Drosophila APC2 and Armadillo participate in tethering mitotic spindles to cortical actin

McCartney, Brooke M.; McEwen, Donald G.; Grevengoed, Elizabeth E.; Maddox, Paul S.; Bejsovec, Amy; Peifer, Mark

doi:10.1038/ncb1001-933

Cited by 152 publications

(172 citation statements)

References 30 publications

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“…Thus, APC attachment to the plasma membrane cortex and to microtubules does not require the APC Cterminal microtubule-or EB1-binding domains. These data are consistent with previous results that show that APC that lacks these domains localized with microtubules when overexpressed in cells 31 , and that Drosophila APC2, which lacks the C-terminal microtubule-binding domain, localized with microtubules 32 .…”

Section: Microtubules Overlay Cortical Apc Punctasupporting

confidence: 93%

APC is a component of an organizing template for cortical microtubule networks

Reilein

Nelson

2005

Nat Cell Biol

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A microtubule network on the basal cortex of polarized epithelial cells consists of noncentrosomal microtubules of mixed polarity. Here, we investigate the proteins that are involved in organizing this network, and we show that end-binding protein 1 (EB1), adenomatous polyposis coli protein (APC) and p150 Glued -although considered to be microtubule plus-end-binding proteins -are localized along the entire length of microtubules within the network, and at Tjunctions between microtubules. The network shows microtubule behaviours that arise from physical interactions between microtubules, including microtubule plus-end stabilization on the sides of other microtubules, and sliding of microtubule ends along other microtubules. APC also localizes to the basal cortex. Microtubules grew over and paused at APC puncta; an in vitro reconstituted microtubule network overlaid APC puncta; and microtubule network reconstitution was inhibited by function-blocking APC antibodies. Thus, APC is a component of a cortical template that guides microtubule network formation.Microtubule interactions with the cell cortex are thought to be important in a wide variety of cell functions, including cyokinesis, cell migration, membrane retraction during cell motility, and vesicle and protein delivery to, and retrieval from, the plasma membrane. However, molecular mechanisms that are involved in specifying microtubule attachment to, and organization at, the cell cortex are poorly understood.Proteins that associate with microtubule plus ends (+Tip proteins) might act as one point of regulation for microtubule-cortex interactions, because the plus ends are localized to the cell periphery in close apposition to the plasma membrane 1 . Several +Tip proteins have been identified, including APC, CLIP-170, EB1 and p150 Glued (reviewed in refs 2, 3). However, many questions remain unanswered regarding the regulation and function of +Tip proteins.Although +Tip proteins have been highlighted as regulators of microtubule dynamics and stability [4][5][6][7][8][9] , their role in microtubule binding and organization at the cell cortex remains poorly understood. Overexpression studies indicate that +Tip proteins are delivered to the cortex in association with microtubules 10,11 , and that they colocalize on the membrane cortex, perhaps in interacting complexes 8,12 . Examination of endogenous EB1 and APC showed that these +Tip proteins generally co-distribute in the same areas of the cell, but that their subcellular localization is not identical 13 .© 2005 Nature Publishing Group 2 Correspondence should be addressed to W.J.N. (wjnelson@stanford.edu).Note: Supplementary Information is available on the Nature Cell Biology website. COMPETING FINANCIAL INTERESTSThe authors declare that they have no competing financial interests. To address questions concerning the organization of microtubules and the functions of +Tip proteins at the cell cortex, we isolated intact basal plasma membranes with the associated cytoskeleton (basal patches) from polarized ...

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Section: Microtubules Overlay Cortical Apc Punctasupporting

confidence: 93%

APC is a component of an organizing template for cortical microtubule networks

Reilein

Nelson

2005

Nat Cell Biol

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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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“…1A), and the syncitial divisions of early embryos. 14 In these works, centrosomes have been shown to be the target for proteins that directly orient the mitotic spindle by forming physical bridges with polarity cues associated with the cell surface and cortical actin. Planar (lateral) divisions are specified based on signals from the adematous polyposis coli (APC) tumor suppressor protein, and Armadillo/beta-catenin.…”

Section: Roles Of the Centrosomementioning

confidence: 99%

HEF1-Aurora A Interactions: Points of Dialog between the Cell Cycle and Cell Attachment Signaling Networks

Pugacheva¹,

Golemis²

2006

Cell Cycle

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Regulated timing of cell division cycles, and geometrical precision in the planar orientation of cell division, are critical during organismal development and remain important for the maintenance of polarized structures in adults. Mounting evidence suggests that these processes are coordinated at the centrosome through the action of proteins that mediate both cell cycle and cell attachment. Our recent work identifying HEF1 as an activator of the Aurora A kinase suggests a novel hub for such integrated signaling. We suggest that defects in components of the machinery specifying the temporal and spatial integration of cell division may induce cancer and other diseases through pleiotropic effects on cell migration, proliferation, apoptosis, and genomic stability.

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Drosophila APC2 and Armadillo participate in tethering mitotic spindles to cortical actin

Cited by 152 publications

References 30 publications

APC is a component of an organizing template for cortical microtubule networks

APC is a component of an organizing template for cortical microtubule networks

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

HEF1-Aurora A Interactions: Points of Dialog between the Cell Cycle and Cell Attachment Signaling Networks

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