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Volumn 19, Issue 1, 2007, Pages 57-66

What can myosin VI do in cells?

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MYOSIN IV; NUCLEOTIDE BINDING PROTEIN;

EID: 33846332811     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2006.12.005     Document Type: Review
Times cited : (96)

References (56)
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    • Park H, Li A, Chen L-Q, Houdusse A, Selvin PR, Sweeney HL: The unique insert at the end of the myosin VI motor is the sole determinant of directionality. Proc Natl Acad Sci USA 2007, in press. This work demonstrates that the unique myosin insert that is part of the converter (insert 2) is the sole determinant of directionality reversal. With it removed, myosin VI is plus-end directed. The approach used is to affix myosin V lever arms to the myosin VI converter with and without insert 2. Motility assays are used to determine the directionality of single- and double-headed constructs. Surprisingly, by examining the step size of the single dimeric molecules using a FIONA assay, the study also demonstrates that the large variability of the myosin VI step size is an inherent property of the motor, and is not due to a flexible lever arm extension.
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    • Bryant Z, Altman D, Spudich JA: The power stroke of myosin VI and determinants of directionality. Proc Natl Acad Sci USA 2007, in press. This work uses an optical trap to measure the size of the stroke and motility assays to determine the directionality of molecules created via sequential truncations of single-headed myosin VI constructs. The longest construct contains the putative lever arm extension, while the shortest removes insert 2. With insert 2 removed, the motor becomes plus-end directed, demonstrating that insert 2 is sufficient to reverse the directionality of the motor. The study also demonstrates that the single-headed myosin VI stroke size is large, even though the lever arm is short, consistent with a near 180° rotation of the converter from the pre-powerstroke to the end of the powerstroke (rigor).
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    • This was a demonstration, using a single molecule imaging technique known as FIONA, that myosin VI, like myosin V, uses a hand-over-hand mechanism for processive movement. This study further shows that the lever arm position fluctuates during stepping. This may underlie the large variability in the myosin VI step size, which appears to be a property of the motor core.
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    • This study presents both structural (EM) and single molecule functional data demonstrating that what we now term the 'lever arm extension' is in part responsible for the large step size of myosin VI. That it is a flexible element, which was inferred from the variability of the step size, is now in doubt.
    • Rock R.S., Ramamurthy B., Dunn A.R., Beccafico S., Rami B.R., Morris C., Spink B.J., Franzini-Armstrong C., Spudich J.A., and Sweeney H.L. A flexible domain is essential for the large step size and processivity of myosin VI. Mol Cell 17 (2005) 603-609. This study presents both structural (EM) and single molecule functional data demonstrating that what we now term the 'lever arm extension' is in part responsible for the large step size of myosin VI. That it is a flexible element, which was inferred from the variability of the step size, is now in doubt.
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    • Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering
    • This work addresses the question of whether or not full-length myosin VI can dimerize and function as a dimer. It demonstrates in vitro that it does when two full-length monomers bind near each other on actin, or are held together by antibody binding. The implication is that cargo binding regulates dimerization in vivo.
    • Park H., Ramamurthy B., Travaglia M., Safer D., Chen L.Q., Franzini-Armstrong C., Selvin P.R., and Sweeney H.L. Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering. Mol Cell 21 (2006) 331-336. This work addresses the question of whether or not full-length myosin VI can dimerize and function as a dimer. It demonstrates in vitro that it does when two full-length monomers bind near each other on actin, or are held together by antibody binding. The implication is that cargo binding regulates dimerization in vivo.
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    • Park, H.1    Ramamurthy, B.2    Travaglia, M.3    Safer, D.4    Chen, L.Q.5    Franzini-Armstrong, C.6    Selvin, P.R.7    Sweeney, H.L.8
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    • A monomeric myosin VI with a large working stroke
    • This was the initial demonstration that full-length myosin VI is isolated from cells as a monomer and does not readily dimerize in vitro. It raises the question of whether myosin VI works as a monomer or dimer in cells, or as both.
    • Lister I., Schmitz S., Walker M., Trinick J., Buss F., Veigel C., and Kendrick-Jones J. A monomeric myosin VI with a large working stroke. EMBO J 23 (2004) 1729-1738. This was the initial demonstration that full-length myosin VI is isolated from cells as a monomer and does not readily dimerize in vitro. It raises the question of whether myosin VI works as a monomer or dimer in cells, or as both.
    • (2004) EMBO J , vol.23 , pp. 1729-1738
    • Lister, I.1    Schmitz, S.2    Walker, M.3    Trinick, J.4    Buss, F.5    Veigel, C.6    Kendrick-Jones, J.7
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    • Dimerized Drosophila myosin VIIa: a processive motor
    • In this study the authors show that myosin VIIA, which has a putative coiled coil similar to that of myosin VI, is a processive motor when forced to dimerize (by the addition of leucine zipper). The authors also state (without showing data) that, as in the case of myosin VI, monomer clustering on actin can lead to dimerization and processive movement in the absence of a leucine zipper. Thus, myosin VIIa joins myosin VI as a candidate for cellular regulation via cargo-mediated dimerization.
    • Yang Y., Kovacs M., Sakamoto T., Zhang F., Kiehart D.P., and Sellers J.R. Dimerized Drosophila myosin VIIa: a processive motor. Proc Natl Acad Sci USA 103 (2006) 5746-5751. In this study the authors show that myosin VIIA, which has a putative coiled coil similar to that of myosin VI, is a processive motor when forced to dimerize (by the addition of leucine zipper). The authors also state (without showing data) that, as in the case of myosin VI, monomer clustering on actin can lead to dimerization and processive movement in the absence of a leucine zipper. Thus, myosin VIIa joins myosin VI as a candidate for cellular regulation via cargo-mediated dimerization.
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    • Yang, Y.1    Kovacs, M.2    Sakamoto, T.3    Zhang, F.4    Kiehart, D.P.5    Sellers, J.R.6
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    • Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography
    • This paper is an elegant use of two-dimensional crystallization and cryoelectron tomography and provides a structure for the inhibited, folded state of myosin V. Unlike myosin VI, myosin V is a constitutive dimer that is thought to unfold and be activated either by cargo binding or by increased calcium concentration in a cell
    • Liu J., Taylor D.W., Krementsova E.B., Trybus K.M., and Taylor K.A. Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography. Nature 442 (2006) 208-211. This paper is an elegant use of two-dimensional crystallization and cryoelectron tomography and provides a structure for the inhibited, folded state of myosin V. Unlike myosin VI, myosin V is a constitutive dimer that is thought to unfold and be activated either by cargo binding or by increased calcium concentration in a cell
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    • Myosin VI altered at threonine 406 stabilizes actin filaments in vivo
    • This is an intriguing demonstration that a mutation mimicking phosphorylation of the myosin VI motor within its actin-binding domain influences its behavior in cells. It is not clear that the mutation truly mimics phosphorylation in the myosin VI context, but the findings warrant further investigation.
    • Naccache S.N., and Hasson T. Myosin VI altered at threonine 406 stabilizes actin filaments in vivo. Cell Motil Cytoskeleton 63 (2006) 633-645. This is an intriguing demonstration that a mutation mimicking phosphorylation of the myosin VI motor within its actin-binding domain influences its behavior in cells. It is not clear that the mutation truly mimics phosphorylation in the myosin VI context, but the findings warrant further investigation.
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    • Naccache, S.N.1    Hasson, T.2
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.