Titlebook: SH Domains; Structure, Mechanism Natalya Kurochkina Book 2015 Springer International Publishing Switzerland 2015 PTKs.Protein interaction.P

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Cytoskeletal Signaling by Src Homology Domain-Containing Adaptor Proteins,(Koch et al. .). This prediction expresses the motivation for the present chapter, which aims to review how SH domain-containing proteins regulate the cytoskeleton, while focusing on how such proteins interact directly with factors that control actin remodeling.

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Helical Assemblies and SH Domains,es composed of tens or even hundreds of proteins. In this chapter, molecular assemblies involved in these processes are described. The emphasis is made on proteins for which function depends on protein-protein interactions with involvement of SH domains and helical assemblies.

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Versatility of SH3 Domains in the Cellular Machinery,ach this high versatility via: (i) The main SH3 recognition motif, proline-rich sequences, presents a geometric two-fold pseudo-symmetry and therefore ligands can bind in either of two possible orientations; (ii) In addition to the canonical sequence, SH3 domains can recognize other interaction moti

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Activation of PI3K by Thyroid Hormone Nuclear Receptors,ntaining metabolic homeostasis. Three major T3 binding TR isoforms (α1, β1, and β2), are encoded by the . and . genes. Increasing evidence has shown that besides the classical mode of nuclear actions, TRs could act via extra-nuclear signaling. One important extra-nuclear pathway is mediated via phos

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,SH Domains’ Interaction with SLiMs: Maximizing Adaptivity of Signaling Networks,ave an impact on diversities of cellular processes such as cell growth, cell migration, immune response, etc. SH2 and SH3 domains recognize and bind to specific primary sequences less than 10 amino acids in length called Short Linear Motifs (SLiMs). By systematically studying the conservation of SLi

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SH Domains and Epidermal Growth Factor Receptors, growth factor (EGFR) is one of the key molecules associated with cancer. Mutant alleles of EGFR L858R and Del E746-A750, which are common in human lung adenocarcinomas, result in increased phosphorylation of signaling molecules. Receptor tyrosine kinases and EGFR inhibitor MIG6 are more phosphoryla

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SH2 Domain Structures and Interactions, sequences. As such, they mediate protein–protein interactions in order to assemble signalling complexes and transduce information to alter cellular behaviour and physiology. Here we review the progress in understanding the molecular functions and structures of SH2 domains since their discovery in 1