Cargando…
The amino terminus of GLUT4 functions as an internalization motif but not an intracellular retention signal when substituted for the transferrin receptor cytoplasmic domain
Previous studies have demonstrated that the amino-terminal cytoplasmic domain of GLUT4 contains a phenylalanine-based targeting motif that determines its steady state distribution between the surface and the interior of cells (Piper, R. C., C. Tai, P. Kuleza, S. Pang, D. Warnock, J. Baenziger, J. W....
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1994
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119955/ https://www.ncbi.nlm.nih.gov/pubmed/8120093 |
Ejemplares similares
-
GLUT-4 NH2 terminus contains a phenylalanine-based targeting motif that regulates intracellular sequestration
Publicado: (1993) -
An intracellular motif of GLUT4 regulates fusion of GLUT4-containing vesicles
por: Heyward, Catherine A, et al.
Publicado: (2008) -
The efficient intracellular sequestration of the insulin-regulatable glucose transporter (GLUT-4) is conferred by the NH2 terminus
Publicado: (1992) -
Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization
Publicado: (1990) -
Evolution of the Twist Subfamily Vertebrate Proteins: Discovery of a Signature Motif and Origin of the Twist1 Glycine-Rich Motifs in the Amino-Terminus Disordered Domain
por: Rodriguez, Yacidzohara, et al.
Publicado: (2016)