Document Detail


Asymmetric cortical extension shifts cleavage furrow position in Drosophila neuroblasts.
MedLine Citation:
PMID:  21937716     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The cytokinetic cleavage furrow is typically positioned symmetrically relative to the cortical cell boundaries, but it can also be asymmetric. The mechanisms that control furrow site specification have been intensively studied, but how polar cortex movements influence ultimate furrow position remains poorly understood. We measured the position of the apical and the basal cortex in asymmetrically dividing Drosophila neuroblasts and observed preferential displacement of the apical cortex that becomes the larger daughter cell during anaphase, effectively shifting the cleavage furrow toward the smaller daughter cell. Asymmetric cortical extension is correlated with the presence of cortical myosin II, which is polarized in neuroblasts. Loss of myosin II asymmetry by perturbing heterotrimeric G-protein signaling results in symmetric extension and equal-sized daughter cells. We propose a model in which contraction-driven asymmetric polar extension of the neuroblast cortex during anaphase contributes to asymmetric furrow position and daughter cell size.
Authors:
Marisa Connell; Clemens Cabernard; Derek Ricketson; Chris Q Doe; Kenneth E Prehoda
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-09-21
Journal Detail:
Title:  Molecular biology of the cell     Volume:  22     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-17     Completed Date:  2012-05-17     Revised Date:  2014-04-23    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4220-6     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Asymmetric Cell Division*
Brain / cytology,  embryology
Cell Cycle Proteins / genetics
Cell Division
Cell Line
Cell Polarity
Cells, Cultured
Drosophila Proteins / metabolism
Drosophila melanogaster / cytology*,  embryology,  genetics
GTP-Binding Proteins / metabolism
Green Fluorescent Proteins
Microtubules / physiology,  ultrastructure
Myosin Type II / metabolism
Neural Stem Cells / cytology*,  ultrastructure
Neurons / cytology*,  metabolism,  ultrastructure
Recombinant Fusion Proteins / metabolism
Signal Transduction
Spindle Apparatus / physiology,  ultrastructure
Grant Support
ID/Acronym/Agency:
068032//PHS HHS; T32 GM007759/GM/NIGMS NIH HHS; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/Drosophila Proteins; 0/Recombinant Fusion Proteins; 147336-22-9/Green Fluorescent Proteins; EC 3.6.1.-/GTP-Binding Proteins; EC 3.6.1.-/Myosin Type II
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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