An Eps Homology (EH) Domain Protein That Binds to the Ral-GTPase Target, RalBP1
Open accessAbstract
Ral proteins constitute a family of small GTPases that can be activated by Ras in cells. In the GTP-bound state, Ral proteins bind to RalBP1, a GTPase-activating protein for CDC42 and Rac GTPases. We have used the two-hybrid system in yeast to clone a cDNA for a novel approximately 85-kDa protein that can bind to an additional site on RalBP1. This newly identified protein contains an Eps homology (EH) domain, which was first detected in the epidermal growth factor (EGF) receptor substrate Eps15. Recently, the EH domain of Eps15 has been shown to bind to proteins containing an asparagine-proline-phenylalanine motif. Moreover, EH domains have been found in proteins involved in endocytosis and/or actin cytoskeleton regulation. The RalBP1 associated Eps-homology domain protein, Reps1, is tyrosine-phosphorylated in response to EGF stimulation of cells. In addition, Reps1 has the capacity to form a complex with the SH3 domains of the adapter proteins Crk and Grb2, which may link Reps1 to an EGF-responsive tyrosine kinase. Thus, Reps1 may coordinate the cellular actions of activated EGF receptors and Ral-GTPases.
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Ralbp1 and Reps1 are involved in the same biological pathway.
“Ralbp1 was also identified as a significant hit in our CRISPR screen (Fig. 1D) and is an interacting factor of Reps1 (Figs. 3B and 5B) (35), suggesting that Ralbp1 and Reps1 are involved in the same biological pathway.”
From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [35]
Ralbp1 is an interacting factor of Reps1.
“Ralbp1 was also identified as a significant hit in our CRISPR screen (Fig. 1D) and is an interacting factor of Reps1 (Figs. 3B and 5B) (35), suggesting that Ralbp1 and Reps1 are involved in the same biological pathway.”
From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [35]
Ralbp1 was identified as a significant hit in the CRISPR screen.
“Ralbp1 was also identified as a significant hit in our CRISPR screen (Fig. 1D) and is an interacting factor of Reps1 (Figs. 3B and 5B) (35), suggesting that Ralbp1 and Reps1 are involved in the same biological pathway.”
From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [35]
RalBP1 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 [35]
RalBP1 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 [35]
The binding experiments in “Cloning of Reps1 cDNA” report that RalBP1 binds Reps1, not POB1 or AP2. A search of our copy for POB1 and AP2 found no passage establishing direct binding to either protein; the Discussion mentions an adaptin association with Eps15 instead. No page numbers were available for these passages. (LLM, conf=0.74)
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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
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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
- Yamaguchi, A., Urano, T., Goi, T., & Feig, L. A.
- Affiliations
- Tufts University (US)
- Corresponding author
- Feig, Larry A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-12
- Volume
- 272
- Issue
- 50
- Pages
- 31230-31234
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2026403140
- Cited by
- 126
- References
- 1
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 2 · 2021: 6 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 9
- FWCI
- 2.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service
- National Institute of General Medical Sciences (GM47707)
- 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, Ral GTPase, protein-protein interaction, EGF receptor signaling, tyrosine phosphorylation, SH3 domain binding, Crk, Grb2, Cdc42, Rac, GTPase-activating protein, endocytosis, actin cytoskeleton regulation
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Calcium-Binding Proteins, Carrier Proteins, Cell Line, Cloning, Molecular, Epidermal Growth Factor, Fungal Proteins, Molecular Sequence Data, Phosphorylation, Tyrosine, DNA, Complementary, src Homology Domains, COS Cells, GTPase-Activating Proteins, Mice
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