PMID- 10655491
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 97
IP  - 3
DP  - 2000 Feb 1
TI  - Mouse VAP33 is associated with the endoplasmic reticulum and microtubules.
PG  - 1101-6
AB  - VAMP/synaptobrevin is a synaptic vesicle protein that is essential for
      neurotransmitter release. Intracellular injection of antisera against the Aplysia
      californica VAMP/synaptobrevin-binding protein ApVAP33 inhibited evoked
      excitatory postsynaptic potentials (EPSPs) in cultured cells, suggesting that
      this association may regulate the function of VAMP/synaptobrevin. We have
      identified and characterized a mouse homologue of ApVAP33, mVAP33. The overall
      domain structure of the proteins is conserved, and they have similar biochemical 
      properties. mVAP33 mRNA is detectable in all mouse tissues examined, in contrast 
      to the more restricted expression seen in A. californica. We analyzed the
      cellular distribution of mVAP33 protein in brain slices and cultured cortical
      cells by light and electron microscopy. Although present at higher levels in
      neurons, immunoreactivity was detected throughout both neurons and glia in a
      reticular pattern similar to that of endoplasmic reticulum-resident proteins.
      mVAP33 does not colocalize with VAMP/synaptobrevin at synaptic structures, but
      expression overlaps with lower levels of VAMP/synaptobrevin in the soma.
      Ultrastructural analysis revealed mVAP33 associated with microtubules and
      intracellular vesicles of heterogeneous size. In primary neuronal cultures, large
      aggregates of mVAP33 are also detected in short filamentous structures, which are
      occasionally associated with intracellular membranes. There is no evidence for
      accumulation of mVAP33 on synaptic vesicles or at the plasma membrane. These data
      suggest that mVAP33 is an endoplasmic-reticulum-resident protein that associates 
      with components of the cytoskeleton. Any functional interaction between mVAP33
      and VAMP/synaptobrevin, therefore, most likely involves the delivery of
      components to synaptic terminals rather than a direct participation in synaptic
      vesicle exocytosis.
FAU - Skehel, P A
AU  - Skehel PA
AD  - Division of Neurophysiology, National Institute for Medical Research, The
      Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom. pskehel@nimr.mrc.ac.uk
FAU - Fabian-Fine, R
AU  - Fabian-Fine R
FAU - Kandel, E R
AU  - Kandel ER
LA  - eng
SI  - GENBANK/AF157497
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Carrier Proteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (R-SNARE Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (VAPA protein, human)
RN  - 0 (Vapa protein, mouse)
RN  - 0 (Vapa protein, rat)
RN  - 0 (Vesicular Transport Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Aplysia/immunology
MH  - Carrier Proteins/immunology/*metabolism
MH  - Cells, Cultured
MH  - Endoplasmic Reticulum/*metabolism
MH  - Excitatory Postsynaptic Potentials
MH  - Fluorescent Antibody Technique, Indirect
MH  - Hippocampus/metabolism/ultrastructure
MH  - Humans
MH  - Immunohistochemistry
MH  - Macromolecular Substances
MH  - Membrane Proteins/analysis/immunology/*metabolism
MH  - Mice
MH  - Microtubules/*metabolism
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/immunology/*metabolism
MH  - Neuroglia/metabolism
MH  - Neurons/metabolism
MH  - Organ Specificity
MH  - R-SNARE Proteins
MH  - RNA, Messenger/analysis
MH  - Rats
MH  - Recombinant Fusion Proteins/immunology/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Species Specificity
MH  - Synaptic Vesicles/*metabolism/ultrastructure
MH  - *Vesicular Transport Proteins
PMC - PMC15535
EDAT- 2000/02/03 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/02/03 09:00
PHST- 2000/02/03 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/02/03 09:00 [entrez]
AID - 10.1073/pnas.97.3.1101 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2000 Feb 1;97(3):1101-6. doi: 10.1073/pnas.97.3.1101.