Novel protein Callipygian defines the back of migrating cells
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 cyt...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Kristen F. Swaney [verfasserIn] |
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| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 112(2015), 29, Seite E3845-E3854 |
|---|---|
| Übergeordnetes Werk: |
volume:112 ; year:2015 ; number:29 ; pages:E3845-E3854 |
| Links: |
|---|
| DOI / URN: |
10.1073/pnas.1509098112 |
|---|
| Katalog-ID: |
OLC1970278234 |
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| 245 | 1 | 0 | |a Novel protein Callipygian defines the back of migrating cells |
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| 520 | |a 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. | ||
| 540 | |a Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences | ||
| 650 | 4 | |a Polymerization - drug effects | |
| 650 | 4 | |a Cell Shape - drug effects | |
| 650 | 4 | |a Protozoan Proteins - metabolism | |
| 650 | 4 | |a Green Fluorescent Proteins - metabolism | |
| 650 | 4 | |a Protein Transport - drug effects | |
| 650 | 4 | |a Cell Surface Extensions - metabolism | |
| 650 | 4 | |a Actins - metabolism | |
| 650 | 4 | |a Dictyostelium - drug effects | |
| 650 | 4 | |a Dictyostelium - cytology | |
| 650 | 4 | |a Chemotactic Factors - pharmacology | |
| 650 | 4 | |a Protozoan Proteins - chemistry | |
| 650 | 4 | |a Cell Differentiation - drug effects | |
| 650 | 4 | |a Phosphatidylinositols - pharmacology | |
| 650 | 4 | |a Cell Movement - drug effects | |
| 650 | 4 | |a Signal Transduction - drug effects | |
| 650 | 4 | |a Cell Polarity - drug effects | |
| 650 | 4 | |a Cell Surface Extensions - drug effects | |
| 650 | 4 | |a Cell Aggregation - drug effects | |
| 650 | 4 | |a Cell migration | |
| 650 | 4 | |a Chemotaxis | |
| 650 | 4 | |a Dictyostelium | |
| 650 | 4 | |a Physiological aspects | |
| 650 | 4 | |a Cell adhesion & migration | |
| 650 | 4 | |a Proteins | |
| 650 | 4 | |a Cytokines | |
| 650 | 4 | |a Cellular biology | |
| 650 | 4 | |a Membranes | |
| 650 | 4 | |a Morphology | |
| 700 | 0 | |a Peter N. Devreotes |4 oth | |
| 700 | 0 | |a Pablo A. Iglesias |4 oth | |
| 700 | 0 | |a Jane Borleis |4 oth | |
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| 856 | 4 | 2 | |u http://www.pnas.org/content/112/29/E3845.abstract |
| 856 | 4 | 2 | |u http://www.ncbi.nlm.nih.gov/pubmed/26130809 |
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10.1073/pnas.1509098112 doi PQ20160211 (DE-627)OLC1970278234 (DE-599)GBVOLC1970278234 (PRQ)c2225-4238d14bd12257f5c84dac7efae9911649639b735de7bfcbc783ade217cbad603 (KEY)0583363920150000112002903845novelproteincallipygiandefinesthebackofmigratingce DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Kristen F. Swaney verfasserin aut Novel protein Callipygian defines the back of migrating cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Polymerization - drug effects Cell Shape - drug effects Protozoan Proteins - metabolism Green Fluorescent Proteins - metabolism Protein Transport - drug effects Cell Surface Extensions - metabolism Actins - metabolism Dictyostelium - drug effects Dictyostelium - cytology Chemotactic Factors - pharmacology Protozoan Proteins - chemistry Cell Differentiation - drug effects Phosphatidylinositols - pharmacology Cell Movement - drug effects Signal Transduction - drug effects Cell Polarity - drug effects Cell Surface Extensions - drug effects Cell Aggregation - drug effects Cell migration Chemotaxis Dictyostelium Physiological aspects Cell adhesion & migration Proteins Cytokines Cellular biology Membranes Morphology Peter N. Devreotes oth Pablo A. Iglesias oth Jane Borleis oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 29, Seite E3845-E3854 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:29 pages:E3845-E3854 http://dx.doi.org/10.1073/pnas.1509098112 Volltext http://www.pnas.org/content/112/29/E3845.abstract http://www.ncbi.nlm.nih.gov/pubmed/26130809 http://search.proquest.com/docview/1699088327 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 29 E3845-E3854 |
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10.1073/pnas.1509098112 doi PQ20160211 (DE-627)OLC1970278234 (DE-599)GBVOLC1970278234 (PRQ)c2225-4238d14bd12257f5c84dac7efae9911649639b735de7bfcbc783ade217cbad603 (KEY)0583363920150000112002903845novelproteincallipygiandefinesthebackofmigratingce DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Kristen F. Swaney verfasserin aut Novel protein Callipygian defines the back of migrating cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Polymerization - drug effects Cell Shape - drug effects Protozoan Proteins - metabolism Green Fluorescent Proteins - metabolism Protein Transport - drug effects Cell Surface Extensions - metabolism Actins - metabolism Dictyostelium - drug effects Dictyostelium - cytology Chemotactic Factors - pharmacology Protozoan Proteins - chemistry Cell Differentiation - drug effects Phosphatidylinositols - pharmacology Cell Movement - drug effects Signal Transduction - drug effects Cell Polarity - drug effects Cell Surface Extensions - drug effects Cell Aggregation - drug effects Cell migration Chemotaxis Dictyostelium Physiological aspects Cell adhesion & migration Proteins Cytokines Cellular biology Membranes Morphology Peter N. Devreotes oth Pablo A. Iglesias oth Jane Borleis oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 29, Seite E3845-E3854 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:29 pages:E3845-E3854 http://dx.doi.org/10.1073/pnas.1509098112 Volltext http://www.pnas.org/content/112/29/E3845.abstract http://www.ncbi.nlm.nih.gov/pubmed/26130809 http://search.proquest.com/docview/1699088327 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 29 E3845-E3854 |
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10.1073/pnas.1509098112 doi PQ20160211 (DE-627)OLC1970278234 (DE-599)GBVOLC1970278234 (PRQ)c2225-4238d14bd12257f5c84dac7efae9911649639b735de7bfcbc783ade217cbad603 (KEY)0583363920150000112002903845novelproteincallipygiandefinesthebackofmigratingce DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Kristen F. Swaney verfasserin aut Novel protein Callipygian defines the back of migrating cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Polymerization - drug effects Cell Shape - drug effects Protozoan Proteins - metabolism Green Fluorescent Proteins - metabolism Protein Transport - drug effects Cell Surface Extensions - metabolism Actins - metabolism Dictyostelium - drug effects Dictyostelium - cytology Chemotactic Factors - pharmacology Protozoan Proteins - chemistry Cell Differentiation - drug effects Phosphatidylinositols - pharmacology Cell Movement - drug effects Signal Transduction - drug effects Cell Polarity - drug effects Cell Surface Extensions - drug effects Cell Aggregation - drug effects Cell migration Chemotaxis Dictyostelium Physiological aspects Cell adhesion & migration Proteins Cytokines Cellular biology Membranes Morphology Peter N. Devreotes oth Pablo A. Iglesias oth Jane Borleis oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 29, Seite E3845-E3854 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:29 pages:E3845-E3854 http://dx.doi.org/10.1073/pnas.1509098112 Volltext http://www.pnas.org/content/112/29/E3845.abstract http://www.ncbi.nlm.nih.gov/pubmed/26130809 http://search.proquest.com/docview/1699088327 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 29 E3845-E3854 |
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10.1073/pnas.1509098112 doi PQ20160211 (DE-627)OLC1970278234 (DE-599)GBVOLC1970278234 (PRQ)c2225-4238d14bd12257f5c84dac7efae9911649639b735de7bfcbc783ade217cbad603 (KEY)0583363920150000112002903845novelproteincallipygiandefinesthebackofmigratingce DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Kristen F. Swaney verfasserin aut Novel protein Callipygian defines the back of migrating cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Polymerization - drug effects Cell Shape - drug effects Protozoan Proteins - metabolism Green Fluorescent Proteins - metabolism Protein Transport - drug effects Cell Surface Extensions - metabolism Actins - metabolism Dictyostelium - drug effects Dictyostelium - cytology Chemotactic Factors - pharmacology Protozoan Proteins - chemistry Cell Differentiation - drug effects Phosphatidylinositols - pharmacology Cell Movement - drug effects Signal Transduction - drug effects Cell Polarity - drug effects Cell Surface Extensions - drug effects Cell Aggregation - drug effects Cell migration Chemotaxis Dictyostelium Physiological aspects Cell adhesion & migration Proteins Cytokines Cellular biology Membranes Morphology Peter N. Devreotes oth Pablo A. Iglesias oth Jane Borleis oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 29, Seite E3845-E3854 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:29 pages:E3845-E3854 http://dx.doi.org/10.1073/pnas.1509098112 Volltext http://www.pnas.org/content/112/29/E3845.abstract http://www.ncbi.nlm.nih.gov/pubmed/26130809 http://search.proquest.com/docview/1699088327 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 29 E3845-E3854 |
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10.1073/pnas.1509098112 doi PQ20160211 (DE-627)OLC1970278234 (DE-599)GBVOLC1970278234 (PRQ)c2225-4238d14bd12257f5c84dac7efae9911649639b735de7bfcbc783ade217cbad603 (KEY)0583363920150000112002903845novelproteincallipygiandefinesthebackofmigratingce DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Kristen F. Swaney verfasserin aut Novel protein Callipygian defines the back of migrating cells 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier 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. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Polymerization - drug effects Cell Shape - drug effects Protozoan Proteins - metabolism Green Fluorescent Proteins - metabolism Protein Transport - drug effects Cell Surface Extensions - metabolism Actins - metabolism Dictyostelium - drug effects Dictyostelium - cytology Chemotactic Factors - pharmacology Protozoan Proteins - chemistry Cell Differentiation - drug effects Phosphatidylinositols - pharmacology Cell Movement - drug effects Signal Transduction - drug effects Cell Polarity - drug effects Cell Surface Extensions - drug effects Cell Aggregation - drug effects Cell migration Chemotaxis Dictyostelium Physiological aspects Cell adhesion & migration Proteins Cytokines Cellular biology Membranes Morphology Peter N. Devreotes oth Pablo A. Iglesias oth Jane Borleis oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 29, Seite E3845-E3854 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:29 pages:E3845-E3854 http://dx.doi.org/10.1073/pnas.1509098112 Volltext http://www.pnas.org/content/112/29/E3845.abstract http://www.ncbi.nlm.nih.gov/pubmed/26130809 http://search.proquest.com/docview/1699088327 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 29 E3845-E3854 |
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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. |
| abstractGer |
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. |
| abstract_unstemmed |
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. |
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Novel protein Callipygian defines the back of migrating cells |
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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.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Polymerization - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell Shape - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protozoan Proteins - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Green Fluorescent Proteins - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Transport - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell Surface Extensions - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Actins - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Dictyostelium - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Dictyostelium - cytology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Chemotactic Factors - pharmacology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protozoan Proteins - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell Differentiation - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Phosphatidylinositols - pharmacology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell Movement - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Signal Transduction - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell Polarity - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell Surface Extensions - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell Aggregation - drug effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell migration</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Chemotaxis</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Dictyostelium</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Physiological aspects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cell adhesion & migration</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Proteins</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cytokines</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cellular biology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Membranes</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Morphology</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Peter N. Devreotes</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Pablo A. 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