Publications by category
Journal articles
Worth AJJ, Metelo J, Bouma G, Moulding D, Fritzsche M, Vernay B, Charras G, Cory GOC, Thrasher AJ, Burns SO, et al (2013). Disease-associated missense mutations in the EVH1 domain disrupt intrinsic WASp function causing dysregulated actin dynamics and impaired dendritic cell migration.
Blood,
121(1), 72-84.
Abstract:
Disease-associated missense mutations in the EVH1 domain disrupt intrinsic WASp function causing dysregulated actin dynamics and impaired dendritic cell migration
Wiskott Aldrich syndrome (WAS), an X-linked immunodeficiency, results from loss-of-function mutations in the human hematopoietic cytoskeletal regulator gene WAS. Many missense mutations in the Ena Vasp homology1 (EVH1) domain preserve low-level WAS protein (WASp) expression and confer a milder clinical phenotype. Although disrupted binding to WASp-interacting protein (WIP) leads to enhanced WASp degradation in vivo, the intrinsic function of EVH1-mutated WASp is poorly understood. In the present study, we show that, despite mediating enhanced actin polymerization compared with wild-type WASp in vitro, EVH1 missense mutated proteins did not support full biologic function in cells, even when levels were restored by forced overexpression. Podosome assembly was aberrant and associated with dysregulated lamellipodia formation and impaired persistence of migration. At sites of residual podosome-associated actin polymerization, localization of EVH1-mutated proteins was preserved even after deletion of the entire domain, implying that WIP-WASp complex formation is not absolutely required for WASp localization. However, retention of mutant proteins in podosomes was significantly impaired and associated with reduced levels of WASp tyrosine phosphorylation. Our results indicate that the EVH1 domain is important not only for WASp stability, but also for intrinsic biologic activity in vivo. © 2013 by the American Society of Hematology.
Abstract.
Macpherson L, Monypenny J, Blundell MP, Cory GO, Tomé-García J, Thrasher AJ, Jones GE, Calle Y (2012). Tyrosine phosphorylation of WASP promotes calpain-mediated podosome disassembly.
Haematologica,
97(5), 687-691.
Abstract:
Tyrosine phosphorylation of WASP promotes calpain-mediated podosome disassembly.
Podosomes are actin-based adhesions involved in migration of cells that have to cross tissue boundaries such as myeloid cells. The Wiskott Aldrich Syndrome Protein regulates de novo actin polymerization during podosome formation and it is cleaved by the protease calpain during podosome disassembly. The mechanisms that may induce the Wiskott Aldrich Syndrome Protein cleavage by calpain remain undetermined. We now report that in myeloid cells, tyrosine phosphorylation of the Wiskott Aldrich Syndrome Protein-tyrosine291 (Human)/tyrosine293 (mouse) not only enhances Wiskott Aldrich Syndrome Protein-mediated actin polymerization but also promotes its calpain-dependent degradation during podosome disassembly. We also show that activation of the Wiskott Aldrich Syndrome Protein leading to podosome formation occurs independently of tyrosine phosphorylation in spleen-derived dendritic cells. We conclude that tyrosine phosphorylation of the Wiskott Aldrich Syndrome Protein integrates dynamics of actin and cell adhesion proteins during podosome disassembly required for mobilization of myeloid cells during the immune response.
Abstract.
Author URL.
Cory G (2011). Scratch-wound assay.
Methods Mol Biol,
769, 25-30.
Abstract:
Scratch-wound assay.
The scratch-wound assay is a simple, reproducible assay commonly used to measure basic cell migration parameters such as speed, persistence, and polarity. Cells are grown to confluence and a thin "wound" introduced by scratching with a pipette tip. Cells at the wound edge polarise and migrate into the wound space. Advantages of this assay are that it does not require the use of specific chemoattractants or gradient chambers and it generates a strong directional migratory response, even in cell types that do not show robust responses in "single cell" migration assays. It is most reliably analysed when performed using time-lapse imaging, which can also yield valuable cell morphology/protein localisation information.
Abstract.
Author URL.
Blundell MP, Bouma G, Metelo J, Worth A, Calle Y, Cowell LA, Westerberg LS, Moulding DA, Mirando S, Kinnon C, et al (2009). Phosphorylation of WASp is a key regulator of activity and stability in vivo.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,
106(37), 15738-15743.
Author URL.
Pocha SM, Cory GO (2009). WAVE2 is regulated by multiple phosphorylation events within its VCA domain.
Cell Motility and the Cytoskeleton,
66(1), 36-47.
Abstract:
WAVE2 is regulated by multiple phosphorylation events within its VCA domain
The (Wiskott-Aldrich Syndrome Protein)-family verprolin homologous protein (WAVE) family of proteins occupies a pivotal position in the cell, converting extracellular signals into the formation of branched filamentous (F) actin structures. WAVE proteins contain a verprolin central acidic (VCA) domain at their C-terminus, responsible for binding to and activating the Arp2/3 complex, which in-turn nucleates the formation of new actin filaments. Here we identify five Casein Kinase 2 (CK2) phosphorylation sites within the VCA domain of WAVE2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the Arp2/3 complex. Phosphorylation of ser 482 and 484 specifically inhibits the activation of the Arp2/3 complex by the WAVE2 VCA domain, but has no effect on the affinity for the Arp2/3 complex when the other phosphorylation sites are occupied. We demonstrate phosphorylation of all five sites on endogenous WAVE2 and show that their mutation to non-phosphorylatable alanine residues inhibits WAVE2 function in vivo, inhibiting cell ruffling and disrupting the integrity of the leading edge of migrating cells. © 2008 Wiley-Liss, Inc.
Abstract.
Full text.
Worth AJJ, Cory GOC, Thrasher AJ, Burns S (2008). Molecular pathogenesis of Wiskott-Aldrich syndrome mutations: insights into the mechanisms of endritic cell migration.
CLINICAL AND EXPERIMENTAL IMMUNOLOGY,
154, 71-72.
Author URL.
Cory G, Cullen PJ (2007). Membrane curvature: the power of bananas, zeppelins and boomerangs. Current Biology, 17(12), 455-457.
Danson CM, Pocha SM, Bloomberg GB, Cory GO (2007). Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity.
Journal of Cell Science,
120(23), 4144-4154.
Abstract:
Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity
The WAVE family of proteins has long been implicated in the stimulus-dependent generation of lamellipodia at the leading edge of migrating cells, with WAVE2 in particular implicated in the formation of peripheral ruffles and chemotactic migration. However, the lack of direct visualisation of cell migration in WAVE2 mutants or knockdowns has made defining the mechanisms of WAVE2 regulation during cell migration difficult. We have characterised three MAP kinase phosphorylation sites within WAVE2 and analysed fibroblast behaviour in a scratch-wound model following introduction of transgenes encoding phospho-defective WAVE2. The cells exhibited an increase in migration speed, a decrease in the persistence of migration, and disruption of polarisation of the Golgi apparatus. All these effects could be mimicked by acute knockdown of endogenous WAVE2 expression with RNAi, indicating that phosphorylation of WAVE2 by MAP kinases regulates cell polarity during migration.
Abstract.
Moulding DA, Blundell MP, Spiller DG, White MRH, Cory GO, Calle Y, Kempski H, Sinclair J, Ancliff PJ, Kinnon C, et al (2007). Unregulated actin polymerization by WASp causes defects of mitosis and cytokinesis in X-linked neutropenia.
Journal of Experimental Medicine,
204(9), 2213-2224.
Abstract:
Unregulated actin polymerization by WASp causes defects of mitosis and cytokinesis in X-linked neutropenia
Specific mutations in the human gene encoding the Wiskott-Aldrich syndrome protein (WASp) that compromise normal auto-inhibition of WASp result in unregulated activation of the actin-related protein 2/3 complex and increased actin polymerizing activity. These activating mutations are associated with an X-linked form of neutropenia with an intrinsic failure of myelopoiesis and an increase in the incidence of cytogenetic abnormalities. To study the underlying mechanisms, active mutant WASpI294T was expressed by gene transfer. This caused enhanced and delocalized actin polymerization throughout the cell, decreased proliferation, and increased apoptosis. Cells became binucleated, suggesting a failure of cytokinesis, and micronuclei were formed, indicative of genomic instability. Live cell imaging demonstrated a delay in mitosis from prometaphase to anaphase and confirmed that multinucleation was a result of aborted cytokinesis. During mitosis, filamentous actin was abnormally localized around the spindle and chromosomes throughout their alignment and separation, and it accumulated within the cleavage furrow around the spindle midzone. These findings reveal a novel mechanism for inhibition of myelopoiesis through defective mitosis and cytokinesis due to hyperactivation and mislocalization of actin polymerization. JEM © the Rockefeller University Press.
Abstract.
Ancliff PJ, Blundell MP, Cory GO, Calle Y, Worth A, Kempski H, Burns S, Jones GE, Sinclair J, Kinnon C, et al (2006). Two novel activating mutations in the Wiskott-Aldrich syndrome protein result in congenital neutropenia.
BLOOD,
108(7), 2182-2189.
Author URL.
Burns S, Cory GO, Vainchenker W, Thrasher AJ (2004). Mechanisms of WASp-mediated hematologic and immunologic disease.
BLOOD,
104(12), 3454-3462.
Author URL.
Cory GO, Cramer R, Blanchoin L, Ridley AJ (2003). Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol Cell, 11(5), 1229-1239.
Cory GOC, Ridley AJ (2002). Cell motility: braking WAVEs.
Nature,
418(6899), 732-733.
Author URL.
Cory GOC, Garg R, Cramer R, Ridley AJ (2002). Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.
J Biol Chem,
277(47), 45115-45121.
Abstract:
Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.
Wiskott-Aldrich Syndrome protein (WASp) is a key regulator of the Arp2/3 complex and the actin cytoskeleton in hematopoietic cells. WASp is capable of forming an auto-inhibited conformation, which can be disrupted by binding of Cdc42 and phosphatidylinositol 4,5-bisphosphate, leading to its activation. Stimulation of the collagen receptor on platelets and crosslinking the B-cell receptor induce tyrosine phosphorylation of WASp. Here we show that the Src family kinase Hck induces phosphorylation of WASp-Tyr(291) independently of Cdc42 and that this causes a shift in the mobility of WASp upon SDS-PAGE. A phospho-mimicking mutant, WASp-Y291E, exhibited an enhanced ability to stimulate actin polymerization in a cell-free system and when microinjected into primary macrophages induced extensive filopodium formation with greater efficiency than wild-type WASp or a Y291F mutant. We propose that phosphorylation of Tyr(291) directly regulates WASp function.
Abstract.
Author URL.
Morrogh LM, Hinshelwood S, Costello P, Cory G, Kinnon C (1999). The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when auto-phosphorylated in vitro. Eur J Immunol, 29(7), 2269-2279.
Kinnon C, Cory GO, MacCarthy-Morrogh L, Banin S, Gout I, Lovering RC, Brickell PM (1997). The identification of Bruton's tyrosine kinase and Wiskott-Aldrich syndrome protein associated proteins and signalling pathways.
Biochem Soc Trans,
25(2), 648-650.
Author URL.
Cory G, MacCarthy-Morrogh L, Banin S, Gout I, Brickell PM, Levinsky RJ, Kinnon C, Lovering RC (1996). Evidence that the Wiskott-Aldrich syndrome protein may be involved in lymphoid cel signalling pathways. J Immunol, 157(9), 3791-3795.
Cory G, Lovering RC, Hinshelwood S, MacCarthy-Morrogh L, Levinsky RJ, Kinnon C (1995). The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase. J Exp Med, 182(2), 611-615.
Conferences
Macpherson L, Monypenny J, Blundell MP, Cory GO, Tome-Garcia J, Thrasher A, Jones GE, Calle Y (2010). Tyrosine Phosphorylation of WASP Promotes Calpain-Mediated Podosome Disassembly in Myeloid Cells.
Author URL.
Publications by year
2013
Worth AJJ, Metelo J, Bouma G, Moulding D, Fritzsche M, Vernay B, Charras G, Cory GOC, Thrasher AJ, Burns SO, et al (2013). Disease-associated missense mutations in the EVH1 domain disrupt intrinsic WASp function causing dysregulated actin dynamics and impaired dendritic cell migration.
Blood,
121(1), 72-84.
Abstract:
Disease-associated missense mutations in the EVH1 domain disrupt intrinsic WASp function causing dysregulated actin dynamics and impaired dendritic cell migration
Wiskott Aldrich syndrome (WAS), an X-linked immunodeficiency, results from loss-of-function mutations in the human hematopoietic cytoskeletal regulator gene WAS. Many missense mutations in the Ena Vasp homology1 (EVH1) domain preserve low-level WAS protein (WASp) expression and confer a milder clinical phenotype. Although disrupted binding to WASp-interacting protein (WIP) leads to enhanced WASp degradation in vivo, the intrinsic function of EVH1-mutated WASp is poorly understood. In the present study, we show that, despite mediating enhanced actin polymerization compared with wild-type WASp in vitro, EVH1 missense mutated proteins did not support full biologic function in cells, even when levels were restored by forced overexpression. Podosome assembly was aberrant and associated with dysregulated lamellipodia formation and impaired persistence of migration. At sites of residual podosome-associated actin polymerization, localization of EVH1-mutated proteins was preserved even after deletion of the entire domain, implying that WIP-WASp complex formation is not absolutely required for WASp localization. However, retention of mutant proteins in podosomes was significantly impaired and associated with reduced levels of WASp tyrosine phosphorylation. Our results indicate that the EVH1 domain is important not only for WASp stability, but also for intrinsic biologic activity in vivo. © 2013 by the American Society of Hematology.
Abstract.
2012
Macpherson L, Monypenny J, Blundell MP, Cory GO, Tomé-García J, Thrasher AJ, Jones GE, Calle Y (2012). Tyrosine phosphorylation of WASP promotes calpain-mediated podosome disassembly.
Haematologica,
97(5), 687-691.
Abstract:
Tyrosine phosphorylation of WASP promotes calpain-mediated podosome disassembly.
Podosomes are actin-based adhesions involved in migration of cells that have to cross tissue boundaries such as myeloid cells. The Wiskott Aldrich Syndrome Protein regulates de novo actin polymerization during podosome formation and it is cleaved by the protease calpain during podosome disassembly. The mechanisms that may induce the Wiskott Aldrich Syndrome Protein cleavage by calpain remain undetermined. We now report that in myeloid cells, tyrosine phosphorylation of the Wiskott Aldrich Syndrome Protein-tyrosine291 (Human)/tyrosine293 (mouse) not only enhances Wiskott Aldrich Syndrome Protein-mediated actin polymerization but also promotes its calpain-dependent degradation during podosome disassembly. We also show that activation of the Wiskott Aldrich Syndrome Protein leading to podosome formation occurs independently of tyrosine phosphorylation in spleen-derived dendritic cells. We conclude that tyrosine phosphorylation of the Wiskott Aldrich Syndrome Protein integrates dynamics of actin and cell adhesion proteins during podosome disassembly required for mobilization of myeloid cells during the immune response.
Abstract.
Author URL.
2011
Cory G (2011). Scratch-wound assay.
Methods Mol Biol,
769, 25-30.
Abstract:
Scratch-wound assay.
The scratch-wound assay is a simple, reproducible assay commonly used to measure basic cell migration parameters such as speed, persistence, and polarity. Cells are grown to confluence and a thin "wound" introduced by scratching with a pipette tip. Cells at the wound edge polarise and migrate into the wound space. Advantages of this assay are that it does not require the use of specific chemoattractants or gradient chambers and it generates a strong directional migratory response, even in cell types that do not show robust responses in "single cell" migration assays. It is most reliably analysed when performed using time-lapse imaging, which can also yield valuable cell morphology/protein localisation information.
Abstract.
Author URL.
2010
Macpherson L, Monypenny J, Blundell MP, Cory GO, Tome-Garcia J, Thrasher A, Jones GE, Calle Y (2010). Tyrosine Phosphorylation of WASP Promotes Calpain-Mediated Podosome Disassembly in Myeloid Cells.
Author URL.
2009
Blundell MP, Bouma G, Metelo J, Worth A, Calle Y, Cowell LA, Westerberg LS, Moulding DA, Mirando S, Kinnon C, et al (2009). Phosphorylation of WASp is a key regulator of activity and stability in vivo.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,
106(37), 15738-15743.
Author URL.
Pocha SM, Cory GO (2009). WAVE2 is regulated by multiple phosphorylation events within its VCA domain.
Cell Motility and the Cytoskeleton,
66(1), 36-47.
Abstract:
WAVE2 is regulated by multiple phosphorylation events within its VCA domain
The (Wiskott-Aldrich Syndrome Protein)-family verprolin homologous protein (WAVE) family of proteins occupies a pivotal position in the cell, converting extracellular signals into the formation of branched filamentous (F) actin structures. WAVE proteins contain a verprolin central acidic (VCA) domain at their C-terminus, responsible for binding to and activating the Arp2/3 complex, which in-turn nucleates the formation of new actin filaments. Here we identify five Casein Kinase 2 (CK2) phosphorylation sites within the VCA domain of WAVE2, serines 482, 484, 488, 489, and 497. Phosphorylation of these sites is required for a high affinity interaction with the Arp2/3 complex. Phosphorylation of ser 482 and 484 specifically inhibits the activation of the Arp2/3 complex by the WAVE2 VCA domain, but has no effect on the affinity for the Arp2/3 complex when the other phosphorylation sites are occupied. We demonstrate phosphorylation of all five sites on endogenous WAVE2 and show that their mutation to non-phosphorylatable alanine residues inhibits WAVE2 function in vivo, inhibiting cell ruffling and disrupting the integrity of the leading edge of migrating cells. © 2008 Wiley-Liss, Inc.
Abstract.
Full text.
2008
Worth AJJ, Cory GOC, Thrasher AJ, Burns S (2008). Molecular pathogenesis of Wiskott-Aldrich syndrome mutations: insights into the mechanisms of endritic cell migration.
CLINICAL AND EXPERIMENTAL IMMUNOLOGY,
154, 71-72.
Author URL.
2007
Cory G, Cullen PJ (2007). Membrane curvature: the power of bananas, zeppelins and boomerangs. Current Biology, 17(12), 455-457.
Danson CM, Pocha SM, Bloomberg GB, Cory GO (2007). Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity.
Journal of Cell Science,
120(23), 4144-4154.
Abstract:
Phosphorylation of WAVE2 by MAP kinases regulates persistent cell migration and polarity
The WAVE family of proteins has long been implicated in the stimulus-dependent generation of lamellipodia at the leading edge of migrating cells, with WAVE2 in particular implicated in the formation of peripheral ruffles and chemotactic migration. However, the lack of direct visualisation of cell migration in WAVE2 mutants or knockdowns has made defining the mechanisms of WAVE2 regulation during cell migration difficult. We have characterised three MAP kinase phosphorylation sites within WAVE2 and analysed fibroblast behaviour in a scratch-wound model following introduction of transgenes encoding phospho-defective WAVE2. The cells exhibited an increase in migration speed, a decrease in the persistence of migration, and disruption of polarisation of the Golgi apparatus. All these effects could be mimicked by acute knockdown of endogenous WAVE2 expression with RNAi, indicating that phosphorylation of WAVE2 by MAP kinases regulates cell polarity during migration.
Abstract.
Moulding DA, Blundell MP, Spiller DG, White MRH, Cory GO, Calle Y, Kempski H, Sinclair J, Ancliff PJ, Kinnon C, et al (2007). Unregulated actin polymerization by WASp causes defects of mitosis and cytokinesis in X-linked neutropenia.
Journal of Experimental Medicine,
204(9), 2213-2224.
Abstract:
Unregulated actin polymerization by WASp causes defects of mitosis and cytokinesis in X-linked neutropenia
Specific mutations in the human gene encoding the Wiskott-Aldrich syndrome protein (WASp) that compromise normal auto-inhibition of WASp result in unregulated activation of the actin-related protein 2/3 complex and increased actin polymerizing activity. These activating mutations are associated with an X-linked form of neutropenia with an intrinsic failure of myelopoiesis and an increase in the incidence of cytogenetic abnormalities. To study the underlying mechanisms, active mutant WASpI294T was expressed by gene transfer. This caused enhanced and delocalized actin polymerization throughout the cell, decreased proliferation, and increased apoptosis. Cells became binucleated, suggesting a failure of cytokinesis, and micronuclei were formed, indicative of genomic instability. Live cell imaging demonstrated a delay in mitosis from prometaphase to anaphase and confirmed that multinucleation was a result of aborted cytokinesis. During mitosis, filamentous actin was abnormally localized around the spindle and chromosomes throughout their alignment and separation, and it accumulated within the cleavage furrow around the spindle midzone. These findings reveal a novel mechanism for inhibition of myelopoiesis through defective mitosis and cytokinesis due to hyperactivation and mislocalization of actin polymerization. JEM © the Rockefeller University Press.
Abstract.
2006
Ancliff PJ, Blundell MP, Cory GO, Calle Y, Worth A, Kempski H, Burns S, Jones GE, Sinclair J, Kinnon C, et al (2006). Two novel activating mutations in the Wiskott-Aldrich syndrome protein result in congenital neutropenia.
BLOOD,
108(7), 2182-2189.
Author URL.
2004
Burns S, Cory GO, Vainchenker W, Thrasher AJ (2004). Mechanisms of WASp-mediated hematologic and immunologic disease.
BLOOD,
104(12), 3454-3462.
Author URL.
2003
Cory GO, Cramer R, Blanchoin L, Ridley AJ (2003). Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol Cell, 11(5), 1229-1239.
2002
Cory GOC, Ridley AJ (2002). Cell motility: braking WAVEs.
Nature,
418(6899), 732-733.
Author URL.
Cory GOC, Garg R, Cramer R, Ridley AJ (2002). Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.
J Biol Chem,
277(47), 45115-45121.
Abstract:
Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome protein.
Wiskott-Aldrich Syndrome protein (WASp) is a key regulator of the Arp2/3 complex and the actin cytoskeleton in hematopoietic cells. WASp is capable of forming an auto-inhibited conformation, which can be disrupted by binding of Cdc42 and phosphatidylinositol 4,5-bisphosphate, leading to its activation. Stimulation of the collagen receptor on platelets and crosslinking the B-cell receptor induce tyrosine phosphorylation of WASp. Here we show that the Src family kinase Hck induces phosphorylation of WASp-Tyr(291) independently of Cdc42 and that this causes a shift in the mobility of WASp upon SDS-PAGE. A phospho-mimicking mutant, WASp-Y291E, exhibited an enhanced ability to stimulate actin polymerization in a cell-free system and when microinjected into primary macrophages induced extensive filopodium formation with greater efficiency than wild-type WASp or a Y291F mutant. We propose that phosphorylation of Tyr(291) directly regulates WASp function.
Abstract.
Author URL.
1999
Morrogh LM, Hinshelwood S, Costello P, Cory G, Kinnon C (1999). The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when auto-phosphorylated in vitro. Eur J Immunol, 29(7), 2269-2279.
1997
Kinnon C, Cory GO, MacCarthy-Morrogh L, Banin S, Gout I, Lovering RC, Brickell PM (1997). The identification of Bruton's tyrosine kinase and Wiskott-Aldrich syndrome protein associated proteins and signalling pathways.
Biochem Soc Trans,
25(2), 648-650.
Author URL.
1996
Cory G, MacCarthy-Morrogh L, Banin S, Gout I, Brickell PM, Levinsky RJ, Kinnon C, Lovering RC (1996). Evidence that the Wiskott-Aldrich syndrome protein may be involved in lymphoid cel signalling pathways. J Immunol, 157(9), 3791-3795.
1995
Cory G, Lovering RC, Hinshelwood S, MacCarthy-Morrogh L, Levinsky RJ, Kinnon C (1995). The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase. J Exp Med, 182(2), 611-615.
