Importin β2 Mediates the Spatio-temporal Regulation of Anillin through a Noncanonical Nuclear Localization Signal

Chen, Anan; Akhshi, Tara; Lavoie, Brigitte D.; Wilde, Andrew

doi:10.1074/jbc.m115.649160

Cited by 19 publications

(25 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1b ), that does not bind to DIAPH3 (Fig. 3a ), but does bind to CD2AP and importin β2 that interact with anillin regions immediately surrounding RQPL 23 , 24 (Supplementary Fig. 1c–e ).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Cytokinesis requires localized β-actin filament production by an actin isoform specific nucleator

et al. 2017

View full text Add to dashboard Cite

Cytokinesis is initiated by the localized assembly of the contractile ring, a dynamic actomyosin structure that generates a membrane furrow between the segregating chromosomal masses to divide a cell into two. Here we show that the stabilization and organization of the cytokinetic furrow is specifically dependent on localized β-actin filament assembly at the site of cytokinesis. β-actin filaments are assembled directly at the furrow by an anillin-dependent pathway that enhances RhoA-dependent activation of the formin DIAPH3, an actin nucleator. DIAPH3 specifically generates homopolymeric filaments of β-actin in vitro. By employing enhancers and activators, cells can achieve acute spatio-temporal control over isoform-specific actin arrays that are required for distinct cellular functions.

show abstract

Section: Resultsmentioning

confidence: 99%

“…Recombinant GST and 6× His-tagged proteins proteins were expressed and purified from BL21 Escherichia coli cells and MBP fusion proteins expressed and purified from ER2 E . coli (New England Biolabs) 23 . In brief, cells were grown in LB media at 37 °C to an optical density of 0.6 at A 600 .…”

Section: Methodsmentioning

confidence: 99%

Cytokinesis requires localized β-actin filament production by an actin isoform specific nucleator

et al. 2017

View full text Add to dashboard Cite

show abstract

“…7D). Anillin is reported to normally be nuclear in interphase (Chen et al, 2015), but we observed cortical anillin in cells undergoing ectopic furrowing (Fig. 5F).…”

Section: Ectopic Contractile Furrows Induced By Incenp St752ee Requirmentioning

confidence: 56%

Cell cycle-independent furrowing triggered by phosphomimetic mutations of the INCENP STD motif requires Plk1

Papini

Fant

Ogawa

et al. 2019

Journal of Cell Science

View full text Add to dashboard Cite

Timely and precise control of Aurora B kinase, the chromosomal passenger complex (CPC) catalytic subunit, is essential for accurate chromosome segregation and cytokinesis. Post-translational modifications of CPC subunits are directly involved in controlling Aurora B activity. Here, we identified a highly conserved acidic STD-rich motif of INCENP that is phosphorylated during mitosis in vivo and by Plk1 in vitro and is involved in controlling Aurora B activity. By using an INCENP conditional-knockout cell line, we show that impairing the phosphorylation status of this region disrupts chromosome congression and induces cytokinesis failure. In contrast, mimicking constitutive phosphorylation not only rescues cytokinesis but also induces ectopic furrows and contractile ring formation in a Plk1-and ROCK1-dependent manner independent of cell cycle and microtubule status. Our experiments identify the phospho-regulation of the INCENP STD motif as a novel mechanism that is key for chromosome alignment and cytokinesis. This article has an associated First Person interview with the first author of the paper.

show abstract

“…These results are somewhat confounded by a recent study using a temperature sensitive RCC1 cell line, also in humans, which suggests that chromosomally-derived Ran.GTP in anaphase is actually responsible for reducing the amount of cortical Anillin during asymmetric cell divisions (Kiyomitsu and Cheeseman, 2013 ). Moreover, the ability of Importin β2 to bind Anillin has been shown not to affect mitosis or cytokinesis; rather it required to sequester the protein in the nucleus in interphase, preventing abnormal cellular architecture (Chen et al, 2015 ). Although this could reflect differences between distinct populations of Anillin regulated through distinct Importins (see Section The Core Ran Pathway in Drosophila Embryos), such an explanation does not explain the discrepancy between a cortically-derived Ran.GTP gradient which may act positively upon Anillin and a chromosomally-derived Ran.GTP gradient that negatively regulates Anillin localization.…”

Section: Spatio-temporal Aspects Of Ran Functionmentioning

confidence: 99%

“…In support of this, several SAFs have, indeed, been shown to function in the nucleus during interphase (Jasin, 2002 ; Jaiswal and Narayan, 2008 ; Jiang et al, 2009 ; Reichert et al, 2011 ; Ohata et al, 2013 ; O'shaughnessy and Hendrich, 2013 ; Aydin et al, 2014 ; Neumayer et al, 2014 ; Vidi et al, 2014 ; Ha et al, 2015 ). Moreover, removal of NLSs from SAFs can result in interphase MT abnormalities (e.g., Chen et al, 2015 ). Such sequestration of already-active proteins in the nucleus prior to mitosis may therefore provide a way for cells to generate MTs quickly as soon as NEB occurs—a notion supported by the observation that dHURP immediately and preferentially localizes to those centrosomally-nucleated MTs facing the nucleus within the nucleus upon mitotic entry (Hayward et al, 2014 ).…”

Section: Final Remarksmentioning

confidence: 99%

The Ran Pathway in Drosophila melanogaster Mitosis

Chen

Barker

Wakefield

2015

Front. Cell Dev. Biol.

View full text Add to dashboard Cite

Over the last two decades, the small GTPase Ran has emerged as a central regulator of both mitosis and meiosis, particularly in the generation, maintenance, and regulation of the microtubule (MT)-based bipolar spindle. Ran-regulated pathways in mitosis bear many similarities to the well-characterized functions of Ran in nuclear transport and, as with transport, the majority of these mitotic effects are mediated through affecting the physical interaction between karyopherins and Spindle Assembly Factors (SAFs)—a loose term describing proteins or protein complexes involved in spindle assembly through promoting nucleation, stabilization, and/or depolymerization of MTs, through anchoring MTs to specific structures such as centrosomes, chromatin or kinetochores, or through sliding MTs along each other to generate the force required to achieve bipolarity. As such, the Ran-mediated pathway represents a crucial functional module within the wider spindle assembly landscape. Research into mitosis using the model organism Drosophila melanogaster has contributed substantially to our understanding of centrosome and spindle function. However, in comparison to mammalian systems, very little is known about the contribution of Ran-mediated pathways in Drosophila mitosis. This article sets out to summarize our understanding of the roles of the Ran pathway components in Drosophila mitosis, focusing on the syncytial blastoderm embryo, arguing that it can provide important insights into the conserved functions on Ran during spindle formation.

show abstract

Importin β2 Mediates the Spatio-temporal Regulation of Anillin through a Noncanonical Nuclear Localization Signal

Cited by 19 publications

References 39 publications

Cytokinesis requires localized β-actin filament production by an actin isoform specific nucleator

Cytokinesis requires localized β-actin filament production by an actin isoform specific nucleator

Cell cycle-independent furrowing triggered by phosphomimetic mutations of the INCENP STD motif requires Plk1

The Ran Pathway in Drosophila melanogaster Mitosis

Contact Info

Product

Resources

About