Une myosine à contre-sens

Julie Ménétrey; Amel Bahloul; Anne Houdusse

doi:10.1051/medsci/2006222120

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Volume 22 / Numéro 2 (Février 2006)

Med Sci (Paris), 22 2 (2006) 120-122

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Numéro		Med Sci (Paris) Volume 22, Numéro 2, Février 2006


Page(s)		120 - 122
Section		Nouvelles
DOI		https://doi.org/10.1051/medsci/2006222120
Publié en ligne		15 février 2006

Wells AL, Lin AW, Chen LQ, et al. Myosin VI is an actin-based motor that moves backwards. Nature 1999; 401 : 505–8. [Google Scholar]
Rock RS, Rice SE, Wells AL, et al. Myosin VI is a processive motor with a large step size. Proc Natl Acad Sci USA 2001; 98 : 13655–9. [Google Scholar]
Homma K, Yoshimura M, Saito J, et al. The core of the motor domain determines the direction of myosin movement. Nature 2001; 412 : 831–4. [Google Scholar]
Bahloul A, Chevreux G, Wells AL, et al. The unique insert in myosin VI is a structural calcium-calmodulin binding site. Proc Natl Acad Sci USA 2004; 101 : 4787–92. [Google Scholar]
Ménétrey J, Bahloul A, Wells AL, et al. The structure of myosin VI reveals the mechanism of directionality reversal for the myosin motors. Nature 2005; 435 : 779-85. [Google Scholar]
Coureux PD, Wells AL, Ménétrey J, et al. A structural state of the myosin V motor without bound nucleotide. Nature 2003; 425 : 419–23. [Google Scholar]
Rock RS, Ramamurthy B, Dunn AR, et al. A flexible domain is essential for the large step size and processivity of myosin VI. Mol Cell 2005; 17 : 603–9. [Google Scholar]
Rosenfeld SS, Fordyce PM, Jefferson GM, et al. Stepping and stretching : how kinesin uses internal strain to walk processively. J Biol Chem 2003; 278 : 18530–6. [Google Scholar]
Yildiz A, Park H, Safer D, et al. Myosin VI steps via a hand-over-hand mechanism with its lever arm undergoing fluctuations when attached to actin. J Biol Chem 2004; 279 : 37223–6. [Google Scholar]
Houdusse A, Kalabokis VN, Himmel D, et al. Atomic structure of scallop myosin subfragment S1 complexed with MgADP : a novel conformation of the myosin head. Cell 1999; 97 : 459–70. [Google Scholar]

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[1] Wells AL, Lin AW, Chen LQ, et al. Myosin VI is an actin-based motor that moves backwards. Nature 1999; 401 : 505–8. [Google Scholar]

[2] Rock RS, Rice SE, Wells AL, et al. Myosin VI is a processive motor with a large step size. Proc Natl Acad Sci USA 2001; 98 : 13655–9. [Google Scholar]

[3] Homma K, Yoshimura M, Saito J, et al. The core of the motor domain determines the direction of myosin movement. Nature 2001; 412 : 831–4. [Google Scholar]

[4] Bahloul A, Chevreux G, Wells AL, et al. The unique insert in myosin VI is a structural calcium-calmodulin binding site. Proc Natl Acad Sci USA 2004; 101 : 4787–92. [Google Scholar]

[5] Ménétrey J, Bahloul A, Wells AL, et al. The structure of myosin VI reveals the mechanism of directionality reversal for the myosin motors. Nature 2005; 435 : 779-85. [Google Scholar]

[6] Coureux PD, Wells AL, Ménétrey J, et al. A structural state of the myosin V motor without bound nucleotide. Nature 2003; 425 : 419–23. [Google Scholar]

[7] Rock RS, Ramamurthy B, Dunn AR, et al. A flexible domain is essential for the large step size and processivity of myosin VI. Mol Cell 2005; 17 : 603–9. [Google Scholar]

[8] Rosenfeld SS, Fordyce PM, Jefferson GM, et al. Stepping and stretching : how kinesin uses internal strain to walk processively. J Biol Chem 2003; 278 : 18530–6. [Google Scholar]

[9] Yildiz A, Park H, Safer D, et al. Myosin VI steps via a hand-over-hand mechanism with its lever arm undergoing fluctuations when attached to actin. J Biol Chem 2004; 279 : 37223–6. [Google Scholar]

[10] Houdusse A, Kalabokis VN, Himmel D, et al. Atomic structure of scallop myosin subfragment S1 complexed with MgADP : a novel conformation of the myosin head. Cell 1999; 97 : 459–70. [Google Scholar]