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

Prabuddha Gupta, Nils C. Gauthier, Yu Cheng-Han, Yuan Zuanning, Bruno Pontes, Malte Ohmstede, René Martin, Hans Joachim Knölker, Hans Günther Döbereiner, Mira Krendel, Michael Sheetz

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Because 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 actinrich early adhesions, unlike Myosin 1G, 1B or 1C (short tailed isoforms). Myosin 1E co-localizes with CARMIL, FHOD1, Arp3 and b3-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 1EDSH3) 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.

Original languageEnglish (US)
Pages (from-to)1-12
Number of pages12
JournalBiology Open
Volume2
Issue number12
DOIs
StatePublished - Jan 1 2013
Externally publishedYes

Fingerprint

pseudopodia
Pseudopodia
Myosins
myosin
Polymerization
polymerization
actin
adhesion
Actins
Adhesion
src Homology Domains
microfilament proteins
Protein Isoforms
Cell-Matrix Junctions
Paxillin
Microfilament Proteins
Oligomerization
active transport
Active Biological Transport
integrins

Keywords

  • Cell-matrix adhesion
  • Myosin 1E
  • Transport

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Cite this

Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation. / Gupta, Prabuddha; Gauthier, Nils C.; Cheng-Han, Yu; Zuanning, Yuan; Pontes, Bruno; Ohmstede, Malte; Martin, René; Knölker, Hans Joachim; Döbereiner, Hans Günther; Krendel, Mira; Sheetz, Michael.

In: Biology Open, Vol. 2, No. 12, 01.01.2013, p. 1-12.

Research output: Contribution to journalArticle

Gupta, P, Gauthier, NC, Cheng-Han, Y, Zuanning, Y, Pontes, B, Ohmstede, M, Martin, R, Knölker, HJ, Döbereiner, HG, Krendel, M & Sheetz, M 2013, 'Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation', Biology Open, vol. 2, no. 12, pp. 1-12. https://doi.org/10.1242/bio.20135827
Gupta, Prabuddha ; Gauthier, Nils C. ; Cheng-Han, Yu ; Zuanning, Yuan ; Pontes, Bruno ; Ohmstede, Malte ; Martin, René ; Knölker, Hans Joachim ; Döbereiner, Hans Günther ; Krendel, Mira ; Sheetz, Michael. / Myosin 1E localizes to actin polymerization sites in lamellipodia, affecting actin dynamics and adhesion formation. In: Biology Open. 2013 ; Vol. 2, No. 12. pp. 1-12.
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AU - Pontes, Bruno

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AU - Martin, René

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