Kinesin Superfamily KIF1Balpha Protein Binds to the PDZ Domain of MALS-3 / 대한해부학회지
Korean Journal of Anatomy
;
: 375-382, 2006.
Artigo
em Inglês
| WPRIM
| ID: wpr-643797
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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Encéfalo
/
Organelas
/
Cinesinas
/
Técnicas do Sistema de Duplo-Híbrido
/
Domínios PDZ
/
Glutationa Transferase
/
Microtúbulos
/
Mitocôndrias
Limite:
Animais
/
Humanos
Idioma:
Inglês
Revista:
Korean Journal of Anatomy
Ano de publicação:
2006
Tipo de documento:
Artigo
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