Kinesin Superfamily KIF1Balpha Protein Binds to the PDZ Domain of MALS-3.
- Author:
Sang Jin KIM
1
;
Chul Hee LEE
;
Hye Young PARK
;
Sung Su YEA
;
Won Hee JANG
;
Sang Kyeong LEE
;
Yeong Hong PARK
;
Yongwook JUNG
;
Dae Hyun SEOG
Author Information
1. Department of Biochemistry, College of Medicine,Inje University, Busan 614-735, Korea. daehyun@inje.ac.kr
- Publication Type:Original Article
- Keywords:
Kinesin;
Molecular motors;
Microtubule;
Adaptor proteins;
PDZ;
MALS
- MeSH:
Animals;
Brain;
Glutathione Transferase;
Humans;
Kinesin*;
Mice;
Microtubules;
Mitochondria;
Organelles;
PDZ Domains*;
Two-Hybrid System Techniques
- From:Korean Journal of Anatomy
2006;39(5):375-382
- CountryRepublic of Korea
- Language:English
-
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.
