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Cited by 143Cellular transport and secretionProtein Kinase Regulation and GTPase SignalingExtracellular vesicles in disease

The Brain Exocyst Complex Interacts with RalA in a GTP-dependent Manner

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Brymora, Adam, Valova, Valentina A., Larsen, Martin R., Roufogalis, Basil D., Robinson, Phillip J.·2001·Journal of Biological Chemistry
DOI 10.1074/jbc.c100320200
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Abstract

Ral is a small GTPase involved in critical cellular signaling pathways. The two isoforms, RalA and RalB, are widely distributed in different tissues, with RalA being enriched in brain. The best characterized RalA signaling pathways involve RalBP1 and phospholipase D. To investigate RalA signaling in neuronal cells we searched for RalA-binding proteins in brain. We found at least eight proteins that bound RalA in a GTP-dependent manner. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) identified these as the components of the exocyst complex. The yeast exocyst is a regulator of polarized secretion, docking vesicles to regions of the plasma membrane involved in active exocytosis. We identified the human FLJ10893 protein as the mammalian homologue of the yeast exocyst protein Sec3p. The exocyst complex did not contain the previously identified exocyst component rSec15, but a new homologue of both yeast Sec15p and rSec15, called KIAA0919. Western blots confirmed that two rat exocyst proteins, rSec6 and rSec8, bound active RalA in nerve terminals, as did RalBP1. Phospholipase D bound RalA in a nucleotide-independent manner. This places the RalA signaling system in mammalian nerve terminals, where the exocyst may act as an effector for activated RalA in directing sites of exocytosis.

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  • The exocyst is required for neurite outgrowth and the addition of neuronal membrane proteins, including the insertion of glutamate receptors, and the maturation of photoreceptors.

    “It is required for neurite outgrowth and the addition of neuronal membrane proteins, including the insertion of glutamate receptors, and the maturation of photoreceptors (Brymora et al, 2001;Vega and Hsu, 2001;Murthy et al, 2003;Sans et al, 2003;Beronja et al, 2005;Liebl et al, 2005;Mehta et al, 2005;Gerges et al, 2006).”

    From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Brymora et al, 2001

    Our copy states that the exocyst is required for neurite outgrowth (passage [2], labeled Abstract; page unavailable). It does not address the addition of neuronal membrane proteins, glutamate-receptor insertion, or photoreceptor maturation; searches for those terms returned no supporting passages. (LLM, conf=0.88)

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  • Ca2+ entry is a consequence of excitatory transmission in the mammalian brain and mammalian neurons contain both Ral and the exocyst.

    “Ca 2 þ entry is a consequence of excitatory transmission in the mammalian brain and mammalian neurons contain both Ral and the exocyst”

    From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Brymora et al, 2001

    The Abstract reports that RalA is enriched in brain and that rat exocyst proteins bind active RalA in nerve terminals, supporting the statement that mammalian neurons contain both. It also says nerve-terminal exocytosis and endocytosis are Ca2+-dependent, but does not say that Ca2+ entry is a consequence of excitatory transmission in the mammalian brain. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

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Authors
Brymora, A., Valova, V. A., Larsen, M. R., Roufogalis, B. D., & Robinson, P. J.
Affiliations
  • The University of Sydney (AU)
  • Children's Medical Research Institute (AU)
  • Macquarie University (AU)
Corresponding author
Robinson, Phillip J.
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-08
Volume
276
Issue
32
Pages
29792-29797
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.c100320200
OpenAlex
W2068137415
Cited by
143
References
0
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2023: 3 · 2021: 2 · 2019: 7 · 2018: 1 · 2017: 4 · 2016: 5 · 2015: 4 · 2014: 6 · 2013: 4 · 2012: 7
FWCI
4.55
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
Keywords
RalA, exocyst complex, small GTPase signaling, RALBP1, phospholipase D, Sec6, Sec8, polarized secretion, exocytosis, presynaptic terminals
MeSH terms
Amino Acid Sequence, Animals, Brain, Cloning, Molecular, Cytosol, Exocytosis, Glutathione Transferase, Guanosine Triphosphate, Humans, Molecular Sequence Data, Neurons, Protein Binding, Recombinant Proteins, Sheep, Blotting, Western, Signal Transduction, Sequence Homology, Amino Acid, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, GTP-Binding Proteins, Protein Isoforms, GTP Phosphohydrolases, ral GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Rats

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