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-Structure paper
タイトル | Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. |
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ジャーナル・号・ページ | Cell, Vol. 142, Issue 3, Page 433-443, Year 2010 |
掲載日 | 2010年8月6日 |
著者 | Radhika Subramanian / Elizabeth M Wilson-Kubalek / Christopher P Arthur / Matthew J Bick / Elizabeth A Campbell / Seth A Darst / Ronald A Milligan / Tarun M Kapoor / |
PubMed 要旨 | Formation of microtubule architectures, required for cell shape maintenance in yeast, directional cell expansion in plants and cytokinesis in eukaryotes, depends on antiparallel microtubule ...Formation of microtubule architectures, required for cell shape maintenance in yeast, directional cell expansion in plants and cytokinesis in eukaryotes, depends on antiparallel microtubule crosslinking by the conserved MAP65 protein family. Here, we combine structural and single molecule fluorescence methods to examine how PRC1, the human MAP65, crosslinks antiparallel microtubules. We find that PRC1's microtubule binding is mediated by a structured domain with a spectrin-fold and an unstructured Lys/Arg-rich domain. These two domains, at each end of a homodimer, are connected by a linkage that is flexible on single microtubules, but forms well-defined crossbridges between antiparallel filaments. Further, we show that PRC1 crosslinks are compliant and do not substantially resist filament sliding by motor proteins in vitro. Together, our data show how MAP65s, by combining structural flexibility and rigidity, tune microtubule associations to establish crosslinks that selectively "mark" antiparallel overlap in dynamic cytoskeletal networks. |
リンク | Cell / PubMed:20691902 / PubMed Central |
手法 | EM (らせん対称) / X線回折 |
解像度 | 1.75 - 30.0 Å |
構造データ | EMDB-5205: EMDB-5212: PDB-3nrx: PDB-3nry: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | PROTEIN BINDING (タンパク質) / spectrin fold / microtubule binding domain / microtubule binding protein |