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question about 3'UTR

Barry Shur barry at cellbio.emory.edu
Wed Jun 16 13:50:56 EST 2004

Dear Glycobiologist colleagues:

A graduate student in a neuroscience program has approached me with 
an observation that I cannot address. He is studying the function of 
naturally occurring polymorphisms in the 3'UTR of the dopamine 
transporter (varying occurrences of a 40 bp repeat, usually 9 or 10 
repeats). He created constructs containing 0 -10 repeats, but did not 
modify the sequences encoding protein. All constructs were expressed 
fine in heterologous cells, and produced varying amounts of 
radiolabeled ligand binding for each construct that appears to be a 
reflection of the amount of protein made. When he ran Western blots 
of these lysates, the different proteins are differentially 
glycosylated, as judged by migration on SDS-PAGE. Enzymatic 
deglycosylation reduced all of their sizes to that expected of the 
dopamine transporter polypeptide core.

Does anyone know of a precedent in which the 3'UTR influences the 
degree of glycosylation? The one idea I had was that it was a 
reflection of transit time through the secretory pathway, but the 
glycosylation patterns (by 1D gels) do not correlate with the amount 
of dopamine transporter synthesized by these cells (i.e., the 
constructs making the most and least protein are both maximally 
glycosylated vs other constructs)

Any ideas would be greatly appreciated.

Best regards,

Barry Shur
Barry D. Shur, Ph.D.
Candler Professor and Chairman
Department of Cell Biology
Emory University School of Medicine
615 Michael Street
Atlanta, GA 30322

voice: 404-727-4315
cell: 404-313-5469
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email: barry at cellbio.emory.edu

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