein (WASp) plays a crucial role in B10 cell development and that WASp-deficient B10 cells may contribute to autoimmunity in Wiskott-Aldrich syndrome.
N-terminus of Cas (show CTNND1 Proteins) associates with the FAK (show PTK2 Proteins)-N-WASP complex at the protrusive edge of the cell and that the C-terminus of Cas (show CTNND1 Proteins) associates with the immobilized integrin-SFK cluster.
These results strongly suggest that the association between the WASP N-terminal domain and Btk plays an important role in the TLR2-signaling pathway in macrophages.
N-WASP WWCA domains can processively attach to growing barbed-end bundles and increase their diffusion-limited elongation rate.
The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. The presence of a number of different motifs suggests that they are regulated by a number of different stimuli, and interact with multiple proteins. Recent studies have demonstrated that these proteins, directly or indirectly, associate with the small GTPase, Cdc42, known to regulate formation of actin filaments, and the cytoskeletal organizing complex, Arp2/3. The WASL gene product is a homolog of WAS protein, however, unlike the latter, it is ubiquitously expressed and shows highest expression in neural tissues. It has been shown to bind Cdc42 directly, and induce formation of long actin microspikes.
, Wiskott-Aldrich syndrome, like
, neural Wiskott-Aldrich syndrome protein
, Wiskott-Aldrich syndrome gene-like protein
, thrombocytopenia 1 (X-linked)
, wiskott-Aldrich syndrome protein
, Wiskott-Aldrich syndrome homolog
, wiskott-Aldrich syndrome protein homolog