Association of the kinesin motor KIF1A with the multimodular protein liprin-alpha

J Biol Chem. 2003 Mar 28;278(13):11393-401. doi: 10.1074/jbc.M211874200. Epub 2003 Jan 8.

Abstract

Liprin-alpha/SYD-2 is a multimodular scaffolding protein important for presynaptic differentiation and postsynaptic targeting of alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid glutamate receptors. However, the molecular mechanisms underlying these functions remain largely unknown. Here we report that liprin-alpha interacts with the neuron-specific kinesin motor KIF1A. KIF1A colocalizes with liprin-alpha in various subcellular regions of neurons. KIF1A coaccumulates with liprin-alpha in ligated sciatic nerves. KIF1A cofractionates and coimmunopreciptates with liprin-alpha and various liprin-alpha-associated membrane, signaling, and scaffolding proteins including alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid receptors, GRIP/ABP, RIM, GIT1, and beta PIX. These results suggest that liprin-alpha functions as a KIF1A receptor, linking KIF1A to various liprin-alpha-associated proteins for their transport in neurons.

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Brain / metabolism
  • Immunohistochemistry
  • Kinesins / metabolism*
  • Microscopy, Immunoelectron
  • Nerve Tissue Proteins / metabolism*
  • Phosphoproteins / metabolism*
  • Precipitin Tests
  • Protein Binding
  • Rats
  • Receptors, AMPA / metabolism
  • Signal Transduction
  • Subcellular Fractions / metabolism
  • Two-Hybrid System Techniques

Substances

  • Adaptor Proteins, Signal Transducing
  • Kif1a protein, rat
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Ppfia4 protein, rat
  • Receptors, AMPA
  • Kinesins