ArticleOncogene2000
Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src.
Article in Oncogene, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 60 citations in OpenAlex.
- Elevation of ADAM12 facilitates tumor progression by enhancing metastasis and immune infiltration in gastric cancer.International journal of oncology · 2022Article
- Proteomic screening identifies the zonula occludens protein ZO-1 as a new partner for ADAM12 in invadopodia-like structures.Oncotarget · 2018Article
- Identification of SH3 domain proteins interacting with the cytoplasmic tail of the a disintegrin and metalloprotease 10 (ADAM10).PloS one · 2014Article
- Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1.The Journal of biological chemistry · 2012Article
- Identification of ILK as a new partner of the ADAM12 disintegrin and metalloprotease in cell adhesion and survival.Molecular biology of the cell · 2012Article
- Engagement of β-arrestin by transactivated insulin-like growth factor receptor is needed for V2 vasopressin receptor-stimulated ERK1/2 activation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The ADAM metalloproteinases.Molecular aspects of medicine · 2008Review
- RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis.The Journal of biological chemistry · 2008Article
- Grb2 signaling in cell motility and cancer.Expert opinion on therapeutic targets · 2008Review
- Anchoring junctions as drug targets: role in contraceptive development.Pharmacological reviews · 2008Review
- Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding.Molecular neurodegeneration · 2007Article
- Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome.EMBO reports · 2006Article
- Epigenetic silencing of the adhesion molecule ADAM23 is highly frequent in breast tumors.Oncogene · 2004Article
- Syndecans in tumor cell adhesion and signaling.Reproductive biology and endocrinology : RB&E · 2004Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Meltrin alpha/ADAM12 is a member of the ADAM/MDC family proteins characterized by the presence of metalloprotease and disintegrin domains. This protein also contains a single transmembrane domain and a relatively long cytoplasmic domain containing several proline-rich sequences. These sequences are compatible with the consensus sequences for binding the Src homology 3 (SH3) domains. To determine whether the proline-rich sequences interact with SH3 domains in several proteins, binding of recombinant SH3 domains to the meltrin alpha cytoplasmic domain was analysed by pull-down assays. The SH3 domains of Src and Yes bound strongly, but that of Abl or phosphatidylinositol 3-kinase p85 subunit did not. Full-length Grb2/Ash bound strongly, whereas its N-terminal SH3 domain alone did less strongly. Src and Grb2 in bovine brain extracts also bound to meltrin alpha cytoplasmic domain on affinity resin. Furthermore, immunoprecipitation with a monoclonal antibody to meltrin alpha resulted in coprecipitation of Src and Grb2 with meltrin alpha in cell extracts, suggesting that Src and Grb2 are associated in vivo with meltrin alpha cytoplasmic domain. This notion was also supported by the findings that exogenously expressed meltrin cytoplasmic domain coexisted with Src and Grb2 on the membrane ruffles. The C-terminal Tyr901 of meltrin alpha was phosphorylated both in vitro and in cultured cells by v-Src. These results may imply that meltrin alpha cytoplasmic domain is involved in a signal transduction for some biological function through the interaction with SH3-containing proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.