The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.
about
Complex interactions of the protein L-isoaspartyl methyltransferase and calmodulin revealed with the yeast two-hybrid systemTransient kinetic analysis of the 130-kDa myosin I (MYR-1 gene product) from rat liver. A myosin I designed for maintenance of tension?Mammalian class I myosin, Myo1b, is monomeric and cross-links actin filaments as determined by hydrodynamic studies and electron microscopyRat myr 4 defines a novel subclass of myosin I: identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivityThe ATPase activity of Myr3, a rat myosin I, is allosterically inhibited by its own tail domain and by Ca2+ binding to its light chain calmodulin.Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells.In vivo function of class I myosins.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 familyCalcium regulation of myosin-I tension sensingDisplacement-clamp measurement of the forces exerted by gating springs in the hair bundle.Assembly of the intestinal brush border: appearance and redistribution of microvillar core proteins in developing chick enterocytes.Mapping of the microvillar 110K-calmodulin complex: calmodulin-associated or -free fragments of the 110-kD polypeptide bind F-actin and retain ATPase activity.Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domainsReassociation of microvillar core proteins: making a microvillar core in vitro.The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme.The dynamic distribution of fluorescent analogues of actin and myosin in protrusions at the leading edge of migrating Swiss 3T3 fibroblasts.Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).Plasma membrane association of Acanthamoeba myosin ICalmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro.Binding of brush border myosin I to phospholipid vesicles.COOH terminus of membrane IgM is essential for an antigen-specific induction of some but not all early activation events in mature B cells.Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistryBrush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis.Organization of the actin filament cytoskeleton in the intestinal brush border: a quantitative and qualitative immunoelectron microscope studyChicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptidesPurification and characterization of a mammalian myosin ICalmodulin binding to Drosophila NinaC required for termination of phototransduction.Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement.The unconventional myosin encoded by the myoA gene plays a role in Dictyostelium motility.Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border.The organization of myosin and actin in rapid frozen nerve growth cones.Modulation of cellular morphology and locomotory activity by antibodies against myosin.Intracellular calcium and cAMP regulate directional pigment movements in teleost erythrophores.Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane proteinRestoration of cytoskeletal and membrane tethering defects but not defects in membrane trafficking in the intestinal brush border of mice lacking both myosin Ia and myosin VI.ATPase activity of the microvillar 110 kDa polypeptide-calmodulin complex is activated in Mg2+ and inhibited in K+-EDTA by F-actin.Evidence for a new member of the myosin I family from mammalian brain.Enzymatic characterization and functional domain mapping of brain myosin-V.A second isoform of chicken brush border myosin I contains a 29-residue inserted sequence that binds calmodulin.
P2860
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P2860
The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
The 110-kD protein-calmodulin ...... s an actin-activated MgATPase.
@ast
The 110-kD protein-calmodulin ...... s an actin-activated MgATPase.
@en
type
label
The 110-kD protein-calmodulin ...... s an actin-activated MgATPase.
@ast
The 110-kD protein-calmodulin ...... s an actin-activated MgATPase.
@en
prefLabel
The 110-kD protein-calmodulin ...... s an actin-activated MgATPase.
@ast
The 110-kD protein-calmodulin ...... s an actin-activated MgATPase.
@en
P2860
P356
P1476
The 110-kD protein-calmodulin ...... s an actin-activated MgATPase.
@en
P2093
K A Conzelman
M S Mooseker
P2860
P304
P356
10.1083/JCB.105.1.313
P407
P577
1987-07-01T00:00:00Z