Eintrag weiter verarbeiten
Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging
Gespeichert in:
| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , |
| In: | Journal of Cell Science, 122, 2009, 6, S. 813-821 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Crane, Jonathan M. Verkman, Alan S. Crane, Jonathan M. Verkman, Alan S. |
|---|---|
| author |
Crane, Jonathan M. Verkman, Alan S. |
| spellingShingle |
Crane, Jonathan M. Verkman, Alan S. Journal of Cell Science Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging Cell Biology |
| author_sort |
crane, jonathan m. |
| spelling |
Crane, Jonathan M. Verkman, Alan S. 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.042341 <jats:p>We investigated the molecular determinants of aquaporin-4 (AQP4) assembly in orthogonal arrays of particles (OAPs) by visualizing fluorescently labeled AQP4 mutants in cell membranes using quantum-dot single-particle tracking and total internal reflection fluorescence microscopy. The full-length `long' (M1) form of AQP4 diffused freely in membranes and did not form OAPs, whereas the `short' (M23) form of AQP4 formed OAPs and was nearly immobile. Analysis of AQP4 deletion mutants revealed progressive disruption of OAPs by the addition of three to seven residues at the AQP4-M23 N-terminus, with polyalanines as effective as native AQP4 fragments. OAPs disappeared upon downstream deletions of AQP4-M23, which, from analysis of point mutants, involves N-terminus interactions of residues Val24, Ala25 and Phe26. OAP formation was also prevented by introducing proline residues at sites just downstream from the hydrophobic N-terminus of AQP4-M23. AQP1, an AQP4 homolog that does not form OAPs, was induced to form OAPs upon replacement of its N-terminal domain with that of AQP4-M23. Our results indicate that OAP formation by AQP4-M23 is stabilized by hydrophobic intermolecular interactions involving N-terminus residues, and that absence of OAPs in AQP4-M1 results from non-selective blocking of this interaction by seven residues just upstream from Met23.</jats:p> Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging Journal of Cell Science |
| doi_str_mv |
10.1242/jcs.042341 |
| facet_avail |
Online Free |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI0Mi9qY3MuMDQyMzQx |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI0Mi9qY3MuMDQyMzQx |
| institution |
DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 |
| imprint |
The Company of Biologists, 2009 |
| imprint_str_mv |
The Company of Biologists, 2009 |
| issn |
1477-9137 0021-9533 |
| issn_str_mv |
1477-9137 0021-9533 |
| language |
English |
| mega_collection |
The Company of Biologists (CrossRef) |
| match_str |
crane2009determinantsofaquaporin4assemblyinorthogonalarraysrevealedbylivecellsinglemoleculefluorescenceimaging |
| publishDateSort |
2009 |
| publisher |
The Company of Biologists |
| recordtype |
ai |
| record_format |
ai |
| series |
Journal of Cell Science |
| source_id |
49 |
| title |
Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_unstemmed |
Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_full |
Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_fullStr |
Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_full_unstemmed |
Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_short |
Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_sort |
determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.042341 |
| publishDate |
2009 |
| physical |
813-821 |
| description |
<jats:p>We investigated the molecular determinants of aquaporin-4 (AQP4) assembly in orthogonal arrays of particles (OAPs) by visualizing fluorescently labeled AQP4 mutants in cell membranes using quantum-dot single-particle tracking and total internal reflection fluorescence microscopy. The full-length `long' (M1) form of AQP4 diffused freely in membranes and did not form OAPs, whereas the `short' (M23) form of AQP4 formed OAPs and was nearly immobile. Analysis of AQP4 deletion mutants revealed progressive disruption of OAPs by the addition of three to seven residues at the AQP4-M23 N-terminus, with polyalanines as effective as native AQP4 fragments. OAPs disappeared upon downstream deletions of AQP4-M23, which, from analysis of point mutants, involves N-terminus interactions of residues Val24, Ala25 and Phe26. OAP formation was also prevented by introducing proline residues at sites just downstream from the hydrophobic N-terminus of AQP4-M23. AQP1, an AQP4 homolog that does not form OAPs, was induced to form OAPs upon replacement of its N-terminal domain with that of AQP4-M23. Our results indicate that OAP formation by AQP4-M23 is stabilized by hydrophobic intermolecular interactions involving N-terminus residues, and that absence of OAPs in AQP4-M1 results from non-selective blocking of this interaction by seven residues just upstream from Met23.</jats:p> |
| container_issue |
6 |
| container_start_page |
813 |
| container_title |
Journal of Cell Science |
| container_volume |
122 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792344749383876608 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T17:12:29.546Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Determinants+of+aquaporin-4+assembly+in+orthogonal+arrays+revealed+by+live-cell+single-molecule+fluorescence+imaging&rft.date=2009-03-15&genre=article&issn=0021-9533&volume=122&issue=6&spage=813&epage=821&pages=813-821&jtitle=Journal+of+Cell+Science&atitle=Determinants+of+aquaporin-4+assembly+in+orthogonal+arrays+revealed+by+live-cell+single-molecule+fluorescence+imaging&aulast=Verkman&aufirst=Alan+S.&rft_id=info%3Adoi%2F10.1242%2Fjcs.042341&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792344749383876608 |
| author | Crane, Jonathan M., Verkman, Alan S. |
| author_facet | Crane, Jonathan M., Verkman, Alan S., Crane, Jonathan M., Verkman, Alan S. |
| author_sort | crane, jonathan m. |
| container_issue | 6 |
| container_start_page | 813 |
| container_title | Journal of Cell Science |
| container_volume | 122 |
| description | <jats:p>We investigated the molecular determinants of aquaporin-4 (AQP4) assembly in orthogonal arrays of particles (OAPs) by visualizing fluorescently labeled AQP4 mutants in cell membranes using quantum-dot single-particle tracking and total internal reflection fluorescence microscopy. The full-length `long' (M1) form of AQP4 diffused freely in membranes and did not form OAPs, whereas the `short' (M23) form of AQP4 formed OAPs and was nearly immobile. Analysis of AQP4 deletion mutants revealed progressive disruption of OAPs by the addition of three to seven residues at the AQP4-M23 N-terminus, with polyalanines as effective as native AQP4 fragments. OAPs disappeared upon downstream deletions of AQP4-M23, which, from analysis of point mutants, involves N-terminus interactions of residues Val24, Ala25 and Phe26. OAP formation was also prevented by introducing proline residues at sites just downstream from the hydrophobic N-terminus of AQP4-M23. AQP1, an AQP4 homolog that does not form OAPs, was induced to form OAPs upon replacement of its N-terminal domain with that of AQP4-M23. Our results indicate that OAP formation by AQP4-M23 is stabilized by hydrophobic intermolecular interactions involving N-terminus residues, and that absence of OAPs in AQP4-M1 results from non-selective blocking of this interaction by seven residues just upstream from Met23.</jats:p> |
| doi_str_mv | 10.1242/jcs.042341 |
| facet_avail | Online, Free |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTI0Mi9qY3MuMDQyMzQx |
| imprint | The Company of Biologists, 2009 |
| imprint_str_mv | The Company of Biologists, 2009 |
| institution | DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1 |
| issn | 1477-9137, 0021-9533 |
| issn_str_mv | 1477-9137, 0021-9533 |
| language | English |
| last_indexed | 2024-03-01T17:12:29.546Z |
| match_str | crane2009determinantsofaquaporin4assemblyinorthogonalarraysrevealedbylivecellsinglemoleculefluorescenceimaging |
| mega_collection | The Company of Biologists (CrossRef) |
| physical | 813-821 |
| publishDate | 2009 |
| publishDateSort | 2009 |
| publisher | The Company of Biologists |
| record_format | ai |
| recordtype | ai |
| series | Journal of Cell Science |
| source_id | 49 |
| spelling | Crane, Jonathan M. Verkman, Alan S. 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.042341 <jats:p>We investigated the molecular determinants of aquaporin-4 (AQP4) assembly in orthogonal arrays of particles (OAPs) by visualizing fluorescently labeled AQP4 mutants in cell membranes using quantum-dot single-particle tracking and total internal reflection fluorescence microscopy. The full-length `long' (M1) form of AQP4 diffused freely in membranes and did not form OAPs, whereas the `short' (M23) form of AQP4 formed OAPs and was nearly immobile. Analysis of AQP4 deletion mutants revealed progressive disruption of OAPs by the addition of three to seven residues at the AQP4-M23 N-terminus, with polyalanines as effective as native AQP4 fragments. OAPs disappeared upon downstream deletions of AQP4-M23, which, from analysis of point mutants, involves N-terminus interactions of residues Val24, Ala25 and Phe26. OAP formation was also prevented by introducing proline residues at sites just downstream from the hydrophobic N-terminus of AQP4-M23. AQP1, an AQP4 homolog that does not form OAPs, was induced to form OAPs upon replacement of its N-terminal domain with that of AQP4-M23. Our results indicate that OAP formation by AQP4-M23 is stabilized by hydrophobic intermolecular interactions involving N-terminus residues, and that absence of OAPs in AQP4-M1 results from non-selective blocking of this interaction by seven residues just upstream from Met23.</jats:p> Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging Journal of Cell Science |
| spellingShingle | Crane, Jonathan M., Verkman, Alan S., Journal of Cell Science, Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging, Cell Biology |
| title | Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_full | Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_fullStr | Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_full_unstemmed | Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_short | Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_sort | determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| title_unstemmed | Determinants of aquaporin-4 assembly in orthogonal arrays revealed by live-cell single-molecule fluorescence imaging |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.042341 |