EBs Recognize a Nucleotide-Dependent Structural Cap at Growing Microtubule Ends

Maurer, Sebastian P.; Fourniol, Franck J.; Bohner, Gergő; Moores, Carolyn A.; Surrey, Thomas

doi:10.1016/j.cell.2012.02.049

Cited by 362 publications

(482 citation statements)

References 62 publications

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“…9). An intriguing idea is that the KR-rich region of MTCL1 stabilizes MTs by binding to the groove between the MT protofilaments, similarly to EB1 and doublecortin 28,29 . Detailed analysis of the interaction mode between the KR-rich region and a single-MT strand is required to clarify this issue.…”

Section: Discussionmentioning

confidence: 99%

MTCL1 crosslinks and stabilizes non-centrosomal microtubules on the Golgi membrane

et al. 2014

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Recent studies have revealed the presence of a microtubule subpopulation called Golgi-derived microtubules that support Golgi ribbon formation, which is required for maintaining polarized cell migration. CLASPs and AKAP450/CG-NAP are involved in their formation, but the underlying molecular mechanisms remain unclear. Here, we find that the microtubule-crosslinking protein, MTCL1, is recruited to the Golgi membranes through interactions with CLASPs and AKAP450/CG-NAP, and promotes microtubule growth from the Golgi membrane. Correspondingly, MTCL1 knockdown specifically impairs the formation of the stable perinuclear microtubule network to which the Golgi ribbon tethers and extends. Rescue experiments demonstrate that besides its crosslinking activity mediated by the N-terminal microtubule-binding region, the C-terminal microtubule-binding region plays essential roles in these MTCL1 functions through a novel microtubule-stabilizing activity. These results suggest that MTCL1 cooperates with CLASPs and AKAP450/CG-NAP in the formation of the Golgi-derived microtubules, and mediates their development into a stable microtubule network.

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Section: Discussionmentioning

confidence: 99%

MTCL1 crosslinks and stabilizes non-centrosomal microtubules on the Golgi membrane

et al. 2014

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“…End-binding proteins recognize a tubulin conformation unique to the growing ends of MTs and can affect the dynamics of plusends by intrinsically altering the structure of the MT end (6)(7)(8) as well as recruiting other interacting proteins (9). In contrast, TOG domain-containing proteins, such as XMAP215, promote MT growth and have been suggested to act as MT "polymerases" (10,11).…”

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confidence: 99%

Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin

Hendershott

Vale

2014

Proc. Natl. Acad. Sci. U.S.A.

153

184

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The microtubule (MT) cytoskeleton plays an essential role in mitosis, intracellular transport, cell shape, and cell migration. The assembly and disassembly of MTs, which can occur through the addition or loss of subunits at the plus-or minus-ends of the polymer, is essential for MTs to carry out their biological functions. A variety of proteins act on MT ends to regulate their dynamics, including a recently described family of MT minus-end binding proteins called calmodulin-regulated spectrin-associated protein (CAMSAP)/Patronin/Nezha. Patronin, the single member of this family in Drosophila, was previously shown to stabilize MT minusends against depolymerization in vitro and in vivo. Here, we show that all three mammalian CAMSAP family members also bind specifically to MT minus-ends and protect them against kinesin-13-induced depolymerization. However, these proteins differ in their abilities to suppress tubulin addition at minus-ends and to dissociate from MTs. CAMSAP1 does not interfere with polymerization and tracks along growing minus-ends. CAMSAP2 and CAMSAP3 decrease the rate of tubulin incorporation and remain bound, thereby creating stretches of decorated MT minus-ends. By using truncation analysis, we find that somewhat different minimal domains of CAMSAP and Patronin are involved in minus-end localization. However, we find that, in both cases, a highly conserved C-terminal domain and a more variable central domain cooperate to suppress minus-end dynamics in vitro and that both regions are required to stabilize minus-ends in Drosophila S2 cells. These results show that members of the CAMSAP/Patronin family all localize to and protect minus-ends but have evolved distinct effects on MT dynamics.tubulin polymerization | cytoskeletal regulation | TIRF microscopy M icrotubules (MTs) are cellular polymers that are important for a variety of functions, including cargo transport and mitotic spindle formation. MTs are composed of dimers of α-and β-tubulin that assemble head-to-tail, creating a polar protofilament. Protofilaments then assemble laterally to form the canonical 13-protofilament MT structure, with β-tubulin exposed at fast-growing plus-ends and α-tubulin exposed at slow-growing minus-ends (1). MTs exhibit an intriguing property termed "dynamic instability," whereby the polymer can abruptly switch between episodes of net growth and shrinkage (2). The rates of growth and shrinkage as well as the frequency of transitions between these two states are regulated by numerous MT-associated proteins, many of which bind to the ends of the polymer (3, 4).The dynamics of MT plus-ends are regulated by a well-characterized network of plus-end tracking proteins (+TIPs) (5). End-binding proteins recognize a tubulin conformation unique to the growing ends of MTs and can affect the dynamics of plusends by intrinsically altering the structure of the MT end (6-8) as well as recruiting other interacting proteins (9). In contrast, TOG domain-containing proteins, such as XMAP215, promote MT growth and have been suggested ...

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“…Mini microtubule dynamics are regulated by an associated protein, BtubC, leading to stable, cytoskeletal rather than cytomotive filaments. The regulation of mini microtubules by BtubC is reminiscent of what certain microtubule associated proteins (MAPs), such as DCX, Clasp, and Mal3, do to microtubules (21)(22)(23).…”

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confidence: 99%

Four-stranded mini microtubules formed by Prosthecobacter BtubAB show dynamic instability

Deng

Fink

Bharat

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Microtubules, the dynamic, yet stiff hollow tubes built from αβ-tubulin protein heterodimers, are thought to be present only in eukaryotic cells. Here, we report a 3.6-Å helical reconstruction electron cryomicroscopy structure of four-stranded mini microtubules formed by bacterial tubulin-like Prosthecobacter dejongeii BtubAB proteins. Despite their much smaller diameter, mini microtubules share many key structural features with eukaryotic microtubules, such as an M-loop, alternating subunits, and a seam that breaks overall helical symmetry. Using in vitro total internal reflection fluorescence microscopy, we show that bacterial mini microtubules treadmill and display dynamic instability, another hallmark of eukaryotic microtubules. The third protein in the btub gene cluster, BtubC, previously known as “bacterial kinesin light chain,” binds along protofilaments every 8 nm, inhibits BtubAB mini microtubule catastrophe, and increases rescue. Our work reveals that some bacteria contain regulated and dynamic cytomotive microtubule systems that were once thought to be only useful in much larger and sophisticated eukaryotic cells.

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EBs Recognize a Nucleotide-Dependent Structural Cap at Growing Microtubule Ends

Cited by 362 publications

References 62 publications

MTCL1 crosslinks and stabilizes non-centrosomal microtubules on the Golgi membrane

MTCL1 crosslinks and stabilizes non-centrosomal microtubules on the Golgi membrane

Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin

Four-stranded mini microtubules formed by Prosthecobacter BtubAB show dynamic instability

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