The scaffold protein MUPP1 regulates odorant-mediated signaling in olfactory sensory neurons

J Cell Sci. 2014 Jun 1;127(Pt 11):2518-27. doi: 10.1242/jcs.144220. Epub 2014 Mar 20.

Abstract

The olfactory signal transduction cascade transforms odor information into electrical signals by a cAMP-based amplification mechanism. The mechanisms underlying the very precise temporal and spatial organization of the relevant signaling components remains poorly understood. Here, we identify, using co-immunoprecipitation experiments, a macromolecular assembly of signal transduction components in mouse olfactory neurons, organized through MUPP1. Disruption of the PDZ signaling complex, through use of an inhibitory peptide, strongly impaired odor responses and changed the activation kinetics of olfactory sensory neurons. In addition, our experiments demonstrate that termination of the response is dependent on PDZ-based scaffolding. These findings provide new insights into the functional organization, and regulation, of olfactory signal transduction.

Keywords: MUPP1; Olfactory neuron; PDZ; Scaffolding protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cyclic AMP / metabolism
  • HEK293 Cells
  • Humans
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • Microfilament Proteins / metabolism
  • Multiprotein Complexes / metabolism*
  • Olfactory Mucosa / physiology*
  • Olfactory Receptor Neurons / metabolism
  • PDZ Domains / genetics
  • Peptide Fragments / metabolism
  • Protein Binding
  • Receptors, Odorant / metabolism
  • Signal Transduction

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Mpdz protein, mouse
  • Multiprotein Complexes
  • Peptide Fragments
  • Receptors, Odorant
  • fascin1 protein, mouse
  • Cyclic AMP