- EMDB-24672: The cryo-EM map of KIF18A bound to KIFBP -
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基本情報
登録情報
データベース: EMDB / ID: EMD-24672
タイトル
The cryo-EM map of KIF18A bound to KIFBP
マップデータ
試料
複合体: KIFBP:KIF18A complex
タンパク質・ペプチド: KIF-binding protein
タンパク質・ペプチド: Kinesin-like protein KIF18A
リガンド: MAGNESIUM ION
リガンド: ADENOSINE-5'-DIPHOSPHATE
キーワード
kinesin regualtion protein / MOTOR PROTEIN
機能・相同性
機能・相同性情報
tubulin-dependent ATPase activity / mitotic spindle astral microtubule / transport along 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 ...tubulin-dependent ATPase activity / mitotic spindle astral microtubule / transport along 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 / mitochondrion transport along microtubule / COPI-dependent Golgi-to-ER retrograde traffic / kinesin complex / mitotic metaphase chromosome alignment / microtubule-based movement / seminiferous tubule development / mitotic sister chromatid segregation / kinesin binding / regulation of microtubule cytoskeleton organization / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / ruffle / neuron projection maintenance / protein sequestering activity / Resolution of Sister Chromatid Cohesion / MHC class II antigen presentation / cellular response to estradiol stimulus / RHO GTPases Activate Formins / caveola / 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 / cytosol / cytoplasm 類似検索 - 分子機能
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 profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / 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 profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain / Kinesin motor domain superfamily / Tetratricopeptide-like helical domain superfamily / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
Kinesin-like protein KIF18A / KIF-binding protein 類似検索 - 構成要素
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM086610
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM094231
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM136822
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM121491
米国
引用
ジャーナル: Sci Adv / 年: 2021 タイトル: Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding. 著者: 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 / 要旨: 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.