The Major Vault Protein Is a Novel Substrate for the Tyrosine Phosphatase SHP-2 and Scaffold Protein in Epidermal Growth Factor Signaling
Open accessAbstract
The catalytic activity of the Src homology 2 (SH2) domain-containing tyrosine phosphatase, SHP-2, is required for virtually all of its signaling effects. Elucidating the molecular mechanisms of SHP-2 signaling, therefore, rests upon the identification of its target substrates. In this report, we have used SHP-2 substrate-trapping mutants to identify the major vault protein (MVP) as a putative SHP-2 substrate. MVP is the predominant component of vaults that are cytoplasmic ribonucleoprotein complexes of unknown function. We show that MVP is dephosphorylated by SHP-2 in vitro and it forms an enzyme-substrate complex with SHP-2 in vivo. In response to epidermal growth factor (EGF), SHP-2 associates via its SH2 domains with tyrosyl-phosphorylated MVP. MVP also interacts with the activated form of the extracellular-regulated kinases (Erks) in response to EGF and a constitutive complex between tyrosyl-phosphorylated MVP, SHP-2, and the Erks was detected in MCF-7 breast cancer cells. Using MVP-deficient fibroblasts, we demonstrate that MVP cooperates with Ras for optimal EGF-induced Elk-1 activation and is required for cell survival. We propose that MVP functions as a novel scaffold protein for both SHP-2 and Erk. The regulation of MVP tyrosyl phosphorylation by SHP-2 may play an important role in cell survival signaling.
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- Authors
- Kolli, S., Zito, C. I., Mossink, M. H., Wiemer, E. A. C., & Bennett, A. M.
- Affiliations
- Yale University (US)
- Erasmus MC (NL)
- Corresponding author
- Bennett, Anton M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-07
- Volume
- 279
- Issue
- 28
- Pages
- 29374-29385
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2003678246
- Cited by
- 154
- References
- 60
- Citations by year
- 2025: 7 · 2024: 11 · 2023: 6 · 2022: 5 · 2021: 8 · 2020: 5 · 2019: 7 · 2018: 6 · 2017: 8 · 2016: 3 · 2015: 4 · 2014: 6 · 2013: 11 · 2012: 10
- FWCI
- 2.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- Funders
- National Cancer Institute (T32CA009085)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR046504)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Keywords
- major vault protein, SHP2, protein tyrosine phosphatase, EGF signaling, substrate trapping, tyrosine phosphorylation, scaffold proteins, ERK, Elk-1, Ras, cell survival signaling, vaults, ribonucleoprotein complexes, MCF-7 cells
- MeSH terms
- Major Vault Protein, Amino Acid Sequence, Animals, Cell Survival, Cells, Cultured, DNA-Binding Proteins, Enzyme Activation, Epidermal Growth Factor, Fibroblasts, Humans, Molecular Sequence Data, Phosphorylation, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Transcription Factors, Signal Transduction, Culture Media, Serum-Free, Protein Tyrosine Phosphatases, Protein Structure, Tertiary, Vault Ribonucleoprotein Particles, Mitogen-Activated Protein Kinases, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, ets-Domain Protein Elk-1, Mice, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases
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