Regulated Conformation of Myosin V
We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition of its enzymatic activity in the absence of cargo and Ca2+. In the absence of Ca2+ where the actin-activated MgATPase activity is low, purified brain myosin V sediments...
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Published in | The Journal of biological chemistry Vol. 279; no. 4; pp. 2333 - 2336 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
23.01.2004
American Society for Biochemistry and Molecular Biology |
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Abstract | We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition of its enzymatic activity in the absence of cargo and Ca2+. In the absence of Ca2+ where the actin-activated MgATPase activity is low, purified brain myosin V sediments in the analytical ultracentrifuge at 14 S as opposed to 11 S in the presence of Ca2+ where the activity is high. At high ionic strength it sediments at 10 S independent of Ca2+, and its regulation is poor. These data are consistent with myosin V having a compact, inactive conformation in the absence of Ca2+ and an extended conformation in the presence of Ca2+ or high ionic strength. Electron microscopy reveals that in the absence of Ca2+ the heads and tail are both folded to give a triangular shape, very different from the extended appearance of myosin V at high ionic strength. A recombinant myosin V heavy meromyosin fragment that is missing the distal portion of the tail domain is not regulated by calcium and has only a small change in sedimentation coefficient, which is in the opposite direction to that seen with intact myosin V. Electron microscopy shows that its heads are extended even in the absence of calcium. These data suggest that interaction between the motor and cargo binding domains may be a general mechanism for shutting down motor protein activity and thereby regulating the active movement of vesicles in cells. |
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AbstractList | We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition
of its enzymatic activity in the absence of cargo and Ca 2+ . In the absence of Ca 2+ where the actin-activated MgATPase activity is low, purified brain myosin V sediments in the analytical ultracentrifuge at
14 S as opposed to 11 S in the presence of Ca 2+ where the activity is high. At high ionic strength it sediments at 10 S independent of Ca 2+ , and its regulation is poor. These data are consistent with myosin V having a compact, inactive conformation in the absence
of Ca 2+ and an extended conformation in the presence of Ca 2+ or high ionic strength. Electron microscopy reveals that in the absence of Ca 2+ the heads and tail are both folded to give a triangular shape, very different from the extended appearance of myosin V at
high ionic strength. A recombinant myosin V heavy meromyosin fragment that is missing the distal portion of the tail domain
is not regulated by calcium and has only a small change in sedimentation coefficient, which is in the opposite direction to
that seen with intact myosin V. Electron microscopy shows that its heads are extended even in the absence of calcium. These
data suggest that interaction between the motor and cargo binding domains may be a general mechanism for shutting down motor
protein activity and thereby regulating the active movement of vesicles in cells. We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition of its enzymatic activity in the absence of cargo and Ca2+. In the absence of Ca2+ where the actin-activated MgATPase activity is low, purified brain myosin V sediments in the analytical ultracentrifuge at 14 S as opposed to 11 S in the presence of Ca2+ where the activity is high. At high ionic strength it sediments at 10 S independent of Ca2+, and its regulation is poor. These data are consistent with myosin V having a compact, inactive conformation in the absence of Ca2+ and an extended conformation in the presence of Ca2+ or high ionic strength. Electron microscopy reveals that in the absence of Ca2+ the heads and tail are both folded to give a triangular shape, very different from the extended appearance of myosin V at high ionic strength. A recombinant myosin V heavy meromyosin fragment that is missing the distal portion of the tail domain is not regulated by calcium and has only a small change in sedimentation coefficient, which is in the opposite direction to that seen with intact myosin V. Electron microscopy shows that its heads are extended even in the absence of calcium. These data suggest that interaction between the motor and cargo binding domains may be a general mechanism for shutting down motor protein activity and thereby regulating the active movement of vesicles in cells. We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition of its enzymatic activity in the absence of cargo and Ca super(2+). In the absence of Ca super(2+) where the actin-activated MgATPase activity is low, purified brain myosin V sediments in the analytical ultracentrifuge at 14 S as opposed to 11 S in the presence of Ca super(2+) where the activity is high. At high ionic strength it sediments at 10 S independent of Ca super(2+), and its regulation is poor. These data are consistent with myosin V having a compact, inactive conformation in the absence of Ca super(2+) and an extended conformation in the presence of Ca super(2+) or high ionic strength. Electron microscopy reveals that in the absence of Ca super(2+) the heads and tail are both folded to give a triangular shape, very different from the extended appearance of myosin V at high ionic strength. A recombinant myosin V heavy meromyosin fragment that is missing the distal portion of the tail domain is not regulated by calcium and has only a small change in sedimentation coefficient, which is in the opposite direction to that seen with intact myosin V. Electron microscopy shows that its heads are extended even in the absence of calcium. These data suggest that interaction between the motor and cargo binding domains may be a general mechanism for shutting down motor protein activity and thereby regulating the active movement of vesicles in cells. We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition of its enzymatic activity in the absence of cargo and Ca(2+). In the absence of Ca(2+) where the actin-activated MgATPase activity is low, purified brain myosin V sediments in the analytical ultracentrifuge at 14 S as opposed to 11 S in the presence of Ca(2+) where the activity is high. At high ionic strength it sediments at 10 S independent of Ca(2+), and its regulation is poor. These data are consistent with myosin V having a compact, inactive conformation in the absence of Ca(2+) and an extended conformation in the presence of Ca(2+) or high ionic strength. Electron microscopy reveals that in the absence of Ca(2+) the heads and tail are both folded to give a triangular shape, very different from the extended appearance of myosin V at high ionic strength. A recombinant myosin V heavy meromyosin fragment that is missing the distal portion of the tail domain is not regulated by calcium and has only a small change in sedimentation coefficient, which is in the opposite direction to that seen with intact myosin V. Electron microscopy shows that its heads are extended even in the absence of calcium. These data suggest that interaction between the motor and cargo binding domains may be a general mechanism for shutting down motor protein activity and thereby regulating the active movement of vesicles in cells. |
Author | Thirumurugan, Kavitha Wang, Fei Stafford, Walter F. Knight, Peter J. Hammer, John A. Sellers, James R. |
Author_xml | – sequence: 1 givenname: Fei surname: Wang fullname: Wang, Fei organization: Laboratory of Molecular Cardiology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 – sequence: 2 givenname: Kavitha surname: Thirumurugan fullname: Thirumurugan, Kavitha organization: Astbury Centre for Structural Molecular Biology, and School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom – sequence: 3 givenname: Walter F. surname: Stafford fullname: Stafford, Walter F. organization: Boston Biomedical Research Institute, Watertown, Massachusetts 02472 – sequence: 4 givenname: John A. surname: Hammer fullname: Hammer, John A. organization: Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 – sequence: 5 givenname: Peter J. surname: Knight fullname: Knight, Peter J. organization: Astbury Centre for Structural Molecular Biology, and School of Biomedical Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom – sequence: 6 givenname: James R. surname: Sellers fullname: Sellers, James R. email: sellersj@nhlbi.nih.gov organization: Laboratory of Molecular Cardiology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/14634000$$D View this record in MEDLINE/PubMed |
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Snippet | We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition of its enzymatic activity in... We have found that myosin V, an important actin-based vesicle transporter, has a folded conformation that is coupled to inhibition of its enzymatic activity in... |
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SubjectTerms | Animals Calcium - chemistry Calcium - metabolism Mice Models, Molecular Molecular Motor Proteins - chemistry Myosin Type V - chemistry Myosin Type V - metabolism Protein Conformation Protein Structure, Tertiary |
Title | Regulated Conformation of Myosin V |
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