The carboxy-terminal region of the TBC1D4 (AS160) RabGAP mediates protein homodimerization.
Int J Biol Macromol
; 103: 965-971, 2017 Oct.
Article
en En
| MEDLINE
| ID: mdl-28545963
ABSTRACT
TBC1D4 (also known as AS160) is a Rab·GTPase-activating protein (RabGAP) which functions in insulin signaling. TBC1D4 is critical for translocation of glucose transporter 4 (GLUT4), from an inactive, intracellular, vesicle-bound site to the plasma membrane, where it promotes glucose entry into cells. The TBC1D4 protein is structurally subdivided into two N-terminal phosphotyrosine-binding (PTB) domains, a C-terminal catalytic RabGAP domain, and a disordered segment in between containing potential Akt phosphorylation sites. Structural predictions further suggest that a region C-terminal to the RabGAP domain adopts a coiled-coil motif. We show that C-terminal region (CTR) region is largely α-helical and mediates TBC1D4 RabGAP dimerization. RabGAP catalytic activity and thermal stability appear to be independent of CTR-mediated dimerization.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Activadoras de GTPasa
/
Multimerización de Proteína
Límite:
Humans
Idioma:
En
Revista:
Int J Biol Macromol
Año:
2017
Tipo del documento:
Article