ArticleProceedings of the National Academy of Sciences of the United States of America2004
Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Tail domains of myosin-1e regulate phosphatidylinositol signaling and F-actin polymerization at the ventral layer of podosomes.Molecular biology of the cell · 2019Article
- Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.The EMBO journal · 2010Article
- An experimentally based computer search identifies unstructured membrane-binding sites in proteins: application to class I myosins, PAKS, and CARMIL.The Journal of biological chemistry · 2010Article
- Acanthamoeba myosin IC colocalizes with phosphatidylinositol 4,5-bisphosphate at the plasma membrane due to the high concentration of negative charge.The Journal of biological chemistry · 2008Article
- Evidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins.Journal of molecular biology · 2007Article
- The SH3 domain of a M7 interacts with its C-terminal proline-rich region.Protein science : a publication of the Protein Society · 2007Article
- Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Acanthamoeba myosin IC (AMIC) is a single-headed myosin comprised of one heavy chain (129 kDa) and one light chain (17 kDa). The heavy chain has head, neck (light chain-binding), and tail domains. The tail consists of four subdomains: a basic region (BR) (23 kDa) and two Gly/Pro/Ala-rich (GPA) regions, GPA1 (6 kDa) and GPA2 (15 kDa), flanking an Src homology 3 region (6 kDa). Although the AMIC head is similar in sequence, structure, and function (ATPase motor) to other myosin heads, the organization of the tail has been less clear as has its function beyond an assumed role in binding interaction partners, e.g., the BR has a membrane affinity and the GPA components bind F-actin in an ATP-independent manner. To investigate the spatial arrangement of subdomains in the tail, we have used cryo-electron microscopy and image reconstruction to compare actin filaments decorated with WT AMIC and tail-truncated mutants of various lengths. The BR forms an oval-shaped feature, approximately 40 A long, that diverges obliquely from the head, extending azimuthally around the actin filament and toward its barbed end. GPA2 and GPA1 are located together on the inner (actin-proximal) side of the tail, close enough to act in concert in binding the same or another actin filament. The outer face of the BR is strategically exposed for membrane or vesicle binding.
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