scholarly journals Drosophila aPKC is required for mitotic spindle orientation during symmetric division of epithelial cells

Development ◽  
2012 ◽  
Vol 139 (3) ◽  
pp. 503-513 ◽  
Author(s):  
L. G. Guilgur ◽  
P. Prudencio ◽  
T. Ferreira ◽  
A. R. Pimenta-Marques ◽  
R. G. Martinho
Keyword(s):  
Epithelial Cells ◽  
Mitotic Spindle ◽  
Spindle Orientation ◽  
Symmetric Division

scholarly journals Drosophila aPKC is required for mitotic spindle orientation during symmetric division of epithelial cells

2012 ◽  
Vol 125 (3) ◽  
pp. e1-e1
Author(s):  
L. G. Guilgur ◽  
P. Prudencio ◽  
T. Ferreira ◽  
A. R. Pimenta-Marques ◽  
R. G. Martinho
Keyword(s):  
Epithelial Cells ◽  
Mitotic Spindle ◽  
Spindle Orientation ◽  
Symmetric Division

scholarly journals Microtubule end tethering of a processive Kinesin-8 motor Kif18b is required for spindle positioning

2018 ◽  
Author(s):  
Toni McHugh ◽  
Agata Gluszek-Kustusz ◽  
Julie P.I. Welburn
Keyword(s):  
Cell Division ◽  
Mitotic Spindle ◽  
Essential Role ◽  
Gene Knockout ◽  
Integrated Approach ◽  
Spindle Orientation ◽  
Binding Region ◽  
Spindle Positioning ◽  
Symmetric Division ◽  
Astral Microtubule

AbstractMitotic spindle positioning specifies the plane of cell division during anaphase. Spindle orientation and positioning is therefore critical to ensure symmetric division in mitosis and asymmetric division during development. The control of astral microtubule length plays an essential role in positioning the spindle. Here we show using gene knockout that the Kinesin-8 Kif18b controls microtubule length to center the mitotic spindle at metaphase. Using an integrated approach, we reveal that Kif18b is a highly processive plus end-directed motor that uses a C-terminal non-motor microtubule-binding region to accumulate at growing microtubule plus ends. This region is regulated by phosphorylation to spatially control Kif18b accumulation at plus ends and is essential for Kif18b-dependent spindle positioning and regulation of microtubule length. Finally, we demonstrate that Kif18b shortens microtubules by increasing the catastrophe rate of dynamic microtubules. Overall, our work reveals that Kif18b utilizes its motile properties to reach microtubule ends where it regulates astral microtubule length to ensure spindle centering.

scholarly journals Cell–cell adhesion accounts for the different orientation of columnar and hepatocytic cell divisions

2017 ◽  
Vol 216 (11) ◽  
pp. 3847-3859 ◽  
Author(s):  
Francisco Lázaro-Diéguez ◽  
Anne Müsch
Keyword(s):  
Epithelial Cells ◽  
Mitotic Spindle ◽  
Spindle Orientation ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Spindle Rotation ◽  
Rescue Mechanism ◽  
Darby Canine Kidney ◽  
Canine Kidney

Mitotic spindle alignment with the basal or substrate-contacting domain ensures that dividing epithelial cells remain in the plane of the monolayer. Spindle orientation with respect to the substratum is established in metaphase coincident with maximal cell rounding, which enables unobstructed spindle rotation. Misaligned metaphase spindles are believed to result in divisions in which one daughter loses contact with the basal lamina. Here we describe a rescue mechanism that drives substrate-parallel spindle alignment of quasi-diagonal metaphase spindles in anaphase. It requires a Rho- and E-cadherin adhesion–dependent, substrate-parallel contractile actin belt at the apex that governs anaphase cell flattening. In contrast to monolayered Madin–Darby canine kidney cells, hepatocytic epithelial cells, which typically feature tilted metaphase spindles, lack this anaphase flattening mechanism and as a consequence maintain their spindle tilt through cytokinesis. This results in out-of-monolayer divisions, which we propose contribute to the stratified organization of hepatocyte cords in vivo.

scholarly journals Loss of MYO5B expression deregulates late endosome size which hinders mitotic spindle orientation

PLoS Biology ◽  
2019 ◽  
Vol 17 (11) ◽  
pp. e3000531 ◽  
Author(s):  
Changsen Leng ◽  
Arend W. Overeem ◽  
Fernando Cartón-Garcia ◽  
Qinghong Li ◽  
Karin Klappe ◽  
...  
Keyword(s):  
Mitotic Spindle ◽  
Late Endosome ◽  
Spindle Orientation

scholarly journals NuMA-microtubule interactions are critical for spindle orientation and the morphogenesis of diverse epidermal structures

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Lindsey Seldin ◽  
Andrew Muroyama ◽  
Terry Lechler
Keyword(s):  
Cell Fate ◽  
Mitotic Spindle ◽  
Cell Types ◽  
Epidermal Differentiation ◽  
Spindle Orientation ◽  
Direct Function ◽  
Spindle Positioning ◽  
Adult Mice ◽  
Neonatal Lethality ◽  
The Matrix

Mitotic spindle orientation is used to generate cell fate diversity and drive proper tissue morphogenesis. A complex of NuMA and dynein/dynactin is required for robust spindle orientation in a number of cell types. Previous research proposed that cortical dynein/dynactin was sufficient to generate forces on astral microtubules (MTs) to orient the spindle, with NuMA acting as a passive tether. In this study, we demonstrate that dynein/dynactin is insufficient for spindle orientation establishment in keratinocytes and that NuMA’s MT-binding domain, which targets MT tips, is also required. Loss of NuMA-MT interactions in skin caused defects in spindle orientation and epidermal differentiation, leading to neonatal lethality. In addition, we show that NuMA-MT interactions are also required in adult mice for hair follicle morphogenesis and spindle orientation within the transit-amplifying cells of the matrix. Loss of spindle orientation in matrix cells results in defective differentiation of matrix-derived lineages. Our results reveal an additional and direct function of NuMA during mitotic spindle positioning, as well as a reiterative use of spindle orientation in the skin to build diverse structures.

scholarly journals Warts Phosphorylates Mud to Promote Pins-Mediated Mitotic Spindle Orientation in Drosophila , Independent of Yorkie

2015 ◽  
Vol 25 (21) ◽  
pp. 2751-2762 ◽  
Author(s):  
Evan B. Dewey ◽  
Desiree Sanchez ◽  
Christopher A. Johnston
Keyword(s):  
Mitotic Spindle ◽  
Spindle Orientation

scholarly journals PTEN controls glandular morphogenesis through a juxtamembrane β-Arrestin1/ARHGAP21 scaffolding complex

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Arman Javadi ◽  
Ravi K Deevi ◽  
Emma Evergren ◽  
Elodie Blondel-Tepaz ◽  
George S Baillie ◽  
...  
Keyword(s):  
Mitotic Spindle ◽  
Molecular Mechanisms ◽  
Regulatory Protein ◽  
Membrane Binding ◽  
Three Dimensional ◽  
Spindle Orientation ◽  
C2 Domain ◽  
Gtpase Activating Protein ◽  
Defective Mutant ◽  
Glandular Morphogenesis

PTEN controls three-dimensional (3D) glandular morphogenesis by coupling juxtamembrane signaling to mitotic spindle machinery. While molecular mechanisms remain unclear, PTEN interacts through its C2 membrane-binding domain with the scaffold protein β-Arrestin1. Because β-Arrestin1 binds and suppresses the Cdc42 GTPase-activating protein ARHGAP21, we hypothesize that PTEN controls Cdc42 -dependent morphogenic processes through a β-Arrestin1-ARHGAP21 complex. Here, we show that PTEN knockdown (KD) impairs β-Arrestin1 membrane localization, β-Arrestin1-ARHGAP21 interactions, Cdc42 activation, mitotic spindle orientation and 3D glandular morphogenesis. Effects of PTEN deficiency were phenocopied by β-Arrestin1 KD or inhibition of β-Arrestin1-ARHGAP21 interactions. Conversely, silencing of ARHGAP21 enhanced Cdc42 activation and rescued aberrant morphogenic processes of PTEN-deficient cultures. Expression of the PTEN C2 domain mimicked effects of full-length PTEN but a membrane-binding defective mutant of the C2 domain abrogated these properties. Our results show that PTEN controls multicellular assembly through a membrane-associated regulatory protein complex composed of β-Arrestin1, ARHGAP21 and Cdc42.

Phosphorylation of BACH1 switches its function from transcription factor to mitotic chromosome regulator and promotes its interaction with HMMR

2018 ◽  
Vol 475 (5) ◽  
pp. 981-1002 ◽  
Author(s):  
Jie Li ◽  
Hiroki Shima ◽  
Hironari Nishizawa ◽  
Masatoshi Ikeda ◽  
Andrey Brydun ◽  
...  
Keyword(s):  
Mitotic Spindle ◽  
Isotope Labeling ◽  
Binding Activity ◽  
Mass Spectrometry Analysis ◽  
Spindle Orientation ◽  
Mitotic Spindles ◽  
Spectrometry Analysis ◽  
Dna Binding Activity ◽  
Ejection Force ◽  
M Phase

The transcription repressor BACH1 performs mutually independent dual roles in transcription regulation and chromosome alignment during mitosis by supporting polar ejection force of mitotic spindle. We now found that the mitotic spindles became oblique relative to the adhesion surface following endogenous BACH1 depletion in HeLa cells. This spindle orientation rearrangement was rescued by re-expression of BACH1 depending on its interactions with HMMR and CRM1, both of which are required for the positioning of mitotic spindle, but independently of its DNA-binding activity. A mass spectrometry analysis of BACH1 complexes in interphase and M phase revealed that BACH1 lost during mitosis interactions with proteins involved in chromatin and gene expression but retained interactions with HMMR and its known partners including CHICA. By analyzing BACH1 modification using stable isotope labeling with amino acids in cell culture, mitosis-specific phosphorylations of BACH1 were observed, and mutations of these residues abolished the activity of BACH1 to restore mitotic spindle orientation in knockdown cells and to interact with HMMR. Detailed histological analysis of Bach1-deficient mice revealed lengthening of the epithelial fold structures of the intestine. These observations suggest that BACH1 performs stabilization of mitotic spindle orientation together with HMMR and CRM1 in mitosis, and that the cell cycle-specific phosphorylation switches the transcriptional and mitotic functions of BACH1.

scholarly journals Connexin 43 maintains tissue polarity and regulates mitotic spindle orientation in the breast epithelium

2019 ◽  
Vol 132 (10) ◽  
pp. jcs223313 ◽  
Author(s):  
D. Bazzoun ◽  
H. A. Adissu ◽  
L. Wang ◽  
A. Urazaev ◽  
I. Tenvooren ◽  
...  
Keyword(s):  
Mitotic Spindle ◽  
Connexin 43 ◽  
Spindle Orientation ◽  
Breast Epithelium ◽  
Tissue Polarity
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