transport along microtubule / central nervous system projection neuron axonogenesis / mitochondrion transport along microtubule / kinesin binding / protein sequestering activity / neuron projection maintenance / microtubule cytoskeleton organization / in utero embryonic development / cytoskeleton / mitochondrion Similarity search - Function
KIF-1 binding protein / KIF-1 binding protein C terminal / Tetratricopeptide-like helical domain superfamily Similarity search - Domain/homology
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM094231
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM136822
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM121491
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM086610
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM111725
United States
Citation
Journal: Sci Adv / Year: 2021 Title: Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding. Authors: April L Solon / Zhenyu Tan / Katherine L Schutt / Lauren Jepsen / Sarah E Haynes / Alexey I Nesvizhskii / David Sept / Jason Stumpff / Ryoma Ohi / Michael A Cianfrocco / Abstract: Kinesins are regulated in space and time to ensure activation only in the presence of cargo. Kinesin-binding protein (KIFBP), which is mutated in Goldberg-Shprintzen syndrome, binds to and inhibits ...Kinesins are regulated in space and time to ensure activation only in the presence of cargo. Kinesin-binding protein (KIFBP), which is mutated in Goldberg-Shprintzen syndrome, binds to and inhibits the catalytic motor heads of 8 of 45 kinesin superfamily members, but the mechanism remains poorly defined. Here, we used cryo–electron microscopy and cross-linking mass spectrometry to determine high-resolution structures of KIFBP alone and in complex with two mitotic kinesins, revealing structural remodeling of kinesin by KIFBP. We find that KIFBP remodels kinesin motors and blocks microtubule binding (i) via allosteric changes to kinesin and (ii) by sterically blocking access to the microtubule. We identified two regions of KIFBP necessary for kinesin binding and cellular regulation during mitosis. Together, this work further elucidates the molecular mechanism of KIFBP-mediated kinesin inhibition and supports a model in which structural rearrangement of kinesin motor domains by KIFBP abrogates motor protein activity.
History
Deposition
Aug 11, 2021
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Header (metadata) release
Sep 8, 2021
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Map release
Sep 8, 2021
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Update
Jun 5, 2024
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Current status
Jun 5, 2024
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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