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Keywords {🔍}

socs, jak, pubmed, kinase, article, domain, loop, activation, google, scholar, cas, complex, binding, fig, data, kir, structure, central, receptor, inhibitor, bind, shown, inhibition, protein, peptide, human, interaction, nature, motif, affinity, bound, presence, residues, cytokine, tyrosine, site, region, buffer, family, proteins, cytokines, cullin, box, activity, signaling, analysis, substrate, inhibitory, performed, residue,

Topics {✒️}

nature portfolio privacy policy medical research council medical research advertising x-ray crystallography social media x-ray crystal structures solutions reprints nature 387 nature 372 nature 547 nature socs1/elonginb/elonginc ternary complex development reducing sds-page gel socs2/elonginb/elonginc/cullin5 ntd candidate enhancer-activating snps 15n-noesy-hsqc spectra ternary jak2/socs1/peptide complex hanging-drop vapour diffusion references hilton socs/elongin bc complexes 1 mm phenyl-methylsulfonyl fluoride homogenous socs1/bc complexes comprehensive python-based system 1 ml gsh-agarose resin dysregulated cross-talk inhibition results socs1 discussion socs1 unusual n-terminal extension figures refers methods cloning expression socs2/elongin bc/cullin5 structures 13c/15n-labelled ggsocs1δsocsbox bind activation-loop-derived phosphopeptides large-scale structural differences vhl-elonginc-elonginb complex unstructured n-terminal region elonginbc-cullin5 ubiquitin ligase open mainchain-derived hydrogen bonds original author e2-ubiquitin docking site 1 μci 32p-γ-atp stat-induced stat inhibitor obtained synthetic peptides representing jab/socs1/ssi-1 e3 ubiquitin ligase

Questions {❓}

• If SOCS1 does not utilise receptor recruitment as part of its mechanism-of-action then how can it achieve specificity for some cytokines but not others?

Schema {🗺️}

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         headline:The molecular basis of JAK/STAT inhibition by SOCS1
         description:The SOCS family of proteins are negative-feedback inhibitors of signalling induced by cytokines that act via the JAK/STAT pathway. SOCS proteins can act as ubiquitin ligases by recruiting Cullin5 to ubiquitinate signalling components; however, SOCS1, the most potent member of the family, can also inhibit JAK directly. Here we determine the structural basis of both these modes of inhibition. Due to alterations within the SOCS box domain, SOCS1 has a compromised ability to recruit Cullin5; however, it is a direct, potent and selective inhibitor of JAK catalytic activity. The kinase inhibitory region of SOCS1 targets the substrate binding groove of JAK with high specificity and thereby blocks any subsequent phosphorylation. SOCS1 is a potent inhibitor of the interferon gamma (IFNγ) pathway, however, it does not bind the IFNγ receptor, making its mode-of-action distinct from SOCS3. These findings reveal the mechanism used by SOCS1 to inhibit signalling by inflammatory cytokines. 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.
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      headline:The molecular basis of JAK/STAT inhibition by SOCS1
      description:The SOCS family of proteins are negative-feedback inhibitors of signalling induced by cytokines that act via the JAK/STAT pathway. SOCS proteins can act as ubiquitin ligases by recruiting Cullin5 to ubiquitinate signalling components; however, SOCS1, the most potent member of the family, can also inhibit JAK directly. Here we determine the structural basis of both these modes of inhibition. Due to alterations within the SOCS box domain, SOCS1 has a compromised ability to recruit Cullin5; however, it is a direct, potent and selective inhibitor of JAK catalytic activity. The kinase inhibitory region of SOCS1 targets the substrate binding groove of JAK with high specificity and thereby blocks any subsequent phosphorylation. SOCS1 is a potent inhibitor of the interferon gamma (IFNγ) pathway, however, it does not bind the IFNγ receptor, making its mode-of-action distinct from SOCS3. These findings reveal the mechanism used by SOCS1 to inhibit signalling by inflammatory cytokines. 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.
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            type:Organization
            name:Royal Parade
            address:
               name:The University of Melbourne, Royal Parade, Parkville, Australia
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Jeffrey J. Babon
      url:http://orcid.org/0000-0002-5408-6239
      affiliation:
            name:1G Royal Parade
            address:
               name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
               type:PostalAddress
            type:Organization
            name:Royal Parade
            address:
               name:The University of Melbourne, Royal Parade, Parkville, Australia
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia
      name:Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Australia
      name:The University of Melbourne, Royal Parade, Parkville, Australia

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