Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2008 Apr;86(5):1036-43.
doi: 10.1002/jnr.21568.

Increased plasma membrane localization of O-glycosylation-deficient mutant of synaptotagmin I in PC12 cells

Eiko Kanno  1 , Mitsunori Fukuda
Affiliations

Increased plasma membrane localization of O-glycosylation-deficient mutant of synaptotagmin I in PC12 cells

Eiko Kanno et al. J Neurosci Res. 2008 Apr.

Abstract

Synaptotagmin I (Syt I) is a Ca2+-binding protein on synaptic vesicles and presumably functions as a Ca2+ sensor for neurotransmitter release. Native Syt I protein in neuroendocrine PC12 cells undergoes several posttranslational modifications, such as O-glycosylation, N-glycosylation, and fatty acylation, and the latter two modifications have been shown to be required for the proper function of murine Syt I in PC12 cells. However, nothing is known about the physiological significance of the O-glycosylation of Syt I in dense-core vesicle exocytosis in PC12 cells. In this study, we created an O-glycosylation-deficient mutant (named TA = T15A/T16A) and an N-glycosylation-deficient mutant of Syt I (named T26A) and investigated their subcellular distribution in Syt I-deficient PC12 cells, where other Syt isoforms (e.g., IV and IX) and other membrane trafficking proteins (e.g., Rab27A, SNAP-25, syntaxin-1, and VAMP-2) are normally expressed. We found that some cells expressing high level of recombinant wild-type (WT) Syt I protein show mistargeting of Syt I(WT) protein to the plasma membrane, whereas most of the cells show normal dense-core vesicle localization of Syt I(WT) protein. Similar mistargeting was also observed in cells expressing high levels of the Syt I(T26A) and Syt I(TA) mutants, but the mistargeting of the Syt I(TA) mutant to the plasma membrane was much more evident than with the Syt I(WT) or (T26A) mutant. The results indicate that O-glycosylation, not N-glycosylation, is partially involved in efficient targeting of Syt I protein to dense-core vesicles in PC12 cells.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

Publication types

MeSH terms

LinkOut - more resources