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Article: Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation

TitleMyosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation
Authors
KeywordsCell–matrix adhesion
Myosin 1E
Transport
Issue Date2013
PublisherThe Company of Biologists Ltd..
Citation
Biology Open, 2013, v. 2 n. 12, p. 1288-1299 How to Cite?
AbstractBecause the actin network in active lamellipodia is continuously assembling at the edge, moving inward and disassembling, there is a question as to how actin-binding proteins and other components are transported to the leading edge and how nascent adhesions are stabilized. Active transport could play a significant role in these functions but the components involved are unknown. We show here that Myosin 1E (a long tailed Myosin 1 isoform) rapidly moves to the tips of active lamellipodia and to actin-rich early adhesions, unlike Myosin 1G, 1B or 1C (short tailed isoforms). Myosin 1E co-localizes with CARMIL, FHOD1, Arp3 and β3-integrin in those early adhesions. But these structures precede stable paxillin-rich adhesions. Myosin 1E movement depends upon actin-binding domains and the presence of an SH3 oligomerization domain. Overexpression of a Myosin 1E deletion mutant without the extreme C-terminal interacting (SH3) domain (Myosin 1EΔSH3) increases edge fluctuations and decreases stable adhesion lifetimes. In contrast, overexpression of Myosin 1E full tail domain (TH1+TH2+TH3/SH3) decreases edge fluctuation. In Myosin 1E knockdown cells, and more prominently in cells treated with Myosin 1 inhibitor, cell-matrix adhesions are also short-lived and fail to mature. We suggest that, by moving to actin polymerization sites and early adhesion sites in active lamellipodia, Myosin 1E might play important roles in transporting not only important polymerizing proteins but also proteins involved in adhesion stabilization.
Persistent Identifierhttp://hdl.handle.net/10722/202258
ISSN
2015 Impact Factor: 2.135
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorGupta, P-
dc.contributor.authorGauthier, NC-
dc.contributor.authorYu, C-
dc.contributor.authorYuan, Z-
dc.contributor.authorPontes, B-
dc.contributor.authorOhmstede, M-
dc.contributor.authorMartin, R-
dc.contributor.authorKnölker, HJ-
dc.contributor.authorDöbereiner, HG-
dc.contributor.authorKrendel, M-
dc.contributor.authorSheetz, M-
dc.date.accessioned2014-09-01T01:44:40Z-
dc.date.available2014-09-01T01:44:40Z-
dc.date.issued2013-
dc.identifier.citationBiology Open, 2013, v. 2 n. 12, p. 1288-1299-
dc.identifier.issn2046-6390-
dc.identifier.urihttp://hdl.handle.net/10722/202258-
dc.description.abstractBecause the actin network in active lamellipodia is continuously assembling at the edge, moving inward and disassembling, there is a question as to how actin-binding proteins and other components are transported to the leading edge and how nascent adhesions are stabilized. Active transport could play a significant role in these functions but the components involved are unknown. We show here that Myosin 1E (a long tailed Myosin 1 isoform) rapidly moves to the tips of active lamellipodia and to actin-rich early adhesions, unlike Myosin 1G, 1B or 1C (short tailed isoforms). Myosin 1E co-localizes with CARMIL, FHOD1, Arp3 and β3-integrin in those early adhesions. But these structures precede stable paxillin-rich adhesions. Myosin 1E movement depends upon actin-binding domains and the presence of an SH3 oligomerization domain. Overexpression of a Myosin 1E deletion mutant without the extreme C-terminal interacting (SH3) domain (Myosin 1EΔSH3) increases edge fluctuations and decreases stable adhesion lifetimes. In contrast, overexpression of Myosin 1E full tail domain (TH1+TH2+TH3/SH3) decreases edge fluctuation. In Myosin 1E knockdown cells, and more prominently in cells treated with Myosin 1 inhibitor, cell-matrix adhesions are also short-lived and fail to mature. We suggest that, by moving to actin polymerization sites and early adhesion sites in active lamellipodia, Myosin 1E might play important roles in transporting not only important polymerizing proteins but also proteins involved in adhesion stabilization.-
dc.languageeng-
dc.publisherThe Company of Biologists Ltd..-
dc.relation.ispartofBiology Open-
dc.subjectCell–matrix adhesion-
dc.subjectMyosin 1E-
dc.subjectTransport-
dc.titleMyosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formationen_US
dc.typeArticleen_US
dc.identifier.emailYu, C: chyu1@hku.hk-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1242/​bio.20135827-
dc.identifier.pmid24337113-
dc.identifier.pmcidPMC3863413-
dc.identifier.volume2-
dc.identifier.issue12-
dc.identifier.spage1288-
dc.identifier.epage1299-
dc.publisher.placeUnited Kingdom-

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