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PubMed1983

Parasitization by the microhymenopteran Gryon triatomae Masner of eggs of Triatoma maculata (Erichson) in holes and mazes of artificial walls.

Oriental parasitoid wasps, Gryon triatomae, were confined for several weeks in transparent tanks (400 X 180 X 200 mm) with eggs of the neotropical triatomine bug Triatoma maculata. The eggs were lodged in moulded holes (about 50 mm deep and 15 mm diameter) of polystyrene blocks, to simulate walls. The blocks were arranged with the holes either vertical or horizontal; openings of the holes were either 5 mm or 15 mm diameter. One wall included three mazes of linked holes, each maze with one entrance. Eggs were also accessible in an open petri-dish and on top of one wall. Some eggs in the walls and the maze block were in holes sealed off from access by wasps to provide controls, in order to assess fertility of the eggs, since this favours parasitization. This was satisfactory at 82.2% and 88.5% in two tanks studied. Parasitization rates were 32% of 50 eggs exposed to one female G. triatomae, with one male wasp, in one tank, and in the other 55.9% of 136 eggs exposed to 14 female wasps, with five males. In both tanks, eggs in the open petri-dish, in accessible vertical and horizontal holes and on top of walls were parasitized, but parasitization of eggs in the mazes occurred only in the tank with 14 female Gryon and then as far as the last, 18th, hole of the longest maze, a linear penetration by a searching wasp of about 270 mm; the distance travelled could be considerably greater. Late wasp oviposition after protracted questing may have caused the observed 15.8% abortion rate of G. triatomae. The few wasps seen by night were at rest, but at daybreak many more emerged from the walls and flew actively.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1989

Segment W of Campoletis sonorensis virus: expression, gene products, and organization.

Campoletis sonorensis virus (CsV, Polydnaviridae) is a segmented double-stranded DNA virus which has an apparently symbiotic relationship with the parasitic wasp, Campoletis sonorensis. CsV replicates in the oviducts of the parasitic wasp and is injected into the wasp's host, Heliothis virescens (Lepidoptera; Noctuiidae), during oviposition. In the parasitized lepidopteran host, the virus has a dramatic effect on host physiology and viral gene products are believed to play an essential role in the survival of the parasitic wasp's egg and larva. In the current study, we used Northern blot analyses to examine expression from segment W in the parasitized host and in the parasitic wasp. Segment W hybridized primarily to two relatively abundant mRNAs (1.6 and 1.0 kb) from the parasitized host. These 1.6- and 1.0-kb mRNAs, which were previously shown to be transcribed from two closely related genes (WHv1 and WHv2) on segment W (G. W. Blissard, O. P. Smith, and M. D. Summers, 1987, Virology 160, 120-134) increased in relative abundance between 2 and 24 hr postparasitization (pp) and were detected throughout parasitization (8 days). To study the proteins encoded by these closely related genes, the open reading frame from each of the related genes was cloned into a baculovirus expression vector. By pulse labeling in the presence and absence of tunicamycin, we examined secretion and glycosylation of these CsV proteins in infected lepidopteran cells (Spodoptera frugiperda). Expression of segment W in the oviducts of the female wasp was also examined. Segment W hybridized to at least five CsV mRNAs on Northern blots of poly(A) mRNA from C. sonorensis oviducts. To identify specific CsV mRNAs and map putative viral genes expressed in wasp oviduct tissues, segment W was used to screen a cDNA library of C. sonorensis oviduct mRNAs. Three cDNAs were used to identify CsV mRNAs by Northern blot analyses and to map the locations of three putative CsV genes on segment W. Cross-hybridization within the CsV genome was examined with cloned segment W and with the three cloned cDNAs.

Amino Acid Sequence↗

PubMed2001

Successful removal of German yellowjackets (Hymenoptera: Vespidae) by toxic baiting.

Vespula germanica (F.) is a social vespid that has invaded many parts of the world, including Argentina. This wasp usually becomes a pest, affecting several economic activities. It also may impact the host community through predation or competition. The purpose of our study was to field test toxic baiting for reduction of wasp abundance. Wasps were poisoned with 0.1% fipronil mixed with raw minced beef in two beech forest sites on 20 February 2000 in northwestern Patagonia. All nests (46) within the two 6-ha sites with poisoned bait stations were killed, whereas Malaise traps in those sites captured 81.1% fewer wasps at the end of the season than traps in the two control sites. The average reduction of forager wasps on nontoxic baits was 87%. Fipronil was very effective in controlling wasp numbers, although there are limitations to the method, especially concerning conservation purposes. Toxic baiting can be useful in controlling wasp numbers in honey bee hive yards, farms, and parks.

Animals↗

PubMed2006

Wait-and-see prescription for the treatment of acute otitis media: a randomized controlled trial.

CONTEXT: Acute otitis media (AOM) is the most common diagnosis for which antibiotics are prescribed for children. Previous trials that have evaluated a "wait-and-see prescription" (WASP) for antibiotics, with which parents are asked not to fill the prescription unless the child either is not better or is worse in 48 hours, have excluded children with severe AOM. None of these trials were conducted in an emergency department. OBJECTIVES: To determine whether treatment of AOM using a WASP significantly reduces use of antibiotics compared with a "standard prescription" (SP) and to evaluate the effects of this intervention on clinical symptoms and adverse outcomes related to antibiotic use. DESIGN, SETTING, AND PATIENTS: A randomized controlled trial conducted between July 12, 2004, and July 11, 2005. Children with AOM aged 6 months to 12 years seen in an emergency department were randomly assigned to receive either a WASP or an SP. All patients received ibuprofen and otic analgesic drops for use at home. A research assistant, blinded to group assignment, conducted structured phone interviews 4 to 6, 11 to 14, and 30 to 40 days after enrollment to determine outcomes. MAIN OUTCOME MEASURES: Filling of the antibiotic prescription and clinical course. RESULTS: Overall, 283 patients were randomized either to the WASP group (n = 138) or the SP group (n = 145). Substantially more parents in the WASP group did not fill the antibiotic prescription (62% vs 13%; P<.001). There was no statistically significant difference between the groups in the frequency of subsequent fever, otalgia, or unscheduled visits for medical care. Within the WASP group, both fever (relative risk [RR], 2.95; 95% confidence interval [CI], 1.75 - 4.99; P<.001) and otalgia (RR, 1.62; 95% CI, 1.26 - 2.03; P<.001) were associated with filling the prescription. CONCLUSION: The WASP approach substantially reduced unnecessary use of antibiotics in children with AOM seen in an emergency department and may be an alternative to routine use of antimicrobials for treatment of such children. TRIAL REGISTRATION: clinicaltrials.gov Identifier: NCT00250900.

Acute Disease↗

PubMed1999

The identification and characterization of two promoters and the complete genomic sequence for the Wiskott-Aldrich syndrome gene.

The Wiskott-Aldrich syndrome (WAS) is an X-linked disorder characterized by immunodeficiency, eczema and thrombocytopenia. The gene responsible for WAS was identified through positional cloning, and the function of the encoded protein (WASP) is still the subject of much speculation. WASP is currently thought to be involved in the regulation of actin polymerization in hematopoietic cells. To study the elements that regulate the WASP gene, we have identified the sites for transcription initiation. We found that two promoters were responsible for controlling WASP expression. Multiple transcription initiation sites were found immediately adjacent to the translation start site, however an alternate exon with a second promoter region was identified 6 kb upstream. Examination of the 5' sequence adjacent to the initiation sites in both promoters failed to reveal a TATA or CCAAT box, but numerous putative transcription factor binding sites including Sp1, Ets, c-Myb and PU.1 were apparent. Reporter constructs generated from each promoter showed functional activity in the Jurkat T-cell and HEL erythro-megakaryocytic cell lines. Although the alternate exon sequence was extremely GC rich and contained several potential binding elements, the primary promoter was stronger than the upstream promoter in the cell lines assayed. The transcription factor binding site profiles within each promoter suggested that they may play different roles in regulating WASP expression depending on the stage of differentiation and development, and the cell lineage. In this study we have also reported the complete nucleotide sequence of the coding and intervening sequences for the WASP gene. A comprehensive knowledge of the genomic structure and the further characterization of WASP gene expression will facilitate the continued investigation of mutations in WAS patients, and the eventual prospect of gene therapy.

Base Sequence↗

PubMed2005

An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins.

The specific and rapid formation of protein complexes is essential for diverse cellular processes such as remodeling of actin filaments in response to the interaction between Rho GTPases and the Wiskott-Aldrich syndrome proteins (WASp and N-WASp). Although Cdc42, TC10, and other members of the Rho family have been implicated in binding to and activating the WAS proteins, the exact nature of such a protein-protein recognition process has remained obscure. Here, we describe a mechanism that ensures rapid and selective long-range Cdc42-WASp recognition. The crystal structure of TC10, together with mutational and bioinformatic analyses, proved that the basic region of WASp and two unique glutamates in Cdc42 generate favorable electrostatic steering forces that control the accelerated WASp-Cdc42 association reaction. This process is a prerequisite for WASp activation and a critical step in temporal regulation and integration of WASp-mediated cellular responses.

Amino Acid Sequence↗

PubMed1998

Tyrosine phosphorylation of the Wiskott-Aldrich syndrome protein by Lyn and Btk is regulated by CDC42.

The Wiskott-Aldrich syndrome (WAS) is a rare immunodeficiency disease affecting mainly platelets and lymphocytes. Here, we show that the WAS gene product, WASp, is tyrosine phosphorylated upon aggregation of the high affinity IgE receptor (Fc epsilonRI) at the surface of RBL-2H3 rat tumor mast cells. Lyn and the Bruton's tyrosine kinase (Btk), two protein tyrosine kinases involved in Fc epsilonRI-signaling phosphorylate WASp and interact with WASp in vivo. Interestingly, expression of a GTPase defective mutant form of CDC42, that interacts with WASp, is accompanied by a substantial increase in WASp tyrosine phosphorylation. This study suggests that activated CDC42 recruits WASp to the plasma membrane where it becomes phosphorylated by Lyn and Btk. We conclude that WASp represents a connection between protein tyrosine kinase signaling pathways and CDC42 function in cytoskeleton and cell growth regulation in hematopoietic cells.

Agammaglobulinaemia Tyrosine Kinase↗

PubMed1996

Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome.

BACKGROUND: Members of the Rho family of small GTPases play an essential role in controlling the motile behaviour of animal cells. Specifically, Cdc42 and Rac have been shown to induce the formation of filopodia and lamellipodia, respectively, at the cell periphery of Swiss 3T3 fibroblasts. In addition, both GTPases are required for progression through G1 phase of the cell cycle, possibly by regulating the activity of the Jun N-terminal kinase (JNK) signalling pathway. In order to examine more closely the mechanisms underlying the diverse functions of Rho GTPases in mammalian cells, we searched for downstream targets of these proteins. RESULTS: A yeast two-hybrid screen for proteins interacting with the human Cdc42 GTPase identified WASP, a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome (WAS). Recombinant WASP, expressed in Escherichia coli, also bound to Cdc42 and weakly to Rac, but not at all to Rho. The Cdc42/Rac-binding domain was identified in a region between amino acids 201-321 of WASP, and binding was dependent on Cdc42 and Rac being in the GTP-bound conformation. Furthermore, WASP did not catalyze GTPase activation or nucleotide exchange activity on Cdc42. CONCLUSIONS: Positional cloning has implicated WASP in causing WAS, and the protein is defective in patients suffering from the disease. WASP is expressed exclusively in cells of hematopoietic lineage, and lymphocytes from WAS patients have a distorted cell-surface and exhibit reduced proliferative capacity. WASP has recently been found to bind to the Src-homology 3 (SH3) domain of the adapter protein Nck. This observation, and the results presented here, suggest that WAS is the result of defects in signal transduction pathways regulated by Cdc42/Rac and Nck.

Amino Acid Sequence↗

PubMed2003

The Wiskott-Aldrich syndrome protein: forging the link between actin and cell activation.

The Wiskott-Aldrich syndrome protein (WASp) has emerged as a central player in the regulation of actin remodeling in T cells. The unique domain structure of WASp and other WASp family members enables these proteins to associate with a myriad of signaling effectors and to thereby regulate the coupling of T cell antigen receptor (TCR) engagement to both cytoskeletal rearrangement and transcriptional activation. This review focuses on these biochemical properties of WASp and also on the mechanisms whereby WASp interactions with its cognate ligands influence T cell activation. Because of its capacity to shift intracellular location and thereby dictate both the timing and the spatial distribution of actin polymerization following cell stimulation, WASp is well positioned to play major regulatory roles in directing a wide range of cellular processes and signaling pathways. Further dissection of the functional and biochemical properties of WASp therefore represents a promising avenue towards defining the molecular mechanisms that convey TCR stimulatory signals to the actin cytoskeleton and integrate cytoskeletal and other signaling systems so as to evoke a biological response.

Actins↗

PubMed2003

Efficient antigen presentation of soluble, but not particulate, antigen in the absence of Wiskott-Aldrich syndrome protein.

B cells and dendritic cells, lacking functional Wiskott-Aldrich syndrome protein (WASP), have aberrant formation of membrane protrusions. We hypothesized that protrusions may play a role in antigen presentation, and consequently, that impaired antigen presentation may be an underlying factor of the immune deficiency in patients with Wiskott-Aldrich syndrome. In this paper, we investigated the antigen presentation capacity of B cells and dendritic cells from WASP knockout mice, using soluble and particulate antigen, to CD4+ T cells from T-cell receptor transgenic DO11.10 mice. As antigen we used soluble ovalbumin (OVA), a peptide thereof (amino acids 323-339) or bacteria expressing OVA. We found that WASP-deficient B cells and dendritic cells efficiently processed and presented soluble OVA protein as well as its peptide in vitro, inducing proliferation and cytokine production from CD4+ T cells. Antigen presentation of soluble protein was efficient also in vivo, because immunization of WASP-deficient mice with OVA elicited proliferation of transferred, fluorescent-labelled, CD4+ T cells. Although we could detect uptake of bacteria in dendritic cells, processing and presentation of bacterial-expressed OVA was impaired in WASP-deficient dendritic cells. In conclusion, our data suggest that WASP is not needed for processing and presentation of soluble antigen, but that efficient presentation of particulate antigen require WASP.

Animals↗

PubMed2005

The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott-Aldrich syndrome protein.

The GTP/GDP nucleotide switch in Ras superfamily GTPases generally involves differential affinity toward downstream effectors, with the GTP-bound state having a higher affinity for effector than the GDP-bound state. We have developed a quantitative model of allosteric regulation of the Wiskott-Aldrich syndrome protein (WASP) by the Rho GTPase Cdc42 to better understand how GTPase binding is coupled to effector activation. The model accurately predicts WASP affinity for Cdc42, activity toward Arp2/3 complex, and activation by Cdc42 as functions of a two-state allosteric equilibrium in WASP. The ratio of GTPase affinities for the inactive and active states of WASP is appreciably larger for Cdc42-GTP than for Cdc42-GDP. The greater ability to distinguish between the two states of WASP makes Cdc42-GTP a full WASP agonist, whereas Cdc42-GDP is only a partial agonist. Thus, the nucleotide switch controls not only the affinity of Cdc42 for its effector but also the efficiency of coupling between the Cdc42-binding and allosteric equilibria in WASP. This effect can ensure high fidelity and specificity in Cdc42 signaling in crowded membrane environments.

Actin-Related Protein 2↗

PubMed1999

Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages.

Wiskott-Aldrich syndrome protein (WASp) is a hematopoietic-specific, multidomain protein whose mutation is responsible for the immunodeficiency disorder Wiskott-Aldrich syndrome. WASp contains a binding motif for the Rho GTPase CDC42Hs as well as verprolin/cofilin-like actin-regulatory domains, but no specific actin structure regulated by CDC42Hs-WASp has been identified. We found that WASp colocalizes with CDC42Hs and actin in the core of podosomes, a highly dynamic adhesion structure of human blood-derived macrophages. Microinjection of constitutively active V12CDC42Hs or a constitutively active WASp fragment consisting of the verprolin/cofilin-like domains led to the disassemly of podosomes. Conversely, macrophages from patients expressing truncated forms of WASp completely lacked podosomes. These findings indicate that WASp controls podosome assembly and, in cooperation with CDC42Hs, podosome disassembly in primary human macrophages.

Actins↗

PubMed1999

Wiskott-Aldrich syndrome protein induces actin clustering without direct binding to Cdc42.

WASP (Wiskott-Aldrich syndrome protein) was identified as the gene product whose mutation causes the human hereditary disease Wiskott-Aldrich syndrome. WASP contains many functional domains and has been shown to induce the formation of clusters of actin filaments in a manner dependent on Cdc42. However, there has been no report investigating what domain(s) is(are) important for the function. Here we present for the first time the results of detailed analyses on the domain-function relationship of WASP. First, the C-terminal verprolin-cofilin-acidic domain was shown to be essential for the regulation of actin cytoskeleton. In addition, we found that the clustering of WASP itself is distinct from actin clustering. The partial protein containing the region from the N-terminal pleckstrin homology domain to the basic residue-rich region also clustered especially around the nucleus as wild type WASP without inducing actin clustering. Finally, we obtained the quite unexpected result that a WASP mutant deficient in binding to Cdc42 still induced actin cluster formation, indicating that direct interaction between Cdc42 and WASP is not required for the regulation of actin cytoskeleton. This result may explain why no Wiskott-Aldrich syndrome patients have been identified with a missense mutation in the Cdc42-binding site.

Actin Depolymerizing Factors↗

PubMed2000

Activation of the Arp2/3 complex by the Listeria acta protein. Acta binds two actin monomers and three subunits of the Arp2/3 complex.

ActA is a bacterially encoded protein that enables Listeria monocytogenes to hijack the host cell actin cytoskeleton. It promotes Arp2/3-dependent actin nucleation, but its interactions with cellular components of the nucleation machinery are not well understood. Here we show that two domains of ActA (residues 85-104 and 121-138) with sequence similarity to WASP homology 2 domains bind two actin monomers with submicromolar affinity. ActA binds Arp2/3 with a K(d) of 0.6 microm and competes for binding with the WASP family proteins N-WASP and Scar1. By chemical cross-linking, ActA, N-WASP, and Scar1 contact the same three subunits of the Arp2/3 complex, p40, Arp2, and Arp3. Interestingly, profilin competes with ActA for binding of Arp2/3, but actophorin (cofilin) does not. The minimal Arp2/3-binding site of ActA (residues 144-170) is C-terminal to both actin-binding sites and shares sequence homology with Arp2/3-binding regions of WASP family proteins. The maximal activity at saturating concentrations of ActA is identical to the most active domains of the WASP family proteins. We propose that ActA and endogenous WASP family proteins promote Arp2/3-dependent nucleation by similar mechanisms and require simultaneous binding of Arp2 and Arp3.

Actin-Related Protein 2↗

PubMed2006

Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that induces plasma membrane invagination.

Actin reorganization is important for regulation of neuronal morphology. Neural Wiskott-Aldrich syndrome protein (N-WASP) is an important regulator of actin polymerization and also known to be strongly expressed in brain. Recently, Toca-1 (transducer of Cdc42-dependent actin assembly) has been shown to be required for Cdc42 to activate N-WASP from biochemical experiments. Toca-1 has three functional domains: an F-BAR/EFC domain at the N terminus, an HR1 at the center, and an SH3 domain at the C terminus. The F-BAR/EFC domain induces tubular invagination of plasma membrane, while Toca-1 binds both N-WASP and Cdc42 through the SH3 domain and the HR1, respectively. However, the physiological role of Toca-1 is completely unknown. Here we have investigated the neural function of Toca-1. Toca-1 is strongly expressed in neurons including hippocampal neurons in developing brain at early times. Knockdown of Toca-1 in PC12 cells significantly enhances neurite elongation. Consistently, overexpression of Toca-1 suppresses neurite elongation through the F-BAR/EFC domain with a membrane invaginating property, suggesting an implication of membrane trafficking in the neural function of Toca-1. In addition, knockdown of N-WASP, to our surprise, also enhances neurite elongation in PC12 cells, which is in clear contrast to the previous report that dominant negative mutants of N-WASP suppress neurite extension in PC12 cells. On the other hand, knockdown of Toca-1 in cultured rat hippocampal neurons enhances axon branching a little but not axon elongation, while knockdown of N-WASP enhances both axon elongation and branching. These results suggest that a vesicle trafficking regulator Toca-1 regulates different aspects of neuronal morphology from N-WASP.

Adaptor Proteins, Vesicular Transport↗

PubMed2000

Rho family GTPase Cdc42 is essential for the actin-based motility of Shigella in mammalian cells.

Shigella, the causative agent of bacillary dysentery, is capable of directing its movement within host cells by exploiting actin dynamics. The VirG protein expressed at one pole of the bacterium can recruit neural Wiskott-Aldrich syndrome protein (N-WASP), a downstream effector of Cdc42. Here, we show that Cdc42 is required for the actin-based motility of Shigella. Microinjection of a dominant active mutant Cdc42, but not Rac1 or RhoA, into Swiss 3T3 cells accelerated Shigella motility. In add-back experiments in Xenopus egg extracts, addition of a guanine nucleotide dissociation inhibitor for the Rho family, RhoGDI, greatly diminished the bacterial motility or actin assembly, which was restored by adding activated Cdc42. In N-WASP-depleted extracts, the bacterial movement almost arrested was restored by adding exogenous N-WASP but not H208D, an N-WASP mutant defective in binding to Cdc42. In pyrene actin assay, Cdc42 enhanced VirG-stimulating actin polymerization by N-WASP-actin-related protein (Arp)2/3 complex. Actually, Cdc42 stimulated actin cloud formation on the surface of bacteria expressing VirG in a solution containing N-WASP, Arp2/3 complex, and G-actin. Immunohistological study of Shigella-infected cells expressing green fluorescent protein-tagged Cdc42 revealed that Cdc42 accumulated by being colocalized with actin cloud at one pole of intracellular bacterium. Furthermore, overexpression of H208D mutant in cells interfered with the actin assembly of infected Shigella and diminished the intra- and intercellular spreading. These results suggest that Cdc42 activity is involved in initiating actin nucleation mediated by VirG-N-WASP-Arp2/3 complex formed on intracellular Shigella.

3T3 Cells↗

PubMed1998

Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri.

Shigella, the causative agent of bacillary dysentery, is capable of directing its own movement in the cytoplasm of infected epithelial cells. The bacterial surface protein VirG recruits host components mediating actin polymerization, which is thought to serve as the propulsive force. Here, we show that neural Wiskott-Aldrich syndrome protein (N-WASP), which is a critical target for filopodium formation downstream of Cdc42, is required for assembly of the actin tail generated by intracellular S.flexneri. N-WASP accumulates at the front of the actin tail and is capable of interacting with VirG in vitro and in vivo, a phenomenon that is not observed in intracellular Listeria monocytogenes. The verprolin-homology region in N-WASP was required for binding to the glycine-rich repeats domain of VirG, an essential domain for recruitment of F-actin on intracellular S.flexneri. Overexpression of a dominant-negative N-WASP mutant greatly inhibited formation of the actin tail by intracellular S.flexneri. Furthermore, depletion of N-WASP from Xenopus egg extracts shut off Shigella actin tail assembly, and this was restored upon addition of N-WASP protein, suggesting that N-WASP is a critical host factor for the assembly of the actin tail by intracellular Shigella.

Actins↗

PubMed2003

Impaired signaling via the high-affinity IgE receptor in Wiskott-Aldrich syndrome protein-deficient mast cells.

Wiskott-Aldrich syndrome protein (WASP) is the product of the gene deficient in boys with X-linked Wiskott-Aldrich syndrome. We assessed the role of WASP in signaling through the high-affinity IgE receptor (FcepsilonRI) using WASP-deficient mice. IgE-dependent degranulation and cytokine secretion were markedly diminished in bone marrow-derived mast cells from WASP-deficient mice. Upstream signaling events that include FcepsilonRI-triggered total protein tyrosine phosphorylation, and protein tyrosine phosphorylation of FcepsilonRIbeta and Syk were not affected by WASP deficiency. However, tyrosine phosphorylation of phospholipase Cgamma and Ca(2+) mobilization were diminished. IgE-dependent activation of c-Jun N-terminal kinase, cell spreading and redistribution of cellular F-actin in mast cells were reduced in the absence of WASP. We conclude that WASP regulates FcepsilonRI-mediated granule exocytosis, cytokine production and cytoskeletal changes in mast cells.

Actins↗