Structural basis of EB1 effects on microtubule dynamics
نویسندگان
چکیده
منابع مشابه
Structural basis of EB1 effects on microtubule dynamics.
+TIPs (plus-end tracking proteins) are an increasing group of molecules that localize preferentially to the end of growing microtubules. +TIPs regulate microtubule dynamics and contribute to the organization of the microtubular network within the cell. Thus they participate in a wide range of cellular processes including cell division, motility and morphogenesis. EB1 (end-binding 1) is a highly...
متن کاملStructural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1.
Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus ends through a similar mechanism has not been resolved. Here, we report crystal structures of the tubulin bin...
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Highly conserved EB1 family proteins bind to the growing ends of microtubules, recruit multiple cargo proteins, and are critical for making dynamic microtubules in vivo. However, it is unclear how these master regulators of microtubule plus ends promote microtubule dynamics. In this paper, we identify a novel EB1 cargo protein, Sentin. Sentin depletion in Drosophila melanogaster S2 cells, simil...
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The EB1 family represents a highly conserved group of proteins, present in yeast through humans, that localize to spindle and cytoplasmic microtubules, especially at their distal tips. The budding yeast homologue of EB1, Bim1p, regulates microtubule stability and is important for positioning the mitotic spindle, anchoring it to the bud through astral microtubule attachment to the cortical prote...
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Several microtubule-binding proteins including EB1, dynactin, APC, and CLIP-170 localize to the plus-ends of growing microtubules. Although these proteins can bind to microtubules independently, evidence for interactions among them has led to the hypothesis of a plus-end complex. Here we clarify the interaction between EB1 and dynactin and show that EB1 binds directly to the N-terminus of the p...
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ژورنال
عنوان ژورنال: Biochemical Society Transactions
سال: 2009
ISSN: 0300-5127,1470-8752
DOI: 10.1042/bst0370997