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Specific sorting of the a1 isoform of the V-H+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane
- Source :
- Journal of Cell Science, Journal of Cell Science, Company of Biologists, 2003, 116 (Pt 23), pp.4751-62. ⟨10.1242/jcs.00791⟩, Journal of Cell Science, 2003, 116 (Pt 23), pp.4751-62. ⟨10.1242/jcs.00791⟩
- Publication Year :
- 2003
- Publisher :
- HAL CCSD, 2003.
-
Abstract
- Vacuolar H+ATPase (V-ATPase) accumulates protons inside various intracellular organelles, generating the electrochemical proton gradient required for many vital cellular processes. V-ATPase is a complex enzyme with many subunits that are organized into two domains. The membrane domain that translocates protons contains a proteolipid oligomer of several c subunits and a 100 kDa a subunit. Several a-subunit isoforms have been described that are important for tissue specificity and targeting to different membrane compartments, and could also result in the generation of V-ATPases with different functional properties. In the present report, we have cloned the Torpedo marmorata a1 isoform. This isoform was found to be addressed specifically to nerve endings, whereas VATPases in the neuron cell bodies contain a different a-subunit isoform. In nerve terminals, the V-ATPase membrane domain is present not only in synaptic vesicles but also in the presynaptic plasma membrane, where its density could reach 200 molecules μm–2. This V-ATPase interacts with VAMP-2 and with the SNARE complexes involved in synaptic vesicle docking and exocytosis.
- Subjects :
- MESH: Vesicular Transport Proteins
MESH: Sequence Homology, Amino Acid
MESH: R-SNARE Proteins
Vesicular Transport Proteins
V-ATPase
MESH: Amino Acid Sequence
MESH: Protein Isoforms
Torpedo
R-SNARE Proteins
Protein Isoforms
MESH: Animals
Cloning, Molecular
Nerve Endings
0303 health sciences
030302 biochemistry & molecular biology
SNAP25
Cell biology
SNARE complex1
Protein Transport
MESH: Nerve Endings
MESH: Synaptosomes
[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]
MESH: Cryoelectron Microscopy
MESH: Membrane Proteins
SNARE Proteins
Subcellular Fractions
MESH: SNARE Proteins
Gene isoform
Vacuolar Proton-Translocating ATPases
MESH: Protein Transport
Vesicle fusion
Protein subunit
Molecular Sequence Data
MESH: Vacuolar Proton-Translocating ATPases
Biology
Synaptic vesicle
Exocytosis
03 medical and health sciences
Synaptic vesicle docking
Animals
MESH: Cloning, Molecular
Amino Acid Sequence
Electrochemical gradient
030304 developmental biology
MESH: Molecular Sequence Data
Sequence Homology, Amino Acid
Cell Membrane
Cryoelectron Microscopy
Membrane Proteins
Freeze-fracture
Cell Biology
Fusion pore
MESH: Subcellular Fractions
MESH: Torpedo
Synaptosomes
MESH: Cell Membrane
Subjects
Details
- Language :
- English
- ISSN :
- 00219533 and 14779137
- Database :
- OpenAIRE
- Journal :
- Journal of Cell Science, Journal of Cell Science, Company of Biologists, 2003, 116 (Pt 23), pp.4751-62. ⟨10.1242/jcs.00791⟩, Journal of Cell Science, 2003, 116 (Pt 23), pp.4751-62. ⟨10.1242/jcs.00791⟩
- Accession number :
- edsair.doi.dedup.....aa02be5436e35ff374b964c89b3de19b