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Verfasst von:Št̓astná, Jana [VerfasserIn]   i
 Pan, Xiaoyu [VerfasserIn]   i
 Kutscheidt, Stefan [VerfasserIn]   i
 Lohmann, Volker [VerfasserIn]   i
 Fackler, Oliver Till [VerfasserIn]   i
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
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