PMID- 10461881
OWN - NLM
STAT- MEDLINE
DCOM- 19990914
LR  - 20190630
IS  - 0022-3042 (Print)
IS  - 0022-3042 (Linking)
VI  - 73
IP  - 3
DP  - 1999 Sep
TI  - Regulation of synaptotagmin I phosphorylation by multiple protein kinases.
PG  - 921-32
AB  - Synaptotagmin I has been suggested to function as a low-affinity calcium sensor
      for calcium-triggered exocytosis from neurons and neuroendocrine cells. We have
      studied the phosphorylation of synaptotagmin I by a variety of protein kinases in
      vitro and in intact preparations. SyntagI, the purified, recombinant, cytoplasmic
      domain of rat synaptotagmin I, was an effective substrate in vitro for
      Ca2+/calmodulin-dependent protein kinase II (CaMKII), protein kinase C (PKC), and
      casein kinase II (caskII). Sequencing of tryptic phosphopeptides from syntagI
      revealed that CaMKII and PKC phosphorylated the same residue, corresponding to
      Thr112, whereas caskII phosphorylated two residues, corresponding to Thr125 and
      Thr128. Endogenous synaptotagmin I was phosphorylated on purified synaptic
      vesicles by all three kinases. In contrast, no phosphorylation was observed on
      clathrin-coated vesicles, suggesting that phosphorylation of synaptotagmin I in
      vivo occurs only at specific stage(s) of the synaptic vesicle life cycle. In rat 
      brain synaptosomes and PC12 cells, K+-evoked depolarization or treatment with
      phorbol ester caused an increase in the phosphorylation state of synaptotagmin I 
      at Thr112. The results suggest the possibility that the phosphorylation of
      synaptotagmin I by CaMKII and PKC contributes to the mechanism(s) by which these 
      two kinases regulate neurotransmitter release.
FAU - Hilfiker, S
AU  - Hilfiker S
AD  - Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New
      York, New York 10021, USA.
FAU - Pieribone, V A
AU  - Pieribone VA
FAU - Nordstedt, C
AU  - Nordstedt C
FAU - Greengard, P
AU  - Greengard P
FAU - Czernik, A J
AU  - Czernik AJ
LA  - eng
GR  - MH39327/MH/NIMH NIH HHS/United States
GR  - NS35941/NS/NINDS 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 (Calcium-Binding Proteins)
RN  - 0 (Clathrin)
RN  - 0 (Isoenzymes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Phosphoamino Acids)
RN  - 0 (SYT1 protein, human)
RN  - 0 (Synaptotagmin I)
RN  - 0 (Syt1 protein, rat)
RN  - 134193-27-4 (Synaptotagmins)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.1 (Casein Kinase II)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.13 (Protein Kinase C)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Calcium-Binding Proteins
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2
MH  - Calcium-Calmodulin-Dependent Protein Kinases/metabolism
MH  - Casein Kinase II
MH  - Cell Differentiation
MH  - Clathrin/pharmacology
MH  - Conserved Sequence
MH  - Humans
MH  - Isoenzymes/metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*metabolism
MH  - PC12 Cells
MH  - Peptide Mapping
MH  - Phosphoamino Acids/metabolism
MH  - Phosphorylation
MH  - Protein Kinase C/metabolism
MH  - Protein Kinases/*metabolism
MH  - Protein-Serine-Threonine Kinases/metabolism
MH  - Rats
MH  - Synaptosomes/metabolism
MH  - Synaptotagmin I
MH  - Synaptotagmins
EDAT- 1999/08/26 00:00
MHDA- 1999/08/26 00:01
CRDT- 1999/08/26 00:00
PHST- 1999/08/26 00:00 [pubmed]
PHST- 1999/08/26 00:01 [medline]
PHST- 1999/08/26 00:00 [entrez]
AID - 10.1046/j.1471-4159.1999.0730921.x [doi]
PST - ppublish
SO  - J Neurochem. 1999 Sep;73(3):921-32. doi: 10.1046/j.1471-4159.1999.0730921.x.