ArticleThe Journal of cell biology1989
Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 90 citations in OpenAlex.
- Discovery of the first unconventional myosin:Frontiers in physiology · 2023Review
- Non-muscle myosins in tumor progression, cancer cell invasion, and metastasis.Cytoskeleton (Hoboken, N.J.) · 2014Review
- A two-photon FRAP analysis of the cytoskeleton dynamics in the microvilli of intestinal cells.Biophysical journal · 2005Article
- Structural invariance of constitutively active and inactive mutants of acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments.The Journal of cell biology · 1998Article
- Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis.The Journal of cell biology · 1997Article
- Chicken myosin IB mRNA is highly expressed in lymphoid tissues.Journal of anatomy · 1996Article
- myoA of Aspergillus nidulans encodes an essential myosin I required for secretion and polarized growth.The Journal of cell biology · 1995Article
- Molecular analysis of the myosin gene family in Arabidopsis thaliana.Plant molecular biology · 1994Article
- Rat myr 4 defines a novel subclass of myosin I: identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity.The Journal of cell biology · 1994Article
- The structure and function of unconventional myosins: a review.Journal of muscle research and cell motility · 1994Review
- Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry.The Journal of cell biology · 1993Article
- Identification, characterization and cloning of myr 1, a mammalian myosin-I.The Journal of cell biology · 1993Article
- Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes of the myosin I family.The Journal of cell biology · 1993Article
- PCR-dependent amplification and sequence characterization of partial cDNAs encoding myosin-like proteins in Anemia phyllitidis (L.) Sw. and Arabidopsis thaliana (L.) Heynh.Plant molecular biology · 1993Article
- Molecular heterogeneity of the actin filament cytoskeleton associated with microvilli of photoreceptors, Müller's glial cells and pigment epithelial cells of the retina.Histochemistry · 1993Article
- Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains.The Journal of cell biology · 1992Article
- An unconventional myosin heavy chain gene from Drosophila melanogaster.The Journal of cell biology · 1992Article
- Tissue distribution and subcellular localization of mammalian myosin I.The Journal of cell biology · 1992Article
- Localization and specificity of the phospholipid and actin binding sites on the tail of Acanthamoeba myosin IC.The Journal of cell biology · 1992Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The actin bundle within each microvillus of the intestinal brush border is laterally tethered to the membrane by bridges composed of the protein complex, 110-kD-calmodulin. Previous studies have shown that avian 110-kD-calmodulin shares many properties with myosins including mechanochemical activity. In the present study, a cDNA molecule encoding 1,000 amino acids of the 110-kD protein has been sequenced, providing direct evidence that this protein is a vertebrate homologue of the tail-less, single-headed myosin I first described in amoeboid cells. The primary structure of the 110-kD protein (or brush border myosin I heavy chain) consists of two domains, an amino-terminal "head" domain and a 35-kD carboxy-terminal "tail" domain. The head domain is homologous to the S1 domain of other known myosins, with highest homology observed between that of Acanthamoeba myosin IB and the S1 domain of the protein encoded by bovine myosin I heavy chain gene (MIHC; Hoshimaru, M., and S. Nakanishi. 1987. J. Biol. Chem. 262:14625-14632). The carboxy-terminal domain shows no significant homology with any other known myosins except that of the bovine MIHC. This demonstrates that the bovine MIHC gene most probably encodes the heavy chain of bovine brush border myosin I (BBMI). A bacterially expressed fusion protein encoded by the brush border 110-kD cDNA binds calmodulin. Proteolytic removal of the carboxy-terminal domain of the fusion protein results in loss of calmodulin binding activity, a result consistent with previous studies on the domain structure of the 110-kD protein. No hydrophobic sequence is present in the molecule indicating that chicken BBMI heavy chain is probably not an integral membrane protein. Northern blot analysis of various chicken tissue indicates that BBMI heavy chain is preferentially expressed in the intestine.
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