4.8 Article

How myosin VI coordinates its heads during processive movement

Journal

EMBO JOURNAL
Volume 26, Issue 11, Pages 2682-2692

Publisher

WILEY
DOI: 10.1038/sj.emboj.7601720

Keywords

gating; kinetics; motility; processivity; unconventional myosin

Funding

  1. NIAMS NIH HHS [R29 AR044420, R01 AR048931, R01 AR048565, AR048565, AR048931, AR044420, R01 AR044420] Funding Source: Medline
  2. NIGMS NIH HHS [GM068625, R01 GM068625] Funding Source: Medline

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A processive molecular motor must coordinate the enzymatic state of its two catalytic domains in order to prevent premature detachment from its track. For myosin V, internal strain produced when both heads of are attached to an actin track prevents completion of the lever arm swing of the lead head and blocks ADP release. However, this mechanism cannot work for myosin VI, since its lever arm positions are reversed. Here, we demonstrate that myosin VI gating is achieved instead by blocking ATP binding to the lead head once it has released its ADP. The structural basis for this unique gating mechanism involves an insert near the nucleotide binding pocket that is found only in class VI myosin. Reverse strain greatly favors binding of ADP to the lead head, which makes it possible for myosin VI to function as a processive transporter as well as an actin-based anchor. While this mechanism is unlike that of any other myosin superfamily member, it bears remarkable similarities to that of another processive motor from a different superfamily-kinesin I.

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