SH2 and SH3 domain interactions and characterization of a novel protein POSH2 (Pehmeäkantinen kirja)

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Modular protein domains mediate protein-protein interactions in various cellular proteins, including adaptors, enzymes and scaffold proteins. Src homology 2 (SH2)domains comprise a relatively large group of domains, which mediate inter- and intramolecular interactions by binding to tyrosine-phosphorylated ligands.

Phosphorylation of tyrosine residues in proteins controls many facets of signaling in multicellular organisms, and increased tyrosine phosphorylation is associated with uncontrolled cell growth. Another group of domains, Src homology 3 (SH3) domains, mediates protein interactions by binding to ligands containing a polyproline type II (PPII) helix. SH3 domains mediate generally relatively low specificity and affinity interactions, although this might be due to the use of short ligands lacking the regions flanking the binding interface of SH3 domains. These outside regions are known to contribute to the ligand binding of SH3 domains. POSH proteins, which have been implicated as scaffold proteins in the JNK-mediated apoptosis signaling cascade, contain SH3 domains. POSH proteins also participate in protein trafficking and the regulation of protein degradation via ubiquitination.
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