Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral.
Open accessAbstract
Ral-binding protein 1 (RalBP1) is a putative effector protein of Ral and exhibits a GTPase activating activity for Rac and CDC42. To clarify the function of RalBP1, we isolated a novel protein that interacts with RalBP1 by yeast two-hybrid screening and designated it POB1 (partner of RalBP1). POB1 consists of 521 amino acids, shares a homology with Eps15, which has been identified as an epidermal growth factor (EGF) receptor substrate, and has two proline-rich motifs. The POB1 mRNA was expressed in cerebrum, cerebellum, lung, kidney, and testis. POB1 interacted with RalBP1 in COS cells and the C-terminal region of POB1 was responsible for this interaction. The binding domain of RalBP1 to POB1 was distinct from its binding domain to Ral. Ral and POB1 simultaneously interacted with RalBP1 in COS cells. The binding of POB1 to RalBP1 did not affect the GTPase activating activity of RalBP1. Furthermore, POB1 bound to Grb2 but not to Nck or Crk. POB1 was tyrosine-phosphorylated in COS cells upon stimulation with EGF and made a complex with EGF receptor. These results suggest that RalBP1 makes a complex with POB1 and that this complex may provide a link between tyrosine kinase, Src homology 3 (SH3)-containing protein, and Ral.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Yeast two-hybrid screens with PSD-95 identified RalBP1 as a novel PSD-95-interacting protein.
“Yeast two-hybrid screens with PSD-95 identified RalBP1 as a novel PSD-95-interacting protein, which is coupled to other endocytic proteins including POB1, RalA, AP2, epsin, and Eps15 (Figure 1A) [34],[36].”
From Regulated RalBP1 Binding to RalA and PSD-95 Controls AMPA Receptor Endocytosis and LTD (2009) · cites this paper as [34]
The Experimental Procedures describe a yeast two-hybrid screen using RalBP1, not PSD-95. The Isolation of RalBP1-interacting Protein section says the newly identified partner was POB1, not RalBP1. (LLM, conf=0.88)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredRalBP1 directly binds AP2 and POB1.
“RalBP1 directly binds AP2 and POB1 [34],[35]”
From Regulated RalBP1 Binding to RalA and PSD-95 Controls AMPA Receptor Endocytosis and LTD (2009) · cites this paper as [34]
The in-vitro interaction passage (page not provided) explicitly concludes that POB1 binds RalBP1 directly. The cited sentence also attributes direct AP2 binding to the paired citations, but the passages from this paper do not establish that part. (LLM, conf=0.88)
Experimental — accuracy not yet measuredRalBP1 directly interacts with EH domain proteins POB1 and Reps1.
“Endocytosis occurs when active RalA associates with RalBP1/RLIP76 [31],[32], an endocytic adaptor that directly interacts with the μ2 subunit of the endocytic AP2 complex [33] and EH domain proteins POB1 and Reps1 [34],[35].”
From Regulated RalBP1 Binding to RalA and PSD-95 Controls AMPA Receptor Endocytosis and LTD (2009) · cites this paper as [34]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.
Hofer, F., Fields, S., Schneider, C., & Martin, G. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11089 · Cited by 287 · see citing works
Flagged first, then by citations
Research works printed but not linked: 8
- Hofer, F., Fields, S., Schneider, C., and Martin, G. S. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 11089 -11093
- Spaargaren, M., and Bischoff, J. R. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 12609 -12613
- Alexandropoulos, K., Cheng, G., and Baltimore, D. (1995) Proc. Natl. Acad. Sci.
- Sparks, A. B., Rider, J. E., Hoffman, N. G., Fowlkes, D. M., Quilliam, L. A., and Kay, B. K. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 1540 -1544
- Berger, B., Wilson, D. B., Wolf, E., Tonchev, T., Milla, M., and Kim, P. S. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 8259 -8263
- Pearson, R. B., and Kemp, B. E. (1991) Methods Enzymol. 200, 62-81
- Kishida, S., Koyama, S., Matsubara, K., Kishida, M., Matsuura, Y., and Kikuchi, A. (1997) Oncogene 15, in press
- Wong, W. T., Schumacher, C., Salcini, A. E., Romano, A., Castagnino, P., Pelicci, P. G., and Di Fiore, P. P. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 9530 -9534
Cited by
Sorted by citations
M-Sec promotes membrane nanotube formation by interacting with Ral and the exocyst complex
Hase, K., Kimura, S., Takatsu, H., Ohmae, M., Kawano, S., Kitamura, H., Ito, M., Watarai, H., Hazelett, C. C., Yeaman, C., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1990 · Cited by 402 · see citing works
Wiring through tunneling nanotubes--from electrical signals to organelle transfer
Abounit, S., & Zurzolo, C. (2012) · Journal of Cell Science · doi:10.1242/jcs.083279 · Cited by 386 · see citing works
Regulated RalBP1 Binding to RalA and PSD-95 Controls AMPA Receptor Endocytosis and LTD
Han, K., Kim, M.-H., Seeburg, D., Seo, J., Verpelli, C., Han, S., Chung, H. S., Ko, J., Lee, H. W., Kim, K., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000187 · Cited by 71 · see citing works
Ral signaling pathway in health and cancer
Moghadam, A. R., Patrad, E., Tafsiri, E., Peng, W., Fangman, B., Pluard, T. J., Accurso, A., Salacz, M., Shah, K., Ricke, B., et al. (2017) · Cancer Medicine · doi:10.1002/cam4.1105 · Cited by 58 · see citing works
Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module
Wang, S., Chen, X., Crisman, L., Dou, X., Winborn, C. S., Wan, C., Puscher, H., Yin, Q., Kennedy, M. J., & Shen, J. (2023) · Science Advances · doi:10.1126/sciadv.ade2540 · Cited by 14 · see citing works
- Authors
- Ikeda, M., Ishida, O., Hinoi, T., Kishida, S., & Kikuchi, A.
- Affiliations
- Hiroshima University (JP)
- Corresponding author
- Kikuchi, Akira
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-01
- Volume
- 273
- Issue
- 2
- Pages
- 814-821
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2085350573
- Cited by
- 146
- References
- 1
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 8 · 2020: 2 · 2019: 4 · 2018: 1 · 2017: 4 · 2016: 3 · 2015: 6 · 2014: 2 · 2013: 5 · 2012: 10
- FWCI
- 2.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Kato Memorial Bioscience Foundation
- 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
- RALBP1, protein-protein interaction, proline-rich motif, Grb2, EGF receptor, tyrosine phosphorylation, SH3 domain, Ral GTPase, Cdc42, Rac
- MeSH terms
- Amino Acid Sequence, Animals, Calcium-Binding Proteins, Carrier Proteins, Fungal Proteins, Molecular Sequence Data, Phosphoproteins, Protein Binding, Proteins, Recombinant Proteins, Sequence Homology, Amino Acid, src Homology Domains, GTP-Binding Proteins, COS Cells, ral GTP-Binding Proteins, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, ErbB Receptors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
