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p Orchestrating ser...
p Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs
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- Kliche, Johanna (författare)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Biokemi
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- Ivarsson, Ylva (författare)
- Uppsala universitet,Biokemi
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(creator_code:org_t)
- PORTLAND PRESS LTD, 2022
- 2022
- Engelska.
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Ingår i: Biochemical Journal. - : PORTLAND PRESS LTD. - 0264-6021 .- 1470-8728. ; 479:1, s. 1-22
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Abstract
Ämnesord
Stäng
- Cellular function is based on protein-protein interactions. A large proportion of these interactions involves the binding of short linear motifs (SLiMs) by folded globular domains. These interactions are regulated by post-translational modifications, such as phosphorylation, that create and break motif binding sites or tune the affinity of the interactions. In addition, motif-based interactions are involved in targeting serine/threonine kinases and phosphatases to their substrate and contribute to the specificity of the enzymatic actions regulating which sites are phosphorylated. Here, we review how SLiM-based interactions assist in determining the specificity of serine/threonine kinases and phosphatases, and how phosphorylation, in turn, affects motif-based interactions. We provide examples of SLiM-based interactions that are turned on/off, or are tuned by serine/threonine phosphorylation and exemplify how this affects SLiM-based protein complex formation.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- kinase
- modular domain
- phosphatase
- protein–protein interactions
- SLiM
Publikations- och innehållstyp
- ref (ämneskategori)
- for (ämneskategori)
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