- EMDB-24672: The cryo-EM map of KIF18A bound to KIFBP -
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Basic information
Entry
Database: EMDB / ID: EMD-24672
Title
The cryo-EM map of KIF18A bound to KIFBP
Map data
Sample
Complex: KIFBP:KIF18A complex
Protein or peptide: KIF-binding protein
Protein or peptide: Kinesin-like protein KIF18A
Ligand: MAGNESIUM ION
Ligand: ADENOSINE-5'-DIPHOSPHATE
Keywords
kinesin regualtion protein / MOTOR PROTEIN
Function / homology
Function and homology information
tubulin-dependent ATPase activity / mitotic spindle astral microtubule / mitotic spindle midzone / central nervous system projection neuron axonogenesis / kinetochore microtubule / male meiotic nuclear division / microtubule plus-end binding / Kinesins / plus-end-directed microtubule motor activity / microtubule depolymerization ...tubulin-dependent ATPase activity / mitotic spindle astral microtubule / mitotic spindle midzone / central nervous system projection neuron axonogenesis / kinetochore microtubule / male meiotic nuclear division / microtubule plus-end binding / Kinesins / plus-end-directed microtubule motor activity / microtubule depolymerization / COPI-dependent Golgi-to-ER retrograde traffic / kinesin complex / mitotic metaphase chromosome alignment / mitochondrial transport / seminiferous tubule development / microtubule-based movement / mitotic sister chromatid segregation / kinesin binding / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / regulation of microtubule cytoskeleton organization / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / ruffle / Resolution of Sister Chromatid Cohesion / neuron projection maintenance / MHC class II antigen presentation / caveola / cellular response to estradiol stimulus / RHO GTPases Activate Formins / kinetochore / microtubule cytoskeleton organization / Separation of Sister Chromatids / microtubule cytoskeleton / protein transport / actin binding / microtubule binding / in utero embryonic development / cytoskeleton / centrosome / ATP hydrolysis activity / mitochondrion / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function
KIF-1 binding protein / KIF-1 binding protein C terminal / Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily ...KIF-1 binding protein / KIF-1 binding protein C terminal / Kinesin-like protein / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily / Tetratricopeptide-like helical domain superfamily / P-loop containing nucleoside triphosphate hydrolase Similarity search - Domain/homology
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)
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
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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