The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
The Adaptor Protein Fish Associates with Members of the ADAMs Family and Localizes to Podosomes of Src-transformed Cells
Open accessAbstract
Fish is a scaffolding protein and Src substrate. It contains an amino-terminal Phox homology (PX) domain and five Src homology 3 (SH3) domains, as well as multiple motifs for binding both SH2 and SH3 domain-containing proteins. We have determined that the PX domain of Fish binds 3-phosphorylated phosphatidylinositols (including phosphatidylinositol 3-phosphate and phosphatidylinositol 3,4-bisphosphate). Consistent with this, a fusion protein of green fluorescent protein and the Fish PX domain localized to punctate structures similar to endosomes in normal fibroblasts. However, the full-length Fish protein was largely cytoplasmic, suggesting that its PX domain may not be able to make intermolecular interactions in unstimulated cells. In Src-transformed cells, we observed a dramatic re-localization of some Fish molecules to actin-rich structures called podosomes; the PX domain was both necessary and sufficient to effect this translocation. We used a phage display screen with the fifth SH3 domain of Fish and isolated ADAM19 as a binding partner. Subsequent analyses in mammalian cells demonstrated that Fish interacts with several members of the ADAMs family, including ADAMs 12, 15, and 19. In Src-transformed cells, ADAM12 co-localized with Fish in podosomes. Because members of the ADAMs family have been implicated in growth factor processing, as well as cell adhesion and motility, Fish could be acting as an adaptor molecule that allows Src to impinge on these processes.
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Cites
The ADAMs family of metalloproteases: multidomain proteins with multiple functions
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Self-citationLocalization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
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The PX domains of p47phox and p40phox bind to lipid products of PI(3)K
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ADAMs: focus on the protease domain
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Cited by
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The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
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Twist1-Induced Invadopodia Formation Promotes Tumor Metastasis
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The ADAMs: signalling scissors in the tumour microenvironment
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Invadopodia: Specialized Cell Structures for Cancer Invasion
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Metadata
- Authors
- Abram, C. L., Seals, D. F., Pass, I., Salinsky, D., Maurer, L., Roth, T. M., & Courtneidge, S. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 278
- Issue
- 19
- Pages
- 16844-16851
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2064750103
- Cited by
- 262
- References
- 46
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Abram, C. L., Seals, D. F., Pass, I., Salinsky, D., Maurer, L., Roth, T. M., & Courtneidge, S. A. (2003). The Adaptor Protein Fish Associates with Members of the ADAMs Family and Localizes to Podosomes of Src-transformed Cells. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m300267200
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