ArticleThe Biochemical journal2001
Metalloprotease-disintegrin ADAM 12 interacts with alpha-actinin-1.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- 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
- Translocation of the cytoplasmic domain of ADAM13 to the nucleus is essential for Calpain8-a expression and cranial neural crest cell migration.Developmental cell · 2011Article
- Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer.Oncogene · 2010Article
- The ADAM metalloproteinases.Molecular aspects of medicine · 2008Review
- Breast cancer-associated mutations in metalloprotease disintegrin ADAM12 interfere with the intracellular trafficking and processing of the protein.International journal of cancer · 2008Article
- ADAM12 and alpha9beta1 integrin are instrumental in human myogenic cell differentiation.Molecular biology of the cell · 2005Article
- ADAM 33 and its association with airway remodeling and hyperresponsiveness in asthma.Clinical reviews in allergy & immunology · 2004Review
- Syndecans in tumor cell adhesion and signaling.Reproductive biology and endocrinology : RB&E · 2004Review
- Role of metalloprotease disintegrin ADAM12 in determination of quiescent reserve cells during myogenic differentiation in vitro.Molecular and cellular biology · 2003Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ADAM 12, a member of the ADAM family of proteins (containing A Disintegrin And Metalloprotease domain), has been implicated in differentiation and fusion of myoblasts. While the extracellular domain of ADAM 12 contains an active metalloprotease and a region involved in cell adhesion, the function of the cytoplasmic tail of ADAM 12 has been less clear. Here we show that the cytoplasmic domain of ADAM 12 interacts in vitro and in vivo with alpha-actinin-1, an actin-binding and cross-linking protein. Green fluorescent protein fused to ADAM 12 cytoplasmic domain co-localizes with alpha-actinin-1-containing actin stress fibres in C2C12 cells. The interaction between ADAM 12 and alpha-actinin-1 is direct and involves the 58-amino acid C-terminal fragment of ADAM 12 and the 27 kDa N-terminal domain of alpha-actinin-1. Consistently, expression of the 27 kDa fragment of alpha-actinin-1 in C2C12 cells using a mitochondrial targeting system results in recruitment of the co-expressed ADAM 12 cytoplasmic domain to the mitochondrial surface. Moreover, alpha-actinin-1 co-purifies with a transmembrane, His6-tagged form of ADAM 12 expressed in C2C12 myoblasts, indicating that the transmembrane ADAM 12 forms a complex with alpha-actinin-1 in vivo. These results indicate that the actin cytoskeleton may play a critical role in ADAM 12-mediated cell-cell adhesion or cell signalling during myoblast differentiation and fusion.
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