Kinesin-1-dependent transport of the ßPIX/GIT complex in neuronal cells.
BMB Rep
; 54(7): 380-385, 2021 Jul.
Article
em En
| MEDLINE
| ID: mdl-34154701
ABSTRACT
Proper targeting of the ßPAK-interacting exchange factor (ßPIX)/G protein-coupled receptor kinase-interacting target protein (GIT) complex into distinct cellular compartments is essential for its diverse functions including neurite extension and synaptogenesis. However, the mechanism for translocation of this complex is still unknown. In the present study, we reported that the conventional kinesin, called kinesin-1, can transport the ßPIX/GIT complex. Additionally, ßPIX bind to KIF5A, a neuronal isoform of kinesin-1 heavy chain, but not KIF1 and KIF3. Mapping analysis revealed that the tail of KIF5s and LZ domain of ßPIX were the respective binding domains. Silencing KIF5A or the expression of a variety of mutant forms of KIF5A inhibited ßPIX targeting the neurite tips in PC12 cells. Furthermore, truncated mutants of ßPIX without LZ domain did not interact with KIF5A, and were unable to target the neurite tips in PC12 cells. These results defined kinesin-1 as a motor protein of ßPIX, and may provide new insights into ßPIX/GIT complex-dependent neuronal pathophysiology. [BMB Reports 2021; 54(7) 380-385].
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cinesinas
/
Proteínas de Ciclo Celular
/
Fatores de Troca de Nucleotídeo Guanina Rho
Limite:
Animals
Idioma:
En
Revista:
BMB Rep
Assunto da revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Ano de publicação:
2021
Tipo de documento:
Article