The beta-thymosin/WH2 fold: multifunctionality and structure.
作者： R. DOMINGUEZ
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摘要: Remodeling of the actin cytoskeleton in cells is tightly regulated by a vast number actin-binding proteins (ABPs). These interact with via limited set conserved folding motifs. One most abundant motifs beta-thymosin fold, represented prototypical actin-monomer sequestering protein thymosin-beta4. Among many cytoskeletal proteins, fold adopts shorter form, known as WASP homology domain 2. Some characteristic features beta-thymosin/WH2 include its small size (17-43 aa), significant sequence and length variability, frequent occurrence form tandem repeats, remarkable multifunctionality. This paper discusses relationship between structure function on basis four examples: (1) monomer sequestration (thymosin-beta4), (2) filament nucleation (WASP-Arp2/3 complex, Lmod, spire), (3) elongation (Ena/VASP), (4) scaffolding (IRSp53 MIM). Although core all these binding, specific changes modular organization which it found give rise to diverse functions regulation dynamics.
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