ArticleThe international journal of biochemistry & cell biology2013
The carboxyl tail of alpha-actinin-4 regulates its susceptibility to m-calpain and thus functions in cell migration and spreading.
Article in The international journal of biochemistry & cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Review
- The Importance of Alpha-Actinin Proteins in Platelet Formation and Function, and Their Causative Role in Congenital Macrothrombocytopenia.International journal of molecular sciences · 2021Review
- Article
- oxLDL promotes podocyte migration by regulating CXCL16, ADAM10 and ACTN4.Molecular medicine reports · 2020Article
- ACTN4 regulates the stability of RIPK1 in melanoma.Oncogene · 2018Article
- Tyro3-mediated phosphorylation of ACTN4 at tyrosines is FAK-dependent and decreases susceptibility to cleavage by m-Calpain.The international journal of biochemistry & cell biology · 2018Article
- Comparative iTRAQ proteomics revealed proteins associated with horn development in yak.Proteome science · 2018Article
- The fifth sense: Mechanosensory regulation of alpha-actinin-4 and its relevance for cancer metastasis.Seminars in cell & developmental biology · 2017Review
- Tandem phosphorylation within an intrinsically disordered region regulates ACTN4 function.Science signaling · 2015Article
- ACTN4 and the pathways associated with cell motility and adhesion contribute to the process of lung cancer metastasis to the brain.BMC cancer · 2015Article
- α-Actinin-4 is required for amoeboid-type invasiveness of melanoma cells.The Journal of biological chemistry · 2014Article
- Activation of the TRPV1 cation channel contributes to stress-induced astrocyte migration.Glia · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Alpha-actinin-4 links the cytoskeleton to sites of adhesion and has been shown to be modulated to enable cell migration. Such focal adhesions must be labile to accomplish migration, with this detachment occurring at least in part via m-calpain activation (Glading et al., 2001, 2002; Xie et al., 1998). In this study, we report that alpha-actinin-4 is initially cleaved by m-calpain between tyrosine 13 and glycine. Removal of the first 13 amino acids does not affect alpha-actinin-4 binding to actin filaments and its localization within fibroblasts but drives cell migration with less persistence. Binding of phosphoinositides PI(4,5)P2, PI(3,4,5)P3 and PI(3,4)P2 to alpha-actinin-4, as well as binding of alpha-actinin-4 to actin filaments all inhibit m-calpain cleavage of ACTN4 between tyrosine 13 and glycine 14. Interestingly, the carboxyl terminus of alpha-actinin-4 including its calcium binding motifs, is inhibitory for a secondary cleavage of alpha-actinin-4 between lysine 283 and valine 284. The minimal length of inhibitory domain is mapped to the last 11 amino acids of alpha-actinin-4. The C-terminal tail of alpha-actinin-4 is essential for maintaining its normal actin binding activity and localization within cytoplasm and also its colocalization with actin in the lamellipodia of locomoting fibroblasts. Live cell imaging reveals that the 1-890 fragment fails to rescue neither the basal or growth factor-stimulated migration nor the revert the spread area of fibroblasts to the level of NR6WT. These findings suggest that the C-terminal tail of alpha-actinin-4 is essential for its function in cell migration and adhesion to substratum.
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