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Ral and Rab3a are major GTP-binding proteins of axonal rapid transport and synaptic vesicles and do not redistribute following depolarization stimulated synaptosomal exocytosis.
Department of Biochemistry, Boston University School of Medicine, MA 02118.
We have employed high-resolution SDS polyacrylamide gels to demonstrate that there are two major low-molecular-weight GTP-binding proteins associated with axonal membranes including synaptic vesicles, rapid transported membranes and clathrin-coated vesicles. We demonstrate that one of the major proteins is Ral and that the other is Rab3A. Following the depolarization of synaptosomes resulting in increased neurotransmitter release, we see no significant dissociation of either Ral or Rab3a from synaptic vesicle derived membranes in contrast to results reported previously.
PMID: 8373799 [PubMed - indexed for MEDLINE]
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Cited by 11 PubMed Central articles
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RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity.
Frankel P, Aronheim A, Kavanagh E, Balda MS, Matter K, Bunney TD, Marshall CJ.
EMBO J. 2005 Jan 12; 24(1):54-62. Epub 2004 Dec 9.
[EMBO J. 2005]
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Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p.
Boyd C, Hughes T, Pypaert M, Novick P.
J Cell Biol. 2004 Dec 6; 167(5):889-901.
[J Cell Biol. 2004]
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RalA but not RalB enhances polarized delivery of membrane proteins to the basolateral surface of epithelial cells.
Shipitsin M, Feig LA.
Mol Cell Biol. 2004 Jul; 24(13):5746-56.
[Mol Cell Biol. 2004]
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