ArticleThe Biochemical journal2000
Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 78 citations in OpenAlex.
- Functional ADAM12 variants modulate proteolytic activity and influence metabolic traits.Scientific reports · 2026Article
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- ADAM12 abrogation alters immune cell infiltration and improves response to checkpoint blockade therapy in the T11 murine model of triple-negative breast cancer.Oncoimmunology · 2023Article
- A Disintegrin and Metalloproteinase (ADAM) Family: Their Significance in Malignant Tumors of the Central Nervous System (CNS).International journal of molecular sciences · 2021Review
- Multi-organ metastasis as destination for breast cancer cells guided by biomechanical architecture.American journal of cancer research · 2021Article
- Aspartate β-hydroxylase promotes pancreatic ductal adenocarcinoma metastasis through activation of SRC signaling pathway.Journal of hematology & oncology · 2019Article
- Preferred SH3 domain partners of ADAM metalloproteases include shared and ADAM-specific SH3 interactions.PloS one · 2015Article
- Identification of SH3 domain proteins interacting with the cytoplasmic tail of the a disintegrin and metalloprotease 10 (ADAM10).PloS one · 2014Article
- ADAM and ADAMTS family proteins and their role in the colorectal cancer etiopathogenesis.BMB reports · 2013Review
- Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1.The Journal of biological chemistry · 2012Article
- ADAM15 protein amplifies focal adhesion kinase phosphorylation under genotoxic stress conditions.The Journal of biological chemistry · 2012Article
- Suppression of ADAM17-mediated Lyn/Akt pathways induces apoptosis of human leukemia U937 cells: Bungarus multicinctus protease inhibitor-like protein-1 uncovers the cytotoxic mechanism.The Journal of biological chemistry · 2010Article
- The formin-homology protein SmDia interacts with the Src kinase SmTK and the GTPase SmRho1 in the gonads of Schistosoma mansoni.PloS one · 2009Article
- ADAM8: a new therapeutic target for asthma.Expert opinion on therapeutic targets · 2009Review
- The ADAM metalloproteinases.Molecular aspects of medicine · 2008Review
- Stem cell antigen-1 localizes to lipid microdomains and associates with insulin degrading enzyme in skeletal myoblasts.Journal of cellular physiology · 2008Article
- Breast cancer-associated mutations in metalloprotease disintegrin ADAM12 interfere with the intracellular trafficking and processing of the protein.International journal of cancer · 2008Article
- 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
- Syndecans in tumor cell adhesion and signaling.Reproductive biology and endocrinology : RB&E · 2004Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ADAM 12, a member of the ADAM (protein containing a disintegrin and metalloprotease) family of metalloprotease-disintegrins, has been implicated in the differentiation and fusion of skeletal myoblasts, and its expression is dramatically up-regulated in many cancer cells. While the extracellular portion of ADAM 12 contains an active metalloprotease and a cell-adhesion domain, the function of the cytoplasmic portion is much less clear. In this paper, we show that the cytoplasmic tail of ADAM 12 mediates interactions with the non-receptor protein tyrosine kinase Src. The interaction is direct, specific, and involves the N-terminal proline-rich region in the cytoplasmic tail of ADAM 12 and the Src homology 3 (SH3) domain of Src. ADAM 12 and Src co-immunoprecipitate from transfected C2C12 cells, suggesting that the two proteins form a complex in vivo. Co-expression of Src and ADAM 12, but not ADAM 9, in C2C12 cells results in activation of the recombinant Src. Moreover, endogenous ADAM 12 associates with and activates endogenous Src in differentiating C2C12 cells. These results indicate that ADAM 12 may mediate adhesion-induced signalling during myoblast differentiation.
Indexed as
Identifiers
11104699PMC1221530W2002405097What OpenQuestion holds
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.