NDLI: Calpain Sensitive Regions in the N-terminal Cytoplasmic Domains of Glycine Transporters GlyT1A and GlyT1B

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Calpain Sensitive Regions in the N-terminal Cytoplasmic Domains of Glycine Transporters GlyT1A and GlyT1B

Content Provider	Springer Nature Link
Author	Baliova, Martina Jursky, Frantisek
Copyright Year	2005
Abstract	Glycine transporters are members of the Na$^{+}$/Cl$^{−}$ dependent transporter gene family and play crucial roles in regulating inhibitory as well as excitatory neurotransmission. In this report we show that calcium elevation in spinal cord synaptosomes decreases the levels of glycine transporter, GlyT1, N-terminal immunoreactivity, and that this decrease can be blocked by calpain inhibitor. Sequencing of GST fusion proteins containing the N-terminal domains of GlyT1A and B splice variants cleaved with rat recombinant calpain identified calpain cleavage sites after glycine 17 in GlyT1B and N-terminally of the first conserved arginine residue in both GlyT1A and GlyT1B. Expression in HEK293 cells revealed that truncation of the N-terminus of GlyT1 results in significant inhibition of glycine uptake. A syntaxin1A GST fusion protein was able to pull-down N-terminally deleted GlyT1, indicating that calpain cleavage does not eliminate syntaxin1A binding. These results suggest that calpain cleavage may regulate the transport activity/turnover of GlyT1 in vivo by cleaving its N-terminal domain.
Starting Page	1093
Ending Page	1100
Page Count	8
File Format	PDF
ISSN	03643190
Journal	Neurochemical Research
Volume Number	30
Issue Number	9
e-ISSN	15736903
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2005-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calcium calpain Glycine transporter GlyT1 Syntaxin1A Neurosciences Neurology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Cellular and Molecular Neuroscience

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