Korean J Anat.  2006 Oct;39(5):375-382.

Kinesin Superfamily KIF1Balpha Protein Binds to the PDZ Domain of MALS-3

• Kim SJ
• Lee CH
• Park HY
• Yea SS
• Jang WH
• Lee SK
• Park YH
• Jung Y
• Seog DH

Abstract

The Kinesin superfamily proteins (KIFs) make up a large superfamily of molecular motors that transport cargo such as vesicles, protein complexes, and organelles. KIF1Balpha is a monomeric motor that conveys mitochondria and plays an important role in cellular function. Here, we used the yeast two-hybrid system to identify the proteins that interacts with KIF1Balpha and found a specific interaction with the mammalian LIN-7 (MALS)-3/vertebrate homology of LIN-7 (Veri) and synaptic scaffolding molecule (S-SCAM). MALS-3 protein bound to the tail region of KIF1Balpha but not to other kinesin family members in the yeast two-hybrid assay. The "T-X-V" motif at the C-terminal end of KIF1Balpha is essential for interaction with MALS-3. In addition, this protein showed specific interactions in the Glutathione S-transferase (GST) pull-down assay. An antibody to MALS-3 specifically coimmunoprecipitated KIF1Balpha associated with MALS-3 from mouse brain extracts. These results suggest that MALS-3, as KIF1Balpha receptor, is involved in the KIF1Balpha-mediated transport.

Keyword

Kinesin; Molecular motors; Microtubule; Adaptor proteins; PDZ; MALS

MeSH Terms

Animals
Brain
Glutathione Transferase
Humans
Kinesin*
Mice
Microtubules
Mitochondria
Organelles
PDZ Domains*
Two-Hybrid System Techniques
Glutathione Transferase
Kinesin