The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B

Russell J Diefenbach, Eve Diefenbach, Mark W Douglas, Anthony L. Cunningham

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

The conventional microtubule-dependent motor protein kinesin consists of heavy and light chains both of which have been documented to bind a variety of potential linker or cargo proteins. In this study we employed a yeast two-hybrid assay to identify additional binding partners of the kinesin heavy chain isoform KIF5B. A human brain cDNA library was screened with a bait corresponding to amino acid residues 814-963 of human KIF5B. This screen identified the ribosome receptor, p180, as a KIF5B-binding protein. The sites of interaction are residues 1294-1413 of p180 and the C-terminal half of the cargo binding-domain of KIF5B (residues 867-907). The KIF5B-binding site in p180 is homologous to the previously determined KIF5B-binding site in kinectin. The interacting regions of p180 and KIF5B consist almost entirely of heptad repeats, suggesting the interaction is a coiled-coil. A role for the kinesin/p180 interaction may include mRNA localization and/or transport of endoplasmic reticulum-derived vesicles.

Original languageEnglish
Pages (from-to)987-992
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume319
Issue number3
DOIs
Publication statusPublished - 2 Jul 2004
Externally publishedYes

Keywords

  • Animals
  • Humans
  • Kinesin
  • Microtubule-Associated Proteins
  • Protein Binding
  • Receptors, Cytoplasmic and Nuclear
  • Two-Hybrid System Techniques
  • Journal Article
  • Research Support, Non-U.S. Gov't

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