期刊
JOURNAL OF CELL BIOLOGY
卷 176, 期 1, 页码 51-63出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200605097
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资金
- NIAID NIH HHS [R01 AI064668-03, R01 AI035950-14, R01 AI064668, AI64668, R01 AI035950] Funding Source: Medline
- NIGMS NIH HHS [R01 GM070862, R01 GM070862-02, GM070862, T32 GM145304] Funding Source: Medline
Kinesin motor proteins drive the transport of cellular cargoes along microtubule tracks. How motor protein activity is controlled in cells is unresolved, but it is likely coupled to changes in protein conformation and cargo association. By applying the quantitative method fluorescence resonance energy transfer (FRET) stoichiometry to fluorescent protein (FP)-labeled kinesin heavy chain (KHC) and kinesin light chain (KLC) subunits in live cells, we studied the overall structural organization and conformation of Kinesin-1 in the active and inactive states. Inactive Kinesin-1 molecules are folded and autoinhibited such that the KHC tail blocks the initial Interaction of the KHC motor with the microtubule. In addition, in the inactive state, the KHC motor domains are pushed apart by the KLC subunit. Thus, FRET stoichiometry reveals conformational changes of a protein complex in live cells. For Kinesin-1, activation requires a global conformational change that separates the KHC motor and tail domains and a local conformational change that moves the KHC motor domains closer together.
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