The Concentration of Nuf, a Rab11 Effector, at the Microtubule-organizing Center Is Cell Cycle–regulated, Dynein-dependent, and Coincides with Furrow Formation

Riggs, Blake; Fasulo, Barbara; Royou, Anne; Mische, Sarah; Cao, Jian; Hays, Thomas S.; Sullivan, William M.

doi:10.1091/mbc.e07-02-0146

Cited by 55 publications

(84 citation statements)

References 53 publications

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“…3D), suggesting that clustering of Rab11A endosomes in the middle part of the cell is more deleterious for actin organization than their random distribution. Our data support the notion that the localization of Rab11A endosomes strongly correlates with the position of microtubule minus ends, in line with the idea that it is controlled by cytoplasmic dynein (Horgan et al, 2010;Khanal et al, 2016;Riggs et al, 2007). When the microtubule array becomes more radial, Rab11A endosomes accumulate in the central part of the cell, and the formation of apical actin-rich structures is inhibited.…”

Section: Acf7 Binds To Camsap3 and Participates In Its Apical Recruitsupporting

confidence: 90%

Control of apico–basal epithelial polarity by the microtubule minus-end-binding protein CAMSAP3 and spectraplakin ACF7

Noordstra

Liu

Nijenhuis

et al. 2016

Journal of Cell Science

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The microtubule cytoskeleton regulates cell polarity by spatially organizing membrane trafficking and signaling processes. In epithelial cells, microtubules form parallel arrays aligned along the apico-basal axis, and recent work has demonstrated that the members of CAMSAP/Patronin family control apical tethering of microtubule minus ends. Here, we show that in mammalian intestinal epithelial cells, the spectraplakin ACF7 (also known as MACF1) specifically binds to CAMSAP3 and is required for the apical localization of CAMSAP3-decorated microtubule minus ends. Loss of ACF7 but not of CAMSAP3 or its homolog CAMSAP2 affected the formation of polarized epithelial cysts in three-dimensional cultures. In short-term epithelial polarization assays, knockout of CAMSAP3, but not of CAMSAP2, caused microtubule re-organization into a more radial centrosomal array, redistribution of Rab11-positive (also known as Rab11A) endosomes from the apical cell surface to the pericentrosomal region and inhibition of actin brush border formation at the apical side of the cell. We conclude that ACF7 is an important regulator of apico-basal polarity in mammalian intestinal cells and that a radial centrosome-centered microtubule organization can act as an inhibitor of epithelial polarity.

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Section: Acf7 Binds To Camsap3 and Participates In Its Apical Recruitsupporting

confidence: 90%

Control of apico–basal epithelial polarity by the microtubule minus-end-binding protein CAMSAP3 and spectraplakin ACF7

Noordstra

Liu

Nijenhuis

et al. 2016

Journal of Cell Science

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“…Second, CRMP might promote pericentrosomal Rab11 accumulation, which prevents centrosome movement via Dynein. The latter model is consistent with the fact that Rab11 interacts with Dynein via Nuclear-fallout (Riggs et al, 2007;Riggs et al, 2003). Although Numb is proposed to regulate CRMP activity positively during axonal growth via α-Adaptin-dependent endocytosis of L1 receptor (Nishimura et al, 2003), our genetic analyses of centrosome movements in numb, crmp, double numb, crmp mutant pI cells, as well as in response to numb overexpression, show that Numb and CRMP act antagonistically to regulate centrosome movement.…”

Section: Regulation Of Centrosome Dynamics During Pi Cell Divisionsupporting

confidence: 85%

Regulation of centrosome movements by Numb and the Collapsin Response Mediator Protein during Drosophila sensory progenitor asymmetric division

et al. 2013

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SUMMARYAsymmetric cell division generates cell fate diversity during development and adult life. Recent findings have demonstrated that during stem cell divisions, the movement of centrosomes is asymmetric in prophase and that such asymmetry participates in mitotic spindle orientation and cell polarization. Here, we have investigated the dynamics of centrosomes during Drosophila sensory organ precursor asymmetric divisions and find that centrosome movements are asymmetric during cytokinesis. We demonstrate that centrosome movements are controlled by the cell fate determinant Numb, which does not act via its classical effectors, Sanpodo and α-Adaptin, but via the Collapsin Response Mediator Protein (CRMP). Furthermore, we find that CRMP is necessary for efficient Notch signalling and that it regulates the duration of the pericentriolar accumulation of Rab11-positive endosomes, through which the Notch ligand, Delta is recycled. Our work characterizes an additional mode of asymmetric centrosome movement during asymmetric divisions and suggests a model whereby the asymmetry in centrosome movements participates in differential Notch activation to regulate cell fate specification.

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“…Anaphase microtubules are important in furrow formation in the subsequent cell cycle (Riggs et al, 2007). We examined Apc2 mutant microtubule organization and dynamics during cycle 12 anaphase.…”

Section: Research Articlementioning

confidence: 99%

A novel role for an APC2-Diaphanous complex in regulating actin organization inDrosophila

2009

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The rearrangement of cytoskeletal elements is essential for many cellular processes. The tumor suppressor Adenomatous polyposis coli (APC) affects the function of microtubules and actin, but the mechanisms by which it does so are not well understood. Here we report that Drosophila syncytial embryos null for Apc2 display defects in the formation and extension of pseudocleavage furrows, which are cortical actin structures important for mitotic fidelity in early embryos. Furthermore, we show that the formin Diaphanous (DIA) functions with APC2 in this process. Colocalization of APC2 and DIA peaks during furrow extension, and localization of APC2 to furrows is DIA-dependent. Furthermore, APC2 binds DIA directly through a region of APC2 not previously shown to interact with DIA-related formins. Consistent with these results, reduction of dia enhances actin defects in Apc2 mutant embryos. Thus, an APC2-DIA complex appears crucial for actin furrow extension in the syncytial embryo. Interestingly, EB1, a microtubule +TIP and reported partner of vertebrate APC and DIA1, may not function with APC2 and DIA in furrow extension. Finally, whereas DIA-related formins are activated by Rho family GTPases, our data suggest that the APC2-DIA complex might be independent of RHOGEF2 and RHO1. Furthermore, although microtubules play a role in furrow extension, our analysis suggests that APC2 and DIA function in a novel complex that affects actin directly, rather than through an effect on microtubules.

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The Concentration of Nuf, a Rab11 Effector, at the Microtubule-organizing Center Is Cell Cycle–regulated, Dynein-dependent, and Coincides with Furrow Formation

Cited by 55 publications

References 53 publications

Control of apico–basal epithelial polarity by the microtubule minus-end-binding protein CAMSAP3 and spectraplakin ACF7

Control of apico–basal epithelial polarity by the microtubule minus-end-binding protein CAMSAP3 and spectraplakin ACF7

Regulation of centrosome movements by Numb and the Collapsin Response Mediator Protein during Drosophila sensory progenitor asymmetric division

A novel role for an APC2-Diaphanous complex in regulating actin organization inDrosophila

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