Abstract
Scaffold proteins ITSN1 and ITSN2 interact with nuclear RNA-binding proteins
Highlights
Scaffold proteins represent a group of biomolecules that are involved in the modulation of various cellular processes
We suggested that ITSN1/2 SH3 domains play an essential role in the interaction between ITSN1/2 and RNA-binding-proteins (RBPs) as multiple RNA-binding proteins (RBPs) possess proline-rich motifs that directly interact with SH3 domains whereas ITSN1/2-RBPs complexes might be involved in novel nucleus-cytoplasm crosstalk pathways
The analysis demonstrated that ITSN1 SH3 domains precipitated all studied RNA-binding proteins (Fig. 1 A, B, C) whereas SAM68 showed the most significant binding
Summary
Scaffold proteins represent a group of biomolecules that are involved in the modulation of various cellular processes. These proteins are composed of multiple protein-interacting domains and serve as platforms for the formation of functional protein complexes [1]. Intersectins (ITSN1 and ITSN2) are evolutionarily conserved scaffold proteins encoded by two paralogous genes. Long isoforms of ITSN1 (ITSN1l) and ITSN2 (ITSN2l) contain additional C-terminal DH-PH-C2 domains involved in the specific activation of GTPase Cdc42 [3]. ITSN1s, ITSN2s and ITSN2l are expressed ubiquitously whereas ITSN1l is expressed only in neurons [4].
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