EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle

Morrison, Ewan E.; Wardleworth, B N; Askham, Jon M.; Markham, AF; Meredith, D

doi:10.1038/sj.onc.1202247

Cited by 208 publications

(214 citation statements)

References 9 publications

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“…Immuno¯uorescence analysis demonstrated that EB1 in HCT116 cells was associated with the microtubule cytoskeleton throughout the cell cycle (results not shown), as previously shown by ourselves (Morrison et al, 1998a) in a variety of other cell types. Furthermore, Western blotting of PBS/TX100 solubilized HCT116 cell extracts con®rmed that a single, completely soluble EB1 species was expressed in these cells (results not shown).…”

Section: Resultssupporting

confidence: 82%

“…EB1 was detected in all three precipitates. b-catenin was detected in precipitates from AS or G1-S arrested cells, with slightly more seen in G1-S extracts, but little was detected in precipitates from G2-M arrested cells Morrison et al, 1998a). This experiment demonstrates that the interaction between APC and EB1 does not require both proteins to be associated with microtubules, or indeed the presence of an intact microtubule cytoskeleton.…”

Section: Resultsmentioning

confidence: 70%

“…APC has been shown to associate with EB1 (Su et al, 1995), a 30 kDa protein which we (Morrison et al, 1998a) and others (Berrueta et al, 1998;Juwana et al, 1999) have recently shown to be associated with microtubule tips. APC is itself a microtubule tip-associated protein (Munemitsu et al, 1994;Smith et al, 1994;NaÈ thke et al, 1996;Morrison et al, 1997), a feature ascribed to the presence of a microtubule-binding basic domain towards the Cterminus of the protein.…”

Section: Introductionmentioning

confidence: 57%

“…From previous studies (NaÈ thke et al, 1996;Morrison et al, 1997Morrison et al, , 1998a it seemed plausible that the interaction between APC and EB1 served to target APC to microtubule tips. To test this hypothesis a number of expression constructs consisting of de®ned regions from the C-terminus of APC fused to eGFP were produced.…”

Section: Resultsmentioning

confidence: 99%

“…Interestingly, several yeast homologues of EB1 have been shown to play a role in mitotic spindle function, in the maintenance of chromosomal transmission ®delity and in a novel late mitotic checkpoint (Beinhauer et al, 1997;Schwartz et al, 1997;Muhua et al, 1998). We have suggested that the interaction between EB1 and APC may be downregulated during mitosis (Morrison et al, 1998a), a hypothesis based in part on the observation that no association of APC with the mitotic spindle has yet been reported despite the cytoplasmic localization of APC in interphase cells being dependent upon microtubules (NaÈ thke et al, 1996;Morrison et al, 1997). We have further speculated that the phosphorylation of APC at mitosis, for example by the p34 cdc2 mitotic kinase (Trzepacz et al, 1997), may negatively regulate the association with EB1.…”

Section: Introductionmentioning

confidence: 98%

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Regulation and function of the interaction between the APC tumour suppressor protein and EB1

et al. 2000

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The interaction between the adenomatous polyposis coli (APC) tumour suppressor and the microtubule-associated protein EB1 was examined. Immunoprecipitation suggested that APC and EB1 were not associated in cultures of HCT116 cells arrested in mitosis. The C-terminal 170 amino acids of APC, puri®ed as a bacterial fusion protein, precipitated EB1 from cell extracts, signi®cantly re®ning the location of the EB1 interaction domain in APC. In vitro phosphorylation of this fusion protein by either protein kinase A or p34 cdc2 reduced its ability to bind to EB1. Expression of GFP fusions to C-terminal APC sequences lacking or including the APC basic domain but encompassing the EB1 binding region in SW480 cells revealed a microtubule tip association which co-localized with that of EB1. Expression of the basic domain alone revealed a non-speci®c microtubule localization. In vitro interaction studies con®rmed that the APC basic domain did not contribute to EB1 binding. These ®ndings strongly suggest that the interaction between APC and EB1 targets APC to microtubule tips, and that the interaction between the two proteins is down-regulated during mitosis by the previously described mitotic phosphorylation of APC.

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Section: Resultssupporting

confidence: 82%

Section: Resultsmentioning

confidence: 70%

Section: Introductionmentioning

confidence: 57%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Regulation and function of the interaction between the APC tumour suppressor protein and EB1

et al. 2000

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Microtubule Plus End Dynamics − Do We Know How Microtubules Grow?

Haren

Wittmann

2019

BioEssays

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Microtubules form a highly dynamic filament network in all eukaryotic cells. Individual microtubules grow by tubulin dimer subunit addition and frequently switch between phases of growth and shortening. These unique dynamics are powered by GTP hydrolysis and drive microtubule network remodeling, which is central to eukaryotic cell biology and morphogenesis. Yet, our knowledge of the molecular events at growing microtubule ends is incomplete. Here we focus on how microtubules grow. We integrate recent ultrastructural and cell biological data to propose a realistic model of growing microtubule ends comprised of structurally distinct but biochemically overlapping zones. We discuss how regulatory proteins recognize different tubulin conformations along the microtubule lattice. Finally, we hypothesize that independent control of the major structural transitions at growing microtubule ends-tubulin dimer addition and subsequent closure of the MT wall-are optimized in cells to achieve rapid physiological microtubule growth.

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Dynamic properties of APC‐decorated microtubules in living cells

Dayanandan

Butler

Gordon‐Weeks

et al. 2003

Cell Motil. Cytoskeleton

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The adenomatous polyposis coli (APC) tumour suppressor protein is a component of the Wnt signalling pathway in which it plays a major role in controlling nuclear accumulation of beta-catenin and hence in the modulation of beta-catenin-regulated gene transcription. APC also associates with microtubules at the ends of cytoplasmic extensions in epithelial cells, a distribution that can be reproduced in COS cells ectopically expressing APC. To examine the effect of APC on microtubule properties, we monitored directly the behaviour of APC and of APC-decorated microtubules by time-lapse imaging of cytoplasmic extensions in live COS cells expressing APC tagged with a green fluorescent protein. On the proximal part of microtubules, APC was visualised as particulate material moving unidirectionally towards the plus end of microtubules. The distal parts of microtubules were uniformly decorated by APC and were animated by a motile behaviour in the form of aperiodic bending. This behaviour is likely to be the consequence of compression forces acting on microtubules encountering obstacles while elongating. The majority of APC-decorated microtubules in transfected COS cells was sensitive to depolymerisation by nocodazole, but they contained detyrosinated and acetylated alpha-tubulin, suggesting a reduction in the rate of subunit exchange at their growing end. Taken together, these results demonstrate that microtubule domains uniformly decorated by APC display dynamic and motile properties that may be significant for the postulated role of APC in targeting microtubules to specialised membrane sites.

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EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle

Cited by 208 publications

References 9 publications

Regulation and function of the interaction between the APC tumour suppressor protein and EB1

Regulation and function of the interaction between the APC tumour suppressor protein and EB1

Microtubule Plus End Dynamics − Do We Know How Microtubules Grow?

Dynamic properties of APC‐decorated microtubules in living cells

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