Multiple Regulation of Roundabout (Robo) Phosphorylation in a Heterologous Cell System
The Korean Journal of Physiology and Pharmacology
;
: 111-115, 2004.
Article
in English
| WPRIM
| ID: wpr-728494
ABSTRACT
Roundabout (Robo) is the transmembrane receptor for slit, the neuronal guidance molecule. In this study, the tyrosine phosphorylation of Robo was observed in Robo-transfected human embryonic kidney cells and developing rat brains, and found to be increased by the treatment with protein kinase A activator, forskolin. In contrast, protein kinase C activation by phorbol-12-myristate-13-acetate decreased the phosphorylation of Robo. Intracellular calcium was required for the tyrosine phosphorylation. Furthermore, the transfection of an Eph receptor tyrosine kinase dramatically enhanced the tyrosine phosphorylation. These findings indicate that the tyrosine phosphorylation of Robo is regulated by multiple mechanisms, and that Eph receptor kinases may play a role in the regulation of tyrosine phosphorylation of Robo in the rat brain.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Phosphorylation
/
Phosphotransferases
/
Protein Kinases
/
Tyrosine
/
Brain
/
Colforsin
/
Protein Kinase C
/
Transfection
/
Calcium
/
Cyclic AMP-Dependent Protein Kinases
Type of study:
Practice guideline
Limits:
Animals
/
Humans
Language:
English
Journal:
The Korean Journal of Physiology and Pharmacology
Year:
2004
Type:
Article
Similar
MEDLINE
...
LILACS
LIS