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Cited by 225Cellular transport and secretionFungal and yeast genetics researchProtein Kinase Regulation and GTPase Signaling

Exocytosis: The Many Masters of the Exocyst

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Lipschutz, Joshua H, Mostov, Keith E·2002·Current Biology
DOI 10.1016/s0960-9822(02)00753-4
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Abstract

The exocyst is a conserved eight-subunit complex involved in the docking of exocytic vesicles. The exocyst has now been identified as an effector for five small GTPases, including Sec4, Rho1, Rho3, Cdc42 and, most recently, RalA.

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Crossref · 10.1016/s0960-9822(02)00753-4

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  • Regulatory interactions of exocyst proteins with several small GTPases, including RalA and RalB, have been identified.

    “have identified regulatory interactions of exocyst proteins with several small GTPases (Lipschutz and Mostov, 2002;Wu et al, 2008), including the two mammalian Ral isoforms, RalA and RalB.”

    From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Lipschutz and Mostov, 2002

    The indexed text (labeled Abstract; page unavailable) describes exocyst interactions with several small GTPases and explicitly identifies RalA. It does not identify RalB as an interacting isoform, so that part of the claim is not supported by this paper. (LLM, conf=0.88)

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Research works printed but not linked: 19

  1. [1]1. Terbush, D.R. ∙ Maurice, T. ∙ Roth, D. ... The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae EMBO J. 1996; 15:6483-6494 Crossref Scopus (702) PubMed Google Scholar
  2. [2]2. Grindstaff, K.K. ∙ Yeaman, C. ∙ Anandasabapathy, N. ... Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells Cell. 1998; 93:731-740 Full Text Full Text (PDF) Scopus (454) PubMed Google Scholar
  3. [3]3. Hsu, S. ∙ Ting, A.E. ∙ Hazuka, C.D. ... The mammalian brain rsec6/8 complex Neuron. 1996; 17:1209-1219 Full Text Full Text (PDF) Scopus (231) PubMed Google Scholar
  4. [4]4. Finger, F.P. ∙ Hughes, T.E. ∙ Novick, P. Sec3p is a spatial landmark for polarized secretion in budding yeast Cell. 1998; 92:559-571 Full Text Full Text (PDF) Scopus (319) PubMed Google Scholar
  5. [5]5. Guo, W. ∙ Roth, D. ∙ Walch-Solimena, C. ... The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis EMBO J. 1999; 18:1071-1080 Crossref Scopus (513) PubMed Google Scholar
  6. [6]6. Guo, W. ∙ Tamanoi, F. ∙ Novick, P. Spatial regulation of the exocyst complex by Rho1 GTPase Nat. Cell Biol. 2001; 3:353-360 Crossref Scopus (257) PubMed Google Scholar
  7. [7]7. Zhang, X. ∙ Bi, E. ∙ Novick, P. ... Cdc42 Interacts with the Exocyst and Regulates Polarized Exocytosis J. Biol. Chem. 2001; 276:46745-46750 Full Text Full Text (PDF) Scopus (252) PubMed Google Scholar
  8. [8]8. Adamo, J.E. ∙ Rossi, G. ∙ Brennwald, P. The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity Mol. Biol. Cell. 1999; 10:4121-4133 Crossref Scopus (177) PubMed Google Scholar
  9. [9]9. Robinson, N.G. ∙ Guo, L. ∙ Imai, J. ... Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70 Mol. Cell. Biol. 1999; 19:3580-3587 Crossref PubMed Google Scholar
  10. [10]10. Brymora, A. ∙ Valova, V.A. ∙ Larsen, M.R. ... The brain exocyst complex interacts with RalA in a GTP-dependent manner: Identification of a novel mammalian Sec3 gene and a second Sec15 gene J. Biol. Chem. 2001; 13:13 Google Scholar
  11. [11]11. Sugihara, K. ∙ Asano, S. ∙ Tanaka, K. ... The exocyst complex binds the small GTPase RalA to mediate filopodia formation Nat. Cell Biol. 2002; 4:73-78 Crossref Scopus (205) PubMed Google Scholar
  12. [12]12. Moskalenko, S. ∙ Henry, D.O. ∙ Rosse, C. ... The exocyst is a Ral effector complex Nat. Cell Biol. 2002; 4:66-72 Crossref Scopus (358) PubMed Google Scholar
  13. [13]13. Polzin, A. ∙ Shipitsin, M. ∙ Goi, T. ... Ral-GTPase influences the regulation of the readily-releasible pool of synaptic vesicles Mol. Biol. Cell. 2002; 22:1714-1722 Crossref Scopus (67) Google Scholar
  14. [14]14. Hazuka, C.D. ∙ Foletti, D.L. ∙ Hsu, S.C. ... The sec6/8 complex is located at neurite outgrowth and axonal synapse-assembly domains J. Neurosci. 1999; 19:1324-1334 Crossref PubMed Google Scholar
  15. [15]15. Yeaman, C. ∙ Grindstaff, K.K. ∙ Wright, J.R. ... Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells J. Cell Biol. 2001; 155:593-604 Crossref Scopus (143) PubMed Google Scholar
  16. [16]16. Pollack, A.L. ∙ Runyan, R.B. ∙ Mostov, K.E. Morphogenetic mechanisms of epithelial tubulogenesis: MDCK cell polarity is transiently rearranged without loss of cell-cell contact during scatter factor/hepatocyte growth factor-induced tubulogenesis Dev. Biol. 1998; 204:64-79 Crossref Scopus (197) PubMed Google Scholar
  17. [17]17. O'Brien, L.E. ∙ Jou, T.S. ∙ Pollack, A.L. ... Rac1 orientates epithelial apical polarity through effects on basolateral laminin assembly Nat. Cell Biol. 2001; 3:831-838 Crossref Scopus (388) PubMed Google Scholar
  18. [18]18. Lipschutz, J.H. ∙ Guo, W. ∙ O'Brien, L.E. ... Exocyst is involved in cystogenesis and tubulogenesis and acts by modulating synthesis and delivery of basolateral plasma membrane and secretory proteins Mol. Biol. Cell. 2000; 11:4259-4275 Crossref Scopus (124) PubMed Google Scholar
  19. [19]19. Charron, A.J. ∙ Nakamura, S. ∙ Bacallao, R. ... Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease J. Cell Biol. 2000; 149:111-124 Crossref Scopus (111) PubMed Google Scholar

Cited by

Sorted by citations

Authors
Lipschutz, J. H., & Mostov, K. E.
Affiliations
  • University of Pennsylvania (US)
  • University of California, San Francisco (US)
Corresponding author
Lipschutz, Joshua H
ORCID
Venue
Current Biology
Publisher
Elsevier BV
Published
2002-03
Volume
12
Issue
6
Pages
R212-R214
ISSN
0960-9822 (ISSN-L)
DOI
10.1016/s0960-9822(02)00753-4
OpenAlex
W2043466785
Cited by
225
References
0
Citations by year
2025: 1 · 2024: 3 · 2023: 2 · 2022: 3 · 2021: 6 · 2020: 3 · 2019: 6 · 2018: 4 · 2017: 8 · 2016: 3 · 2015: 7 · 2014: 6 · 2013: 7 · 2012: 12
FWCI
7.79
Type
journal article
Language
en
Open access
Licence
Locations
  • Current Biology (publishedVersion)
  • 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 › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
exocyst, exocytosis, small GTPases, Sec4, Rho1, Rho3, Cdc42, RalA, vesicle trafficking
MeSH terms
Animals, Exocytosis, Fungal Proteins, Humans, Mammals, Yeasts, GTP Phosphohydrolases, rab GTP-Binding Proteins, ral GTP-Binding Proteins, rho GTP-Binding Proteins, cdc42 GTP-Binding Protein, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins

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