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  1. AU="Jeffrey J Babon"
  2. AU="Rehana Masood"
  3. AU="Sandra Heskamp"
  4. AU="Omid Sadeghi"
  5. AU="Antaya, Richard"
  6. AU="Papadopoulos, G"
  7. AU="Boughen, Santiago"
  8. AU="Brink, P. L."

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  1. Artikel ; Online: The Role of LNK (SH2B3) in the Regulation of JAK-STAT Signalling in Haematopoiesis

    Rhiannon Morris / Liesl Butler / Andrew Perkins / Nadia J. Kershaw / Jeffrey J. Babon

    Pharmaceuticals, Vol 15, Iss 24, p

    2022  Band 24

    Abstract: LNK is a member of the SH2B family of adaptor proteins and is a non-redundant regulator of cytokine signalling. Cytokines are secreted intercellular messengers that bind to specific receptors on the surface of target cells to activate the Janus Kinase- ... ...

    Abstract LNK is a member of the SH2B family of adaptor proteins and is a non-redundant regulator of cytokine signalling. Cytokines are secreted intercellular messengers that bind to specific receptors on the surface of target cells to activate the Janus Kinase-Signal Transducer and Activator of Transcription (JAK-STAT) signalling pathway. Activation of the JAK-STAT pathway leads to proliferative and often inflammatory effects, and so the amplitude and duration of signalling are tightly controlled. LNK binds phosphotyrosine residues to signalling proteins downstream of cytokines and constrains JAK-STAT signalling. Mutations in LNK have been identified in a range of haematological and inflammatory diseases due to increased signalling following the loss of LNK function. Here, we review the regulation of JAK-STAT signalling via the adaptor protein LNK and discuss the role of LNK in haematological diseases.
    Schlagwörter SH2B3 ; JAK-STAT ; myeloproliferative neoplasms ; Medicine ; R ; Pharmacy and materia medica ; RS1-441
    Thema/Rubrik (Code) 570
    Sprache Englisch
    Erscheinungsdatum 2022-12-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  2. Artikel ; Online: Author Correction

    Edmond M. Linossi / Kunlun Li / Gianluca Veggiani / Cyrus Tan / Farhad Dehkhoda / Colin Hockings / Dale J. Calleja / Narelle Keating / Rebecca Feltham / Andrew J. Brooks / Shawn S. Li / Sachdev S. Sidhu / Jeffrey J. Babon / Nadia J. Kershaw / Sandra E. Nicholson

    Nature Communications, Vol 14, Iss 1, Pp 1-

    Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands

    2023  Band 2

    Schlagwörter Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2023-12-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  3. Artikel ; Online: Structural and functional analysis of target recognition by the lymphocyte adaptor protein LNK

    Rhiannon Morris / Yaoyuan Zhang / Julia I. Ellyard / Carola G. Vinuesa / James M. Murphy / Artem Laktyushin / Nadia J. Kershaw / Jeffrey J. Babon

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Band 9

    Abstract: LNK is a potent negative regulator of cytokine signaling implicated in blood cells proliferation. Here the authors present structures of the substrate recognition (SH2) domain of LNK in complex with phosphorylated motifs from JAK2 and EPOR; providing ... ...

    Abstract LNK is a potent negative regulator of cytokine signaling implicated in blood cells proliferation. Here the authors present structures of the substrate recognition (SH2) domain of LNK in complex with phosphorylated motifs from JAK2 and EPOR; providing insight into its binding specificity and mode of action.
    Schlagwörter Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2021-10-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  4. Artikel ; Online: Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands

    Edmond M. Linossi / Kunlun Li / Gianluca Veggiani / Cyrus Tan / Farhad Dehkhoda / Colin Hockings / Dale J. Calleja / Narelle Keating / Rebecca Feltham / Andrew J. Brooks / Shawn S. Li / Sachdev S. Sidhu / Jeffrey J. Babon / Nadia J. Kershaw / Sandra E. Nicholson

    Nature Communications, Vol 12, Iss 1, Pp 1-

    2021  Band 13

    Abstract: Abstract Suppressor of cytokine signaling (SOCS)2 protein is a key negative regulator of the growth hormone (GH) and Janus kinase (JAK)-Signal Transducers and Activators of Transcription (STAT) signaling cascade. The central SOCS2-Src homology 2 (SH2) ... ...

    Abstract Abstract Suppressor of cytokine signaling (SOCS)2 protein is a key negative regulator of the growth hormone (GH) and Janus kinase (JAK)-Signal Transducers and Activators of Transcription (STAT) signaling cascade. The central SOCS2-Src homology 2 (SH2) domain is characteristic of the SOCS family proteins and is an important module that facilitates recognition of targets bearing phosphorylated tyrosine (pTyr) residues. Here we identify an exosite on the SOCS2-SH2 domain which, when bound to a non-phosphorylated peptide (F3), enhances SH2 affinity for canonical phosphorylated ligands. Solution of the SOCS2/F3 crystal structure reveals F3 as an α-helix which binds on the opposite side of the SH2 domain to the phosphopeptide binding site. F3:exosite binding appears to stabilise the SOCS2-SH2 domain, resulting in slower dissociation of phosphorylated ligands and consequently, enhances binding affinity. This biophysical enhancement of SH2:pTyr binding affinity translates to increase SOCS2 inhibition of GH signaling.
    Schlagwörter Science ; Q
    Thema/Rubrik (Code) 572
    Sprache Englisch
    Erscheinungsdatum 2021-12-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  5. Artikel ; Online: The molecular basis of JAK/STAT inhibition by SOCS1

    Nicholas P. D. Liau / Artem Laktyushin / Isabelle S. Lucet / James M. Murphy / Shenggen Yao / Eden Whitlock / Kimberley Callaghan / Nicos A. Nicola / Nadia J. Kershaw / Jeffrey J. Babon

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Band 14

    Abstract: Cytokines are key molecules in controlling haematopoiesis that signal via the JAK/STAT pathway. Here the authors present the structures of SOCS1 bound to its JAK1 target as well as in complex with elonginB and elonginC, providing a molecular explanation ... ...

    Abstract Cytokines are key molecules in controlling haematopoiesis that signal via the JAK/STAT pathway. Here the authors present the structures of SOCS1 bound to its JAK1 target as well as in complex with elonginB and elonginC, providing a molecular explanation for the potent JAK- inhibitory activity of SOCS1.
    Schlagwörter Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2018-04-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  6. Artikel ; Online: The molecular basis of JAK/STAT inhibition by SOCS1

    Nicholas P. D. Liau / Artem Laktyushin / Isabelle S. Lucet / James M. Murphy / Shenggen Yao / Eden Whitlock / Kimberley Callaghan / Nicos A. Nicola / Nadia J. Kershaw / Jeffrey J. Babon

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Band 14

    Abstract: Cytokines are key molecules in controlling haematopoiesis that signal via the JAK/STAT pathway. Here the authors present the structures of SOCS1 bound to its JAK1 target as well as in complex with elonginB and elonginC, providing a molecular explanation ... ...

    Abstract Cytokines are key molecules in controlling haematopoiesis that signal via the JAK/STAT pathway. Here the authors present the structures of SOCS1 bound to its JAK1 target as well as in complex with elonginB and elonginC, providing a molecular explanation for the potent JAK- inhibitory activity of SOCS1.
    Schlagwörter Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2018-04-01T00:00:00Z
    Verlag Nature Publishing Group
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  7. Artikel: NMR studies of interactions between Bax and BH3 domain-containing peptides in the absence and presence of CHAPS

    Yao, Shenggen / Adeline Y. Robin / Dana Westphal / Geoff V. Thompson / Jeffrey J. Babon / Jerry M. Adams / Peter E. Czabotar / Peter M. Colman

    Archives of biochemistry and biophysics. 2014 Mar. 01, v. 545

    2014  

    Abstract: Activation and oligomerisation of Bax, a key pro-apoptotic Bcl-2 family protein, are key steps in the mitochondrial pathway to apoptosis. The signals for apoptosis are conveyed by the distantly related BH3-only proteins, which use their short BH3 domain, ...

    Abstract Activation and oligomerisation of Bax, a key pro-apoptotic Bcl-2 family protein, are key steps in the mitochondrial pathway to apoptosis. The signals for apoptosis are conveyed by the distantly related BH3-only proteins, which use their short BH3 domain, an amphipathic α-helix, to interact with other Bcl-2 family members. Here we report an NMR study of interactions between BaxΔC and BH3 domain-containing peptides in the absence and presence of CHAPS, a zwitterionic detergent. We find for the first time that CHAPS interacts weakly with BaxΔC (fast exchange on the NMR chemical shift timescale), at concentrations below micelle formation and with an estimated Kd in the tens of mM. Direct and relatively strong-interactions (slow exchange on the NMR chemical shift timescale) were also observed for BaxΔC with BaxBH3 (estimated Kd of circa 150μM) or BimBH3 in the absence of CHAPS. The interaction with either peptide alone induced widespread chemical shift perturbations to BaxΔC in solution which implies that BaxΔC might have undergone significant conformation change upon binding the BH3 peptide. However, BaxΔC remained monomeric upon binding either CHAPS or a BH3 peptide alone, but the presence of both provoked it to form a dimer.
    Schlagwörter apoptosis ; detergents ; micelles ; mitochondria ; nuclear magnetic resonance spectroscopy ; oligomerization ; peptides ; proteins ; surfactants ; zwitterions
    Sprache Englisch
    Erscheinungsverlauf 2014-0301
    Umfang p. 33-43.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2014.01.003
    Datenquelle NAL Katalog (AGRICOLA)

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  8. Artikel ; Online: Suppressor of cytokine signaling (SOCS)5 ameliorates influenza infection via inhibition of EGFR signaling

    Lukasz Kedzierski / Michelle D Tate / Alan C Hsu / Tatiana B Kolesnik / Edmond M Linossi / Laura Dagley / Zhaoguang Dong / Sarah Freeman / Giuseppe Infusini / Malcolm R Starkey / Nicola L Bird / Simon M Chatfield / Jeffrey J Babon / Nicholas Huntington / Gabrielle Belz / Andrew Webb / Peter AB Wark / Nicos A Nicola / Jianqing Xu /
    Katherine Kedzierska / Philip M Hansbro / Sandra E Nicholson

    eLife, Vol

    2017  Band 6

    Abstract: Influenza virus infections have a significant impact on global human health. Individuals with suppressed immunity, or suffering from chronic inflammatory conditions such as COPD, are particularly susceptible to influenza. Here we show that suppressor of ... ...

    Abstract Influenza virus infections have a significant impact on global human health. Individuals with suppressed immunity, or suffering from chronic inflammatory conditions such as COPD, are particularly susceptible to influenza. Here we show that suppressor of cytokine signaling (SOCS) five has a pivotal role in restricting influenza A virus in the airway epithelium, through the regulation of epidermal growth factor receptor (EGFR). Socs5-deficient mice exhibit heightened disease severity, with increased viral titres and weight loss. Socs5 levels were differentially regulated in response to distinct influenza viruses (H1N1, H3N2, H5N1 and H11N9) and were reduced in primary epithelial cells from COPD patients, again correlating with increased susceptibility to influenza. Importantly, restoration of SOCS5 levels restricted influenza virus infection, suggesting that manipulating SOCS5 expression and/or SOCS5 targets might be a novel therapeutic approach to influenza.
    Schlagwörter SOCS5 ; influenza ; EGFR ; COPD ; PI3K ; innate immunity ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Sprache Englisch
    Erscheinungsdatum 2017-02-01T00:00:00Z
    Verlag eLife Sciences Publications Ltd
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  9. Artikel ; Online: Suppressor of Cytokine Signaling (SOCS) 5 utilises distinct domains for regulation of JAK1 and interaction with the adaptor protein Shc-1.

    Edmond M Linossi / Indu R Chandrashekaran / Tatiana B Kolesnik / James M Murphy / Andrew I Webb / Tracy A Willson / Lukasz Kedzierski / Alex N Bullock / Jeffrey J Babon / Raymond S Norton / Nicos A Nicola / Sandra E Nicholson

    PLoS ONE, Vol 8, Iss 8, p e

    2013  Band 70536

    Abstract: Suppressor of Cytokine Signaling (SOCS)5 is thought to act as a tumour suppressor through negative regulation of JAK/STAT and epidermal growth factor (EGF) signaling. However, the mechanism/s by which SOCS5 acts on these two distinct pathways is unclear. ...

    Abstract Suppressor of Cytokine Signaling (SOCS)5 is thought to act as a tumour suppressor through negative regulation of JAK/STAT and epidermal growth factor (EGF) signaling. However, the mechanism/s by which SOCS5 acts on these two distinct pathways is unclear. We show for the first time that SOCS5 can interact directly with JAK via a unique, conserved region in its N-terminus, which we have termed the JAK interaction region (JIR). Co-expression of SOCS5 was able to specifically reduce JAK1 and JAK2 (but not JAK3 or TYK2) autophosphorylation and this function required both the conserved JIR and additional sequences within the long SOCS5 N-terminal region. We further demonstrate that SOCS5 can directly inhibit JAK1 kinase activity, although its mechanism of action appears distinct from that of SOCS1 and SOCS3. In addition, we identify phosphoTyr317 in Shc-1 as a high-affinity substrate for the SOCS5-SH2 domain and suggest that SOCS5 may negatively regulate EGF and growth factor-driven Shc-1 signaling by binding to this site. These findings suggest that different domains in SOCS5 contribute to two distinct mechanisms for regulation of cytokine and growth factor signaling.
    Schlagwörter Medicine ; R ; Science ; Q
    Thema/Rubrik (Code) 572
    Sprache Englisch
    Erscheinungsdatum 2013-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  10. Artikel ; Online: Attenuation of AMPK signaling by ROQUIN promotes T follicular helper cell formation

    Roybel R Ramiscal / Ian A Parish / Robert S Lee-Young / Jeffrey J Babon / Julianna Blagih / Alvin Pratama / Jaime Martin / Naomi Hawley / Jean Y Cappello / Pablo F Nieto / Julia I Ellyard / Nadia J Kershaw / Rebecca A Sweet / Christopher C Goodnow / Russell G Jones / Mark A Febbraio / Carola G Vinuesa / Vicki Athanasopoulos

    eLife, Vol

    2015  Band 4

    Abstract: T follicular helper cells (Tfh) are critical for the longevity and quality of antibody-mediated protection against infection. Yet few signaling pathways have been identified to be unique solely to Tfh development. ROQUIN is a post-transcriptional ... ...

    Abstract T follicular helper cells (Tfh) are critical for the longevity and quality of antibody-mediated protection against infection. Yet few signaling pathways have been identified to be unique solely to Tfh development. ROQUIN is a post-transcriptional repressor of T cells, acting through its ROQ domain to destabilize mRNA targets important for Th1, Th17, and Tfh biology. Here, we report that ROQUIN has a paradoxical function on Tfh differentiation mediated by its RING domain: mice with a T cell-specific deletion of the ROQUIN RING domain have unchanged Th1, Th2, Th17, and Tregs during a T-dependent response but show a profoundly defective antigen-specific Tfh compartment. ROQUIN RING signaling directly antagonized the catalytic α1 subunit of adenosine monophosphate-activated protein kinase (AMPK), a central stress-responsive regulator of cellular metabolism and mTOR signaling, which is known to facilitate T-dependent humoral immunity. We therefore unexpectedly uncover a ROQUIN–AMPK metabolic signaling nexus essential for selectively promoting Tfh responses.
    Schlagwörter T follicular helper cell ; germinal center ; stress granule ; ROQUIN ; AMPK ; mTOR ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Sprache Englisch
    Erscheinungsdatum 2015-10-01T00:00:00Z
    Verlag eLife Sciences Publications Ltd
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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