PMID- 10386995
OWN - NLM
STAT- MEDLINE
DCOM- 19990708
LR  - 20190630
IS  - 0022-3042 (Print)
IS  - 0022-3042 (Linking)
VI  - 73
IP  - 1
DP  - 1999 Jul
TI  - Glycosylation sites flank phosphorylation sites on synapsin I: O-linked
      N-acetylglucosamine residues are localized within domains mediating synapsin I
      interactions.
PG  - 418-28
AB  - Synapsin I is concentrated in nerve terminals, where it appears to anchor
      synaptic vesicles to the cytoskeleton and thereby ensures a steady supply of
      fusion-competent synaptic vesicles. Although phosphorylation-dependent binding of
      synapsin I to cytoskeletal elements and synaptic vesicles is well characterized, 
      little is known about synapsin I's O-linked N-acetylglucosamine (O-GlcNAc)
      modifications. Here, we identified seven in vivo O-GlcNAcylation sites on
      synapsin I by analysis of HPLC-purified digests of rat brain synapsin I. The
      seven O-GlcNAcylation sites (Ser55, Thr56, Thr87, Ser516, Thr524, Thr562, and
      Ser576) in synapsin I are clustered around its five phosphorylation sites in
      domains B and D. The proximity of phosphorylation sites to O-GlcNAcylation sites 
      in the regulatory domains of synapsin I suggests that O-GlcNAcylation may
      modulate phosphorylation and indirectly affect synapsin I interactions. With use 
      of synthetic peptides, however, the presence of an O-GlcNAc at sites Thr562 and
      Ser576 resulted in only a 66% increase in the Km of calcium/calmodulin-dependent 
      protein kinase II phosphorylation of site Ser566 with no effect on its Vmax. We
      conclude that O-GlcNAcylation likely plays a more direct role in synapsin I
      interactions than simply modulating the protein's phosphorylation.
FAU - Cole, R N
AU  - Cole RN
AD  - Department of Biological Chemistry, School of Medicine, Johns Hopkins University,
      Baltimore, Maryland 21205-2185, USA.
FAU - Hart, G W
AU  - Hart GW
LA  - eng
GR  - NSO9415/NS/NINDS NIH HHS/United States
GR  - R01 HD13563/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - J Neurochem
JT  - Journal of neurochemistry
JID - 2985190R
RN  - 0 (Peptide Fragments)
RN  - 0 (Synapsins)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - V956696549 (Acetylglucosamine)
SB  - IM
MH  - Acetylglucosamine/*analysis
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism
MH  - Carbohydrate Conformation
MH  - Chromatography, High Pressure Liquid
MH  - Glycosylation
MH  - Mass Spectrometry
MH  - Molecular Sequence Data
MH  - Peptide Fragments/chemistry/isolation & purification
MH  - Phosphorylation
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Synapsins/*chemistry/*metabolism
EDAT- 1999/07/01 00:00
MHDA- 1999/07/01 00:01
CRDT- 1999/07/01 00:00
PHST- 1999/07/01 00:00 [pubmed]
PHST- 1999/07/01 00:01 [medline]
PHST- 1999/07/01 00:00 [entrez]
AID - 10.1046/j.1471-4159.1999.0730418.x [doi]
PST - ppublish
SO  - J Neurochem. 1999 Jul;73(1):418-28. doi: 10.1046/j.1471-4159.1999.0730418.x.