Related Experiment Video
Updated: Apr 22, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
rCNT2 extracellular cysteines, Cys(615) and Cys(649), are important for maturation and sorting to the plasma membrane
Itziar Pinilla-Macua1, Ana Claudio-Montero1, Marçal Pastor-Anglada1
1Department of Biochemistry and Molecular Biology, University of Barcelona, Institute of Biomedicine (IBUB) and Oncology Program, National Biomedical Research Institute on Liver and Gastrointestinal Diseases (CIBER ehd), Instituto de Salud Carlos III, Barcelona, Spain.
Abstract:
rCNT2 is a purine-preferring concentrative nucleoside transporter implicated in the regulation of extracellular adenosine levels and purinergic signaling. This study addressed the analysis of the CNT2 C-terminus tail as a domain likely to be implicated in transporter sorting. The topological mapping of this segment revealed that Cys(615) and Cys(649) are important residues for the proper trafficking of CNT2 to the plasma membrane. The inhibition of protein disulfide isomerase (PDI) and ER glycosidase I and II impaired rCNT2 trafficking to the cell surface, similarly to Cys(615) and Cys(649) mutants. The present work suggests these two cysteine residues are relevant for the proper sorting of the transporter and its functional performance.
More Related Videos
Related Concept Videos
Transport Across the Golgi
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Mitochondrial Precursor Proteins
Most of the mitochondrial...
Bacterial Protein Maturation
Export of Misfolded Proteins out of the ER
Protein Folding Quality Check in the RER

