The Korean Journal of Physiology and Pharmacology

The Korean Society of Pharmacology (대한약리학회)
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Kinesin Superfamily KIF5 Proteins Bind to ${\beta}III$ Spectrin

  • Paik, Jae-Eun (Departments of Biochemistry and Molecular Cell Physiology Research Group, College of Medicine, Inje University) ;
  • Kim, Na-Ri (Departments of Physiology and Biophysics and Molecular Cell Physiology Research Group, College of Medicine, Inje University) ;
  • Yea, Sung-Su (Departments of Biochemistry, College of Medicine, Inje University) ;
  • Jang, Won-Hee (Departments of Biochemistry, College of Medicine, Inje University) ;
  • Chung, Joon-Young (Departments of Parasitology and Molecular Cell Physiology Research Group, College of Medicine, Inje University) ;
  • Lee, Sang-Kyoung (Departments of Psychiatry and Molecular Cell Physiology Research Group, College of Medicine, Inje University) ;
  • Park, Yeong-Hong (Departments of Biochemistry, College of Medicine, Inje University) ;
  • Han, Jin (Departments of Physiology and Biophysics and Molecular Cell Physiology Research Group, College of Medicine, Inje University) ;
  • Seog, Dae-Hyun (Departments of Biochemistry and Molecular Cell Physiology Research Group, College of Medicine, Inje University)
  • Published : 2004.06.21
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Abstract

The kinesin proteins (KIFs) make up a large superfamily of molecular motors that transport cargo such as vesicles, protein complexes, and organelles. KIF5 is a heterotetrameric motor that conveys vesicles and plays an important role in neuronal function. Here, we used the yeast two-hybrid system to identify the neuronal protein(s) that interacts with the tail region of KIF5 and found a specific interaction with ${\beta}III$ spectrin. The amino acid residues between 1394 and 1774 of ${\beta}III$ spectrin were required for the interaction with KIF5C. ${\beta}III$ spectrin also bound to the tail region of neuronal KIF5A and ubiquitous KIF5B but not to other kinesin family members in the yeast two-hybrid assay. In addition, these proteins showed specific interactions, confirmed by GST pull-down assay and co-immunoprecipitation. ${\beta}III$ spectrin interacted with GST-KIF5 fusion proteins, but not with GST alone. An antibody to ${\beta}III$ spectrin specifically co-immunoprecipitated KIF5s associated with ${\beta}III$ spectrin from mouse brain extracts. These results suggest that KTF5 motor proteins transport vesicles or organelles that are coated with ${\beta}III$ spectrin.

Keywords

References

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