ArticleThe Biochemical journal2001
Myosin VIIA is specifically associated with calmodulin and microtubule-associated protein-2B (MAP-2B).
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 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Spectrum ofGenes · 2021Article
- Mutations in Drosophila crinkled/Myosin VIIA disrupt denticle morphogenesis.Developmental biology · 2021Article
- Usher Syndrome: Genetics and Molecular Links of Hearing Loss and Directions for Therapy.Frontiers in genetics · 2020Review
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- Article
- Unconventional myosins acting unconventionally.Trends in cell biology · 2009Review
- The tail binds to the head-neck domain, inhibiting ATPase activity of myosin VIIA.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Article
- Drosophila crinkled, mutations of which disrupt morphogenesis and cause lethality, encodes fly myosin VIIA.Genetics · 2004Article
- The role of Rab27a in the regulation of melanosome distribution within retinal pigment epithelial cells.Molecular biology of the cell · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin VIIA is a motor molecule with a conserved head domain and tail region unique to myosin VIIA, which probably defines its unique function in vivo. In an attempt to further characterize myosin VIIA function we set out to identify molecule(s) that specifically associate with it. We demonstrate that 17 and 55 kDa proteins from mouse kidney and cochlea co-purify with myosin VIIA on affinity columns carrying immobilized anti-myosin VIIA antibody. N-terminal sequencing and immunoblotting analysis identified the 17 kDa protein as calmodulin, whereas MS and immunoblotting analysis identified the 55 kDa protein as microtubule-associated protein-2B (MAP-2B). Myosin VIIA can also be co-immunoprecipitated from kidney homogenate using anti-calmodulin or anti-MAP2 (recognizing isoforms 2A and 2B) antibodies, confirming the strong association between calmodulin and myosin VIIA and between MAP-2B and myosin VIIA. Myosin VIIA binds to calmodulin with an apparent K(d) of 10(-9) M. Scatchard analysis of the binding of myosin VIIA to MAP-2B provided evidence for two binding sites, with K(d) values of 10(-10) and 10(-9) M, which have been mapped to medial and C-terminal tail domains of myosin VIIA. The characterization of the interaction of calmodulin and MAP-2B with myosin VIIA provides new insights into the function of myosin VIIA.
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