| Online-Ressource |
Verfasst von: | Št̓astná, Jana [VerfasserIn]  |
| Pan, Xiaoyu [VerfasserIn]  |
| Kutscheidt, Stefan [VerfasserIn]  |
| Lohmann, Volker [VerfasserIn]  |
| Fackler, Oliver Till [VerfasserIn]  |
Titel: | Differing and isoform-specific roles for the formin DIAPH3 in plasma membrane blebbing and filopodia formation |
Verf.angabe: | Jana Stastna, Xiaoyu Pan, Haicui Wang, Alina Kollmannsperger, Stefan Kutscheidt, Volker Lohmann, Robert Grosse, Oliver T. Fackler |
Jahr: | 2012 |
Jahr des Originals: | 2011 |
Umfang: | 18 S. |
Teil: | volume:22 |
| year:2012 |
| number:4 |
| pages:728-745 |
| extent:18 |
Fussnoten: | Published: 20 December 2011 ; Gesehen am 20.09.2018 |
Titel Quelle: | Enthalten in: Cell research |
Ort Quelle: | [London] : Macmillan Publishers Limited, part of Springer Nature, 1990 |
Jahr Quelle: | 2012 |
Band/Heft Quelle: | 22(2012), 4, Seite 728-745 |
ISSN Quelle: | 1748-7838 |
Abstract: | Plasma membrane (PM) blebs are dynamic actin-rich cell protrusions that occur, e.g., during cytokinesis, amoeboid cell motility and cell attachment. Using a targeted siRNA screen against 21 actin nucleation factors, we identify a novel and essential role of the human diaphanous formin DIAPH3 in PM blebbing during cell adhesion. Suppression of DIAPH3 inhibited blebbing to promote rapid cell spreading involving β1-integrin. Multiple isoforms of DIAPH3 were detected on the mRNA and protein level of which isoforms 3 and 7 were the largest and most abundant isoforms that however did not induce formation of actin-rich protrusions. Rather, PM blebbing specifically involved the low abundance isoform 1 of DIAPH3 and activation of isoform 7 by deletion of the diaphanous-autoregulatory domain caused the formation of filopodia. Dimerization and actin assembly activity were essential for induction of specific cell protrusions by DIAPH3 isoforms 1 and 7. Our data suggest that the N-terminal region comprising the GTPase-binding domain determined the subcellular localization of the formin as well as its protrusion activity between blebs and filopodia. We propose that isoform-selective actin assembly by DIAPH3 exerts specific and differentially regulated functions during cell adhesion and motility. |
DOI: | doi:10.1038/cr.2011.202 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: http://dx.doi.org/10.1038/cr.2011.202 |
| Volltext: https://www.nature.com/articles/cr2011202 |
| DOI: https://doi.org/10.1038/cr.2011.202 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1581129033 |
Verknüpfungen: | → Zeitschrift |
Differing and isoform-specific roles for the formin DIAPH3 in plasma membrane blebbing and filopodia formation / Št̓astná, Jana [VerfasserIn]; 2012 (Online-Ressource)