scholarly journals Cell-surface localization of Pellino antagonizes Toll-mediated innate immune signalling by controlling MyD88 turnover in Drosophila

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Shanming Ji ◽  
Ming Sun ◽  
Xiudeng Zheng ◽  
Lin Li ◽  
Liwei Sun ◽  
...  
Keyword(s):  
Cell Surface ◽  
Innate Immune ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals A novel motif in the proximal C-terminus of Pannexin 1 regulates cell surface localization

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Anna L. Epp ◽  
Sarah N. Ebert ◽  
Juan C. Sanchez-Arias ◽  
Leigh E. Wicki-Stordeur ◽  
Andrew K. J. Boyce ◽  
...  
Keyword(s):  
Cell Surface ◽  
Pannexin 1 ◽  
C Terminus ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals Cell Surface Localization of Proteolysis of Human Endothelial Angiotensin I-converting Enzyme

1995 ◽  
Vol 270 (48) ◽  
pp. 28962-28969 ◽  
Author(s):  
Véronique Beldent ◽  
Annie Michaud ◽  
Christophe Bonnefoy ◽  
Marie-Thérèse Chauvet ◽  
Pierre Corvol
Keyword(s):  
Cell Surface ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals An essential role for the Glut1 PDZ-binding motif in growth factor regulation of Glut1 degradation and trafficking

2009 ◽  
Vol 418 (2) ◽  
pp. 345-367 ◽  
Author(s):  
Heather L. Wieman ◽  
Sarah R. Horn ◽  
Sarah R. Jacobs ◽  
Brian J. Altman ◽  
Sally Kornbluth ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Glucose Uptake ◽  
Pdz Domain ◽  
Binding Motif ◽  
Lysosomal Degradation ◽  
Interacting Protein ◽  
Surface Localization ◽  
Cell Surface Localization ◽  
Growth Factor Regulation

Cell surface localization of the Glut (glucose transporter), Glut1, is a cytokine-controlled process essential to support the metabolism and survival of haemopoietic cells. Molecular mechanisms that regulate Glut1 trafficking, however, are not certain. In the present study, we show that a C-terminal PDZ-binding motif in Glut1 is critical to promote maximal cytokine-stimulated Glut1 cell surface localization and prevent Glut1 lysosomal degradation in the absence of growth factor. Disruption of this PDZ-binding sequence through deletion or point mutation sharply decreased surface Glut1 levels and led to rapid targeting of internalized Glut1 to lysosomes for proteolysis, particularly in growth factor-deprived cells. The PDZ-domain protein, GIPC (Gα-interacting protein-interacting protein, C-terminus), bound to Glut1 in part via the Glut1 C-terminal PDZ-binding motif, and we found that GIPC deficiency decreased Glut1 surface levels and glucose uptake. Unlike the Glut1 degradation observed on mutation of the Glut1 PDZ-binding domain, however, GIPC deficiency resulted in accumulation of intracellular Glut1 in a pool distinct from the recycling pathway of the TfR (transferrin receptor). Blockade of Glut1 lysosomal targeting after growth factor withdrawal also led to intracellular accumulation of Glut1, a portion of which could be rapidly restored to the cell surface after growth factor stimulation. These results indicate that the C-terminal PDZ-binding motif of Glut1 plays a key role in growth factor regulation of glucose uptake by both allowing GIPC to promote Glut1 trafficking to the cell surface and protecting intracellular Glut1 from lysosomal degradation after growth factor withdrawal, thus allowing the potential for a rapid return of intracellular Glut1 to the cell surface on restimulation.

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