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14-3-3 proteins are...
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Henriksson, Maria L.Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)
(författare)
14-3-3 proteins are required for the inhibition fo Ras by exoenzyme S
- Artikel/kapitelEngelska2000
Förlag, utgivningsår, omfång ...
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2000-07-25
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Portland Press,2000
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LIBRIS-ID:oai:DiVA.org:umu-2456
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-2456URI
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https://doi.org/10.1042/bj3490697DOI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:art swepub-publicationtype
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14-3-3 proteins play a regulatory role and participate in both signal transduction and checkpoint control pathways. 14-3-3 proteins bind phosphoserine ligands, such as Raf-l kinase and Bad, by recognizing the phosphorylated consensus motif, Arg-Ser-Xaa-pSer-Xaa-Pro (where 'Xaa' represents 'any residue', and 'pSer' is 'phosphoserine'). However, 14-3-3 proteins must bind unphosphorylated ligands, such as glycoprotein Ib alpha and Pseudomonas aeruginosa exoenzyme S (ExoS), since it has been suggested that specific residues of 14-3-3 proteins are required for activation of ExoS. Furthermore, an unphosphorylated peptide derived from a phage display library inhibited the binding of both ExoS and Raf-1 to 14-3-3, and bound within the same conserved amphipathic groove on the surface of 14-3-3 as the Raf-derived phosphopeptide (pS-Raf-259). In the present study we identify the interaction site on ExoS for 14-3-3, and show that ExoS and 14-3-3 do indeed interact in vivo. In addition, we show that this interaction is critical for the ADP-ribosylation of Ras by ExoS, both in vitro and in vivo. Loss of the 14-3-3 binding site on ExoS results in an ExoS molecule that is unable to efficiently inactivate Ras, and displays reduced killing activity.
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Trollér, UlrikaUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)
(författare)
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Hallberg, BengtUmeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)beha0004
(författare)
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Umeå universitetInstitutionen för molekylärbiologi (Medicinska fakulteten)
(creator_code:org_t)
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Ingår i:Biochemical Journal: Portland Press349, s. 697-7010264-60211470-8728
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