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Title: Integrating disorder in globular multidomain proteins: Fuzzy sensors and the role of SH3 domains
Author: Arbesú Andrés, Miguel
Pons Vallès, Miquel
Keywords: Proteïnes quinases
Cèl·lules eucariotes
Protein kinases
Eukaryotic cells
Issue Date: 30-Nov-2019
Publisher: Elsevier
Abstract: Intrinsically disordered proteins represent about one third of eukaryotic proteins. An additional third correspond to proteins containing folded domains as well as large intrinsically disordered regions (IDR). While IDRs may represent functionally autonomous domains, in some instances it has become clear that they provide a new layer of regulation for the activity displayed by the folded domains. The sensitivity of the conformational ensembles defining the properties of IDR to small changes in the cellular environment and the capacity to modulate this response through post-translational modifications makes IDR ideal sensors enabling continuous, integrative responses to complex cellular inputs. Folded domains (FD), on the other hand, are ideal effectors, e.g. by catalyzing enzymatic reactions or participating in binary on/off switches. In this perspective review we discuss the possible role of intramolecular fuzzy complexes to integrate the very different dynamic scales of IDR and FD, inspired on the recent observations of such dynamic complexes in Src family kinases, and we explore the possible general role of the SH3 domains connecting IDRs and FD.
Note: Versió postprint del document publicat a:
It is part of: Archives of Biochemistry and Biophysics, 2019, vol. 677, p. 108161
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ISSN: 0003-9861
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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