Skip to main content

Regulation of G-Protein-Coupled Receptor Signalling by the Scaffolding Proteins Spinophilin/Neurabin 2 and Neurabin 1

Buy Article:

$63.00 plus tax (Refund Policy)


Neurabin 1 and neurabin 2/spinophilin were discovered in late 1990s on the basis of their F-actin-binding and protein phosphatase 1 catalytic subunit (PP1c) modulation activities. The neurabins are proteins with modular domains, such as one F-actin-, a receptor- (not found in neurabin 1) and a PP1c-binding domains, a PSD95/DLG/zo-1, three coiledcoil domains and a sterile alpha motif (not found in spinophilin) that govern protein-protein interactions. In the past years, the roles of neurabins have evolved from PP1c-regulatory subunits to important scaffolds binding to a rapidly growing list of cellular proteins. Among the spinophilin and neurabin 1 interactomes, some partner proteins are involved in G-proteincoupled receptor (GPCR) signalling. The most significant difference is that spinophilin, but not neurabin 1, interacts with and plays a specific and direct role in the regulation of at least the α-adrenergic (AR), muscarinic-acetylcholine (m- AChR), dopamine D2 and mu opioid receptors. In contrast, the two scaffolding proteins bind to different members of the regulator of G-protein signalling (RGS) familly. Spinophilin antagonizes multiple functions of arrestin and G-proteincoupled receptor kinase 2 in α-AR signalling. Moreover, spinophilin and neurabin 1 form a functional pair of opposing regulators that reciprocally regulate signalling intensity by the α1-AR. To date, the data on the regulation of GPCR signalling by neurabin 1 are very sparse and the reciprocal regulation seems not to be a general phenomenon. Several studies make on the α1-AR and the m-AChR suggest that spinophilin may selectively regulate Gq-coupled receptor signalling. This review highlights information regarding spinophilin and neurabin 1 function in GPCR signalling.

Keywords: F-actin; F-actin-binding domain; G protein; G-PROTEIN-COUPLED RECEPTOR SIGNALLING; GPCR; PP1c-binding domain; RGS protein; Xenopus laevis; cAMP-dependent PK; neurabin; protein phosphatase 1; scaffold protein; spinophilin; sterile alpha motif

Document Type: Research Article


Publication date: May 1, 2011

More about this publication?
  • Current Chemical Biology aims to publish full-length and mini reviews on exciting new developments at the chemistry-biology interface, covering topics relating to Chemical Synthesis, Science at Chemistry-Biology Interface and Chemical Mechanisms of Biological Systems.

    Current Chemical Biology covers the following areas: Chemical Synthesis (Syntheses of biologically important macromolecules including proteins, polypeptides, oligonucleotides, oligosaccharides etc.; Asymmetric synthesis; Combinatorial synthesis; Diversity-oriented synthesis; Template-directed synthesis; Biomimetic synthesis; Solid phase biomolecular synthesis; Synthesis of small biomolecules: amino acids, peptides, lipids, carbohydrates and nucleosides; and Natural product synthesis).

    Science at Chemistry-Biology Interface (Chemical informatics; Macromolecular catalysts and receptors; Enzymatic synthesis; Biosynthetic engineering; Combinatorial biosynthesis; Plant cell based chemistry; Bacterial and viral cell based chemistry; Chemistry of cellular processes in plants/animals; Receptor chemistry; Cell signaling chemistry; Drug design through understanding of disease processes; Synthetic biology; New high throughput screening techniques; Small molecular array fabrication; Chemical genomics; Chemical and biological approaches to carbohydrates proteins and nucleic acids design; Chemical and biological regulation of biosynthetic pathways; and Unnatural biomolecular analogs).

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more