scholarly journals Basolateral Sorting Signal

2020 ◽  
Author(s):  
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PLoS ONE ◽  
2016 ◽  
Vol 11 (12) ◽  
pp. e0167763 ◽  
Author(s):  
Michele D. Kattke ◽  
Albert H. Chan ◽  
Andrew Duong ◽  
Danielle L. Sexton ◽  
Michael R. Sawaya ◽  
...  

1995 ◽  
Vol 108 (1) ◽  
pp. 369-377 ◽  
Author(s):  
K.L. Soole ◽  
M.A. Jepson ◽  
G.P. Hazlewood ◽  
H.J. Gilbert ◽  
B.H. Hirst

To evaluate whether a glycosylphosphatidylinositol (GPI) anchor can function as a protein sorting signal in polarized intestinal epithelial cells, the GPI-attachment sequence from Thy-1 was fused to bacterial endoglucanase E' (EGE') from Clostridium thermocellum and polarity of secretion of the chimeric EGE'-GPI protein was evaluated. The chimeric EGE'-GPI protein was shown to be associated with a GPI anchor by TX-114 phase-partitioning and susceptibility to phosphoinositol-specific phospholipase C. In polarized MDCK cells, EGE' was localized almost exclusively to the apical cell surface, while in polarized intestinal Caco-2 cells, although 80% of the extracellular form of the enzyme was routed through the apical membrane over a 24 hour period, EGE' was also detected at the basolateral membrane. Rates of delivery of EGE'-GPI to the two membrane domains in Caco-2 cells, as determined with a biotinylation protocol, revealed apical delivery was approximately 2.5 times that of basolateral. EGE' delivered to the basolateral cell surface was transcytosed to the apical surface. These data indicate that a GPI anchor does represent a dominant apical sorting signal in intestinal epithelial cells. However, the mis-sorting of a proportion of EGE'GPI to the basolateral surface of Caco-2 cells provides an explanation for additional sorting signals in the ectodomain of some endogenous GPI-anchored proteins.


2000 ◽  
Vol 182 (23) ◽  
pp. 6857-6861 ◽  
Author(s):  
Beatriz Martı́nez ◽  
Jouko Sillanpää ◽  
Egbert Smit ◽  
Timo K. Korhonen ◽  
Peter H. Pouwels

The cbsA gene encoding the collagen-binding S-layer protein of Lactobacillus crispatus JCM5810 was expressed inL. casei ATCC 393T. The S-protein was not retained on the surface of the recombinant bacteria but was secreted into the medium. By translational fusion of CbsA to the cell wall sorting signal of the proteinase, PrtP, of L. casei, CbsA was presented at the surface, rendering the transformants able to bind to immobilized collagens.


Traffic ◽  
2004 ◽  
Vol 5 (6) ◽  
pp. 437-448 ◽  
Author(s):  
Tomoo Shiba ◽  
Satoshi Kametaka ◽  
Masato Kawasaki ◽  
Masahiro Shibata ◽  
Satoshi Waguri ◽  
...  
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FEBS Letters ◽  
1992 ◽  
Vol 308 (1) ◽  
pp. 14-17 ◽  
Author(s):  
Lotte Katrine Vogel ◽  
Ove Norén ◽  
Hans Sjöström

2005 ◽  
Vol 18 (5) ◽  
pp. 519-531 ◽  
Author(s):  
Stefan Höning ◽  
Doris Ricotta ◽  
Michael Krauss ◽  
Kira Späte ◽  
Barbara Spolaore ◽  
...  

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