Cited by 258Protein Kinase Regulation and GTPase SignalingCellular transport and secretionProtein Tyrosine Phosphatases

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The ral gene: a new ras related gene isolated by the use of a synthetic probe.

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Chardin, P., Tavitian, A.·1986·The EMBO Journal

Abstract

We synthesized a set of 20-mer oligonucleotides corresponding to a sequence of seven amino acids strictly conserved in all the different ras proteins, from yeast to man, as well as in rho and YPT, two proteins distantly related to p21 ras (approximately 30% amino acid homology). This oligonucleotide probe was used to search for new members of the ras family. We describe here a new ras related gene named ral, isolated from a cDNA library of immortalized simian B-lymphocytes. The ral gene codes for a 206 amino acid protein of expected mol. wt 23.5 kd that shares greater than 50% homology with H-ras, K-ras or N-ras. The GTP binding regions of p21 ras and a C-terminal cysteine involved in membrane anchoring are also present in ral; this strongly suggests that ral is a GTP binding protein with membrane localization. Furthermore, several external regions of p21 ras presumably involved in the interaction with effector, receptor and/or regulatory proteins are highly homologous to the corresponding regions in ral. Therefore some of the proteins that interact with ral might be identical or closely related to those interacting with p21 ras.

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Crossref · 10.1002/j.1460-2075.1986.tb04485.x

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  • RalA regulates vesicle tethering and fusion through interacting with exocyst.

    “Ralbp1 binds to RalA, a small GTPase regulating vesicle tethering and fusion through interacting with exocyst (11, 20, 41–44).”

    From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [41]

    The Discussion describes ral as a ras-related protein and says its conserved GTP-binding regions strongly suggest it binds GTP. It does not identify an exocyst interaction or a role in vesicle tethering and fusion; instead, it says ral’s precise interacting proteins remained to be characterized. The cited paper therefore supports only the small-GTPase characterization, and even that was an inference rather than a demonstrated result. (LLM, conf=0.87)

    Experimental — accuracy not yet measured
  • Ralbp1 binds to RalA.

    “Ralbp1 binds to RalA, a small GTPase regulating vesicle tethering and fusion through interacting with exocyst (11, 20, 41–44).”

    From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [41]

    The Discussion suggests that Ral may interact with other proteins but says its precise interacting proteins remain to be characterized. A search of our copy for Ralbp1, RLIP76, and binding to RalA found no passage identifying Ralbp1 or establishing the claimed interaction. (LLM, conf=0.76)

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Citations

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Research works printed but not linked: 7

  1. Der,C.J., Pan,B.T. and Cooper,G.M. (1986) Mol. Cell. Biol., in press.
  2. Feig,L.A., Pan,B.T., Roberts,T.M. and Cooper,G.M. (1986) Proc. Natl. Acad. Sci. USA, in press.
  3. Huynh,T., Young,R. and Davis,R. (1985) In Glover,D. (ed.), DNA Cloning: A Practical Approach. IRL Press, Oxford, vol. 1, pp. 49-78.
  4. Maniatis,T., Fritsch,E.F. and Sambrook,J. (1982) Molecular Cloning: A Lab- oratory Manual. Cold Spring Harbor Laboratory Press, NY.
  5. Robishaw,J.D., Russell,D.W., Harris,B.A., Smigel,M.D. and Gilman,A.G. (1986) Proc. Natl. Acad. Sci. USA, 83, 1251-1255.
  6. Sanger,F., Nicklen,S. and Coulson,A.R. (1977) Proc. Natl. Acad. Sci. USA, 74, 5463-5467.
  7. Sigal,I.S., Gibbs,J.B., D'Alonzo,J.S. and Scolnick,E.M. (1986) Proc. Natl. Acad. Sci. USA, 13, 4725 -4729.

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Metadata

Authors
Chardin, P., & Tavitian, A.
Venue
The EMBO Journal
Published
1986-09-01
Volume
5
Issue
9
Pages
2203-2208
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
OpenAlex
W35071699
Cited by
258
References
0
Citations by year
2026: 2 · 2025: 1 · 2023: 3 · 2022: 2 · 2021: 2 · 2020: 5 · 2019: 3 · 2018: 2 · 2017: 3 · 2016: 5 · 2015: 3 · 2014: 7 · 2013: 4 · 2012: 1
FWCI
9.50
Type
journal article
Language
en
Open access
Locations
  • The EMBO Journal (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
Ras-related proteins, p21ras, G proteins, synthetic oligonucleotide probes, H-Ras, KRAS, NRAS, B cells, protein homology
MeSH terms
Amino Acid Sequence, Animals, B-Lymphocytes, Base Sequence, Cell Line, DNA, DNA Restriction Enzymes, Fungal Proteins, Genes, Synthetic, Humans, Nucleic Acid Hybridization, Oligodeoxyribonucleotides, Oncogenes, ras Proteins

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