Identification of N-WASP homologs in human and rat brain

Fukuoka, Maiko; Miki, Hiroaki; Takenawa, Tadaomi

doi:10.1016/s0378-1119(97)00184-4

Cited by 46 publications

(25 citation statements)

References 19 publications

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“…Antibodies against N-WASP and WISH were prepared as described previously (27,28). Other primary antibodies included rabbit polyclonal anti-WAVE antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) and mouse monoclonal antibodies to Ab (Chemicon, Temecula, CA, USA), Rac1 (BD Transduction Laboratories, Lexington, KY, USA), and Cdc42 (Santa Cruz Biotechnology).…”

Section: Methodsmentioning

confidence: 99%

Involvement of Wiskott-Aldrich Syndrome Protein Family Verprolin-Homologous Protein (WAVE) and Rac1 in the Phagocytosis of Amyloid-β(1 – 42) in Rat Microglia

et al. 2003

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Section: Methodsmentioning

confidence: 99%

Involvement of Wiskott-Aldrich Syndrome Protein Family Verprolin-Homologous Protein (WAVE) and Rac1 in the Phagocytosis of Amyloid-β(1 – 42) in Rat Microglia

et al. 2003

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“…Although Src activation and cortactin tyrosine phosphorylation are coincident with thrombin-mediated platelet activation following binding to a IIB b 3 integrin (Fox et al, 1993), there is also evidence that the hematopoieticspec®c kinase Syk plays an important role in cortactin tyrosine phosphorylation during platelet maturation and activation. Syk is homologous to the lymphocyte- Derry et al (1995) (WASP), Fukuoka et al (1997) (N-WASP) and Bear et al (1998) (Scar-1). (c) Src tyrosine phosphorylation sites on cortactin conform to a consensus SH2-binding motif.…”

Section: Cortactin As a Target For Tyrosine And Serine/threonine Protmentioning

confidence: 99%

Cortactin: coupling membrane dynamics to cortical actin assembly

2001

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Exposure of cells to a variety of external signals causes rapid changes in plasma membrane morphology. Plasma membrane dynamics, including membrane ru e and microspike formation, fusion or ®ssion of intracellular vesicles, and the spatial organization of transmembrane proteins, is directly controlled by the dynamic reorganization of the underlying actin cytoskeleton. Two members of the Rho family of small GTPases, Cdc42 and Rac, have been well established as mediators of extracellular signaling events that impact cortical actin organization. Actin-based signaling through Cdc42 and Rac ultimately results in activation of the actin-related protein (Arp) 2/3 complex, which promotes the formation of branched actin networks. In addition, the activity of both receptor and non-receptor protein tyrosine kinases along with numerous actin binding proteins works in concert with Arp2/3-mediated actin polymerization in regulating the formation of dynamic cortical actin-associated structures. In this review we discuss the structure and role of the cortical actin binding protein cortactin in Rho GTPase and tyrosine kinase signaling events, with the emphasis on the roles cortactin plays in tyrosine phosphorylation-based signal transduction, regulating cortical actin assembly, transmembrane receptor organization and membrane dynamics. We also consider how aberrant regulation of cortactin levels contributes to tumor cell invasion and metastasis. Oncogene (2001) 20, 6418 ± 6434.

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“…Following gel excision and tryptic digestion, SH3-interacting proteins were identified by either MALDI-TOF MS or LC-MS/MS. Among the proteins identified were CMS/CD2AP, subsequently referred to as CD2AP (22,23), FISH (37), ASAP1 (38), and N-WASP (39). The MALDI mass fingerprint obtained for CD2AP is shown in Fig.…”

Section: Identification Of Proteins Binding To the Sh3 Domain Ofmentioning

confidence: 99%

A Cortactin-CD2-associated Protein (CD2AP) Complex Provides a Novel Link between Epidermal Growth Factor Receptor Endocytosis and the Actin Cytoskeleton

Lynch

Winata

Lyons

et al. 2003

Journal of Biological Chemistry

208

194

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Growth factor regulation of the cortical actin cytoskeleton is fundamental to a wide variety of cellular processes. The cortical actin-associated protein, cortactin, regulates the formation of dynamic actin networks via the actin-related protein (Arp)2/3 complex and hence is a key mediator of such responses. In order to reveal novel roles for this versatile protein, we used a proteomics-based approach to isolate cortactin-interacting proteins. This identified several proteins, including CD2-associated protein (CD2AP), as targets for the cortactin Src homology 3 domain. Co-immunoprecipitation of CD2AP with cortactin occurred at endogenous expression levels, was transiently induced by epidermal growth factor (EGF) treatment, and required the cortactin Src homology 3 domain. The CD2AP-binding site for cortactin mapped to the second of three proline-rich regions. Because CD2AP is closely related to Cbl-interacting protein of 85 kDa (CIN85), which regulates growth factor receptor down-regulation via complex formation with Cbl and endophilin, we investigated whether the CD2AP-cortactin complex performs a similar function. EGF treatment of cells led to transient association of Cbl and the epidermal growth factor receptor (EGFR) with a constitutive CD2AP-endophilin complex. Cortactin was recruited into this complex with slightly delayed kinetics compared with Cbl and the EGFR. Immunofluorescence analysis revealed that the EGFR, CD2AP, and cortactin co-localized in regions of EGF-induced membrane ruffles. Therefore, by binding both CD2AP and the Arp2/3 complex, cortactin links receptor endocytosis to actin polymerization, which may facilitate the trafficking of internalized growth factor receptors.Subcellular compartmentalization and trafficking of signal transduction complexes and a variety of dynamic cellular responses to extracellular stimuli require regulated interactions between specific components of signaling pathways and the cytoskeleton. These interactions may be direct or mediated by particular adaptor or scaffolding proteins. Among these, cortactin was identified as a v-Src substrate associated with the cortical actin cytoskeleton approximately a decade ago, although insights into its cellular function and the underlying mechanisms have only been obtained recently (1).In line with an adaptor role, cortactin is a multidomain protein, with the individual modules capable of mediating specific protein-protein interactions (1). The N-terminal region mediates binding to the Arp 1 2/3 complex, a highly conserved regulator of the assembly and structure of actin networks (2), and contains a DDW motif characteristic of Arp2/3-interacting proteins such as WASP, Myo3p, and ActA (2, 3). This is followed by six and a half copies of a 37-amino acid repeat, with the fourth repeat necessary for binding to F-actin in vitro (2). Downstream of the repeats is a predicted helical domain and a region rich in serine, threonine, and proline residues. The latter is a target for both tyrosine and serine/threonine phosphorylation (4 -6)....

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Identification of N-WASP homologs in human and rat brain

Cited by 46 publications

References 19 publications

Involvement of Wiskott-Aldrich Syndrome Protein Family Verprolin-Homologous Protein (WAVE) and Rac1 in the Phagocytosis of Amyloid-β(1 – 42) in Rat Microglia

Involvement of Wiskott-Aldrich Syndrome Protein Family Verprolin-Homologous Protein (WAVE) and Rac1 in the Phagocytosis of Amyloid-β(1 – 42) in Rat Microglia

Cortactin: coupling membrane dynamics to cortical actin assembly

A Cortactin-CD2-associated Protein (CD2AP) Complex Provides a Novel Link between Epidermal Growth Factor Receptor Endocytosis and the Actin Cytoskeleton

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