Positioning of the Mitotic Spindle by a Cortical-Microtubule Capture Mechanism

Lee, Laifong; Tirnauer, Jennifer S.; Li, Junjun; Schuyler, Scott C.; Liu, Jenny Y.; Pellman, David

doi:10.1126/science.287.5461.2260

Cited by 255 publications

(231 citation statements)

References 31 publications

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“…EB1 directs the microtubule-mediated delivery of connexin hemichannels to adherens junctions in epithelial cells (Shaw et al, 2007). APC directs the capture of EB1-tagged microtubules to cadherin/β-catenin-rich complexes (Lee et al, 2000;McCartney et al, 2001;Barth et al, 2002;Hamada and Bienz, 2002;Mimori-Kiyosue and Tsukita, 2003). Thus, APC positions EB1-tagged microtubules to precise positions of the cell surface.…”

Section: Discussionmentioning

confidence: 99%

Adenomatous polyposis coli plays a key role, in vivo, in coordinating assembly of the neuronal nicotinic postsynaptic complex

Rosenberg

Yang

Giovanni

et al. 2008

Molecular and Cellular Neuroscience

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The neuronal nicotinic synapse plays a central role in normal cognitive and autonomic function. Molecular mechanisms that direct the assembly of this synapse remain poorly defined, however. We show here that adenomatous polyposis coli (APC) organizes a multi-molecular complex that is essential for targeting α3*nAChRs to synapses. APC interaction with microtubule plus-end binding protein EB1 is required for α3*nAChR surface membrane insertion and stabilization. APC brings together EB1, the key cytoskeletal regulators macrophin and IQGAP1, and 14-3-3 adapter protein at nicotinic synapses. 14-3-3, in turn, links the α3-subunit to APC. This multi-molecular APC complex stabilizes the local microtubule and F-actin cytoskeleton and links postsynaptic components to the cytoskeleton-essential functions for controlling the molecular composition and stability of synapses. This work identifies macrophin, IQGAP1 and 14-3-3 as novel nicotinic synapse components and defines a new role for APC as an in vivo coordinator of nicotinic postsynaptic assembly in vertebrate neurons.

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Section: Discussionmentioning

confidence: 99%

Adenomatous polyposis coli plays a key role, in vivo, in coordinating assembly of the neuronal nicotinic postsynaptic complex

Rosenberg

Yang

Giovanni

et al. 2008

Molecular and Cellular Neuroscience

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“…As a result, symmetric division took place. During mitosis, spindle positioning involves a cortical-microtubule capture mechanism and several proteins are involved in the interaction between microtubules and the cortex [26,27]. In Saccharomyces cerevisiae, microtubule cortical attachment includes mediation by actin, Kar9p, Bud6p and Bni1p [28,29].…”

Section: Discussionmentioning

confidence: 99%

Effects of MEK inhibitor U0126 on meiotic progression in mouse oocytes: microtuble organization, asymmetric division and metaphase II arrest

et al. 2003

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In this study we used U0126, a potent and specific inhibitor of MEK, to study the roles of MEK/ERK/p90 rsk signaling pathway in the meiotic cell cycle of mouse oocytes. The phosphorylation of MAP kinase and p90 rsk in the oocytes treated with 1.5 M U0126 was the same as that in oocytes cultured in drug-free medium. With 1.5 M U0126 treatment, the spindles appeared normal as they formed in oocytes, but failed to maintain its structure. Instead, the spindle lost one pole or elongated extraordinarily. After further culture, some oocytes extruded gigantic polar bodies (>30 m) that later divided into two small ones. Some oocytes underwent symmetric division and produced two equal-size daughter cells in which normal spindles formed. In oocytes with different division patterns, MAP kinase was normally phosphorylated. When the concentration of U0126 was increased to 15 M, the phosphorylation of both MAPK and p90 rsk were inhibited, while symmetric division was decreased. When incubating in medium containing 15 M U0126 for 14 h, oocytes were activated, but part of them failed to emit polar bodies. MII oocytes were also activated by 15 M U0126, at the same time the dephosphorylation of MAP kinase and p90 rsk was observed. Our results indicate that 1) MEK plays important but not indispensable roles in microtubule organization; 2) MEK keeps normal meiotic spindle morphology, targets peripheral spindle positioning and regulates asymmetric division by activating some unknown substrates other than MAP kinase /p90 rsk ; and 3) activation of MEK/ERK/p90 rsk cascade maintains MII arrest in mouse oocytes.

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“…In budding yeast, the EB1 homologue Bim1 and APC-like protein Kar9 are microtubule plus-end (ϩend)-interacting proteins (ϩTIP) that link astral microtubules to the cortex and facilitate spindle placement at the bud neck before anaphase (Carminati and Stearns, 1997;Tirnauer et al, 1999;Beach et al, 2000;Lee et al, 2000;Miller et al, 2000;Yin et al, 2000;Liakopoulos et al, 2003;Maekawa et al, 2003). Paradoxically, EB1/Bim1 and APC/Kar9 can also localize to microtubule-organizing centers; centrosomes or spindle pole bodies (SPBs) in yeast, independently of astral microtubules (Liakopoulos et al, 2003;Louie et al, 2004;Maekawa and Schiebel, 2004).…”

Section: Introductionmentioning

confidence: 99%

γ-Tubulin Is Required for Proper Recruitment and Assembly of Kar9–Bim1 Complexes in Budding Yeast

Cuschieri

Miller

Vogel

2006

MBoC

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Microtubule plus-end-interacting proteins (؉TIPs) promote the dynamic interactions between the plus ends (؉ends) of astral microtubules and cortical actin that are required for preanaphase spindle positioning. Paradoxically, ؉TIPs such as the EB1 orthologue Bim1 and Kar9 also associate with spindle pole bodies (SPBs), the centrosome equivalent in budding yeast. Here, we show that deletion of four C-terminal residues of the budding yeast ␥-tubulin Tub4 (tub4-⌬dsyl) perturbs Bim1 and Kar9 localization to SPBs and Kar9-dependant spindle positioning. Surprisingly, we find Kar9 localizes to microtubule ؉ends in tub4-⌬dsyl cells, but these microtubules fail to position the spindle when targeted to the bud. Using cofluorescence and coaffinity purification, we show Kar9 complexes in tub4-⌬dsyl cells contain reduced levels of Bim1. Astral microtubule dynamics is suppressed in tub4-⌬dsyl cells, but it are restored by deletion of Kar9. Moreover, Myo2-and F-actin-dependent dwelling of Kar9 in the bud is observed in tub4-⌬dsyl cells, suggesting defective Kar9 complexes tether microtubule ؉ends to the cortex. Overproduction of Bim1, but not Kar9, restores Kar9-dependent spindle positioning in the tub4-⌬dsyl mutant, reduces cortical dwelling, and promotes Bim1-Kar9 interactions. We propose that SPBs, via the tail of Tub4, promote the assembly of functional ؉TIP complexes before their deployment to microtubule ؉ends.

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Positioning of the Mitotic Spindle by a Cortical-Microtubule Capture Mechanism

Cited by 255 publications

References 31 publications

Adenomatous polyposis coli plays a key role, in vivo, in coordinating assembly of the neuronal nicotinic postsynaptic complex

Adenomatous polyposis coli plays a key role, in vivo, in coordinating assembly of the neuronal nicotinic postsynaptic complex

Effects of MEK inhibitor U0126 on meiotic progression in mouse oocytes: microtuble organization, asymmetric division and metaphase II arrest

γ-Tubulin Is Required for Proper Recruitment and Assembly of Kar9–Bim1 Complexes in Budding Yeast

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