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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Swaney, Kristen F. Iglesias, Pablo A. Borleis, Jane Devreotes, Peter N. |
| Description | Author Affiliation: Swaney KF ( Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205); Borleis J ( Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205); Iglesias PA ( Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205); Devreotes PN ( Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205); |
| Abstract | Asymmetric protein localization is essential for cell polarity and migration. We report a novel protein, Callipygian (CynA), which localizes to the lagging edge before other proteins and becomes more tightly restricted as cells polarize; additionally, it accumulates in the cleavage furrow during cytokinesis. CynA protein that is tightly localized, or 'clustered,' to the cell rear is immobile, but when polarity is disrupted, it disperses throughout the membrane and responds to uniform chemoattractant stimulation by transiently localizing to the cytosol. These behaviors require a pleckstrin homology-domain membrane tether and a WD40 clustering domain, which can also direct other membrane proteins to the back. Fragments of CynA lacking the pleckstrin homology domain, which are normally found in the cytosol, localize to the lagging edge membrane when coexpressed with full-length protein, showing that CynA clustering is mediated by oligomerization. Cells lacking CynA have aberrant lateral protrusions, altered leading-edge morphology, and decreased directional persistence, whereas those overexpressing the protein display exaggerated features of polarity. Consistently, actin polymerization is inhibited at sites of CynA accumulation, thereby restricting protrusions to the opposite edge. We suggest that the mutual antagonism between CynA and regions of responsiveness creates a positive feedback loop that restricts CynA to the rear and contributes to the establishment of the cell axis. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 29 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Movement Cell Polarity Dictyostelium Cytology Protozoan Proteins Metabolism Actins Cell Aggregation Drug Effects Cell Differentiation Cell Shape Cell Surface Extensions Chemotactic Factors Pharmacology Green Fluorescent Proteins Phosphatidylinositols Polymerization Protein Structure, Tertiary Protein Transport Chemistry Signal Transduction Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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