The unique insert at the end of the myosin VI motor is the sole determinant of directionality

No abstract is available for this paper.

• Publication year

  2007

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  2007-01-16

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1073/pnas.0610066104PMID 17213313PMCID PMC1764864
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering.

  2006cited by this paper
• The structure of the myosin VI motor reveals the mechanism of directionality reversal

  2005cited by this paper
• A flexible domain is essential for the large step size and processivity of myosin VI.

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• Molecular engineering of a backwards-moving myosin motor

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• The mechanism of myosin VI translocation and its load-induced anchoring.

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• Myosin VI: cellular functions and motor properties.

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• The unique insert in myosin VI is a structural calcium-calmodulin binding site.

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• Myosin VI walks hand-over-hand along actin

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• Nanometer localization of single green fluorescent proteins: evidence that myosin V walks hand-over-hand via telemark configuration.

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• Myosin VI Steps via a Hand-over-Hand Mechanism with Its Lever Arm Undergoing Fluctuations when Attached to Actin*

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• Myosin VI: a structural role in actin organization important for protein and organelle localization and trafficking.

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• A structural state of the myosin V motor without bound nucleotide

  2003cited by this paper
• Class VI myosin moves processively along actin filaments backward with large steps.

  2002cited by this paper
• Role of the lever arm in the processive stepping of myosin V

  2002cited by this paper
• Myosin VI is a processive motor with a large step size

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• Kinetic Mechanism and Regulation of Myosin VI*

  2001cited by this paper
• The core of the motor domain determines the direction of myosin movement

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  2000cited by this paper
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  1999cited by this paper
• Kinetic Tuning of Myosin via a Flexible Loop Adjacent to the Nucleotide Binding Pocket*

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• Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis

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• Formation of Aberrant Myotubes by Myoblasts Lacking Myosin VI Is Associated with Alterations in the Cytoskeleton Organization, Myoblast Adhesion and Fusion

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• Exploration par simulations numériques de l'auto-organisation du cytosquelette sous conditions géométriquement contrôlées. (Exploration by numerical simulations of cytoskeleton auto-organization)

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• Mouse Myosin-19 Is a Plus-end-directed, High-duty Ratio Molecular Motor*

  2014cites this paper
• Molecular machines like myosin use randomness to behave predictably.

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• Myosin VI has a One Track Mind Versus Myosin Va When Moving on Actin Bundles or at an Intersection

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• Identifying Highly Conserved and Unique Structural Elements in Myosin VI

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• Dynamic Exchange of Myosin VI on Endocytic Structures*

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• Engineering controllable bidirectional molecular motors based on myosin

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• Processive steps in the reverse direction require uncoupling of the lead head lever arm of myosin VI.

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• Identifying Highly Conserved and Unique Structural Elements in Myosin VI

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• Simultaneous observation of the lever arm and head explains myosin VI dual function.

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• Free energy of conformational transition paths in biomolecules: the string method and its application to myosin VI.

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• A conformational transition in the myosin VI converter contributes to the variable step size.

  2011cites this paper
• Single-molecule studies of unconventional motor protein myosin VI

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• Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI.

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• Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis

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