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Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading

We previously reported a novel interaction between v-Crk and myosin-1c, and demonstrated that this interaction is essential for cell migration, even in the absence of p130CAS. We here demonstrate a role for Crk-myosin-1c interaction in cell adhesion and spreading. Crk-knockout (Crk(‑/‑)) mouse embry...

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Autores principales: Oh, Hyejin, Kim, Hwan, Shin, Baehyun, Lee, Kun Ho, Yeo, Myeong Gu, Song, Woo Keun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753442/
https://www.ncbi.nlm.nih.gov/pubmed/23983611
http://dx.doi.org/10.7150/ijbs.6459
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author Oh, Hyejin
Kim, Hwan
Shin, Baehyun
Lee, Kun Ho
Yeo, Myeong Gu
Song, Woo Keun
author_facet Oh, Hyejin
Kim, Hwan
Shin, Baehyun
Lee, Kun Ho
Yeo, Myeong Gu
Song, Woo Keun
author_sort Oh, Hyejin
collection PubMed
description We previously reported a novel interaction between v-Crk and myosin-1c, and demonstrated that this interaction is essential for cell migration, even in the absence of p130CAS. We here demonstrate a role for Crk-myosin-1c interaction in cell adhesion and spreading. Crk-knockout (Crk(‑/‑)) mouse embryo fibroblasts (MEFs) exhibited significantly decreased cell spreading and reduced Rac1 activity. A stroboscopic analysis of cell dynamics during cell spreading revealed that the cell-spreading deficiency in Crk(‑/‑) MEFs was due to the short protrusion/retraction distances and long persistence times of membrane extensions. The low activity of Rac1 in Crk(‑/‑) MEFs, which led to delayed cell spreading in these cells, is consistent with the observed defects in membrane dynamics. Reintroduction of v-Crk into Crk(‑/‑) MEFs rescued these defects, restoring cell-spreading activity and membrane dynamics to Crk(+/+) MEF levels, and normalizing Rac1 activity. Knockdown of myosin-1c by introduction of small interfering RNA resulted in a delay in cell spreading and reduced Rac1 activity to low levels, suggesting that myosin-1c also plays an essential role in cell adhesion and spreading. In addition, deletion of the v-Crk SH3 domain, which interacts with the myosin-1c tail, led to defects in cell spreading. Overexpression of the GFP-myosin-1c tail domain effectively inhibited the v-Crk-myosin-1c interaction and led to a slight decrease in cell spreading and cell surface area. Collectively, these findings suggest that the v-Crk-myosin-1c interaction, which modulates membrane dynamics by regulating Rac1 activity, is crucial for cell adhesion and spreading.
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spelling pubmed-37534422013-08-27 Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading Oh, Hyejin Kim, Hwan Shin, Baehyun Lee, Kun Ho Yeo, Myeong Gu Song, Woo Keun Int J Biol Sci Research Paper We previously reported a novel interaction between v-Crk and myosin-1c, and demonstrated that this interaction is essential for cell migration, even in the absence of p130CAS. We here demonstrate a role for Crk-myosin-1c interaction in cell adhesion and spreading. Crk-knockout (Crk(‑/‑)) mouse embryo fibroblasts (MEFs) exhibited significantly decreased cell spreading and reduced Rac1 activity. A stroboscopic analysis of cell dynamics during cell spreading revealed that the cell-spreading deficiency in Crk(‑/‑) MEFs was due to the short protrusion/retraction distances and long persistence times of membrane extensions. The low activity of Rac1 in Crk(‑/‑) MEFs, which led to delayed cell spreading in these cells, is consistent with the observed defects in membrane dynamics. Reintroduction of v-Crk into Crk(‑/‑) MEFs rescued these defects, restoring cell-spreading activity and membrane dynamics to Crk(+/+) MEF levels, and normalizing Rac1 activity. Knockdown of myosin-1c by introduction of small interfering RNA resulted in a delay in cell spreading and reduced Rac1 activity to low levels, suggesting that myosin-1c also plays an essential role in cell adhesion and spreading. In addition, deletion of the v-Crk SH3 domain, which interacts with the myosin-1c tail, led to defects in cell spreading. Overexpression of the GFP-myosin-1c tail domain effectively inhibited the v-Crk-myosin-1c interaction and led to a slight decrease in cell spreading and cell surface area. Collectively, these findings suggest that the v-Crk-myosin-1c interaction, which modulates membrane dynamics by regulating Rac1 activity, is crucial for cell adhesion and spreading. Ivyspring International Publisher 2013-08-15 /pmc/articles/PMC3753442/ /pubmed/23983611 http://dx.doi.org/10.7150/ijbs.6459 Text en © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.
spellingShingle Research Paper
Oh, Hyejin
Kim, Hwan
Shin, Baehyun
Lee, Kun Ho
Yeo, Myeong Gu
Song, Woo Keun
Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading
title Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading
title_full Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading
title_fullStr Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading
title_full_unstemmed Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading
title_short Interaction of Crk with Myosin-1c Participates in Fibronectin-Induced Cell Spreading
title_sort interaction of crk with myosin-1c participates in fibronectin-induced cell spreading
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753442/
https://www.ncbi.nlm.nih.gov/pubmed/23983611
http://dx.doi.org/10.7150/ijbs.6459
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