IRSp53 mediates podosome formation via VASP in NIH-Src cells.

Podosomes are cellular "feet," characterized by F-actin-rich membrane protrusions, which drive cell migration and invasion into the extracellular matrix. Small GTPases that regulate the actin cytoskeleton, such as Cdc42 and Rac are central regulators of podosome formation. The adaptor prot...

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Autores principales:	Tsukasa Oikawa, Hitomi Okamura, Franziska Dietrich, Yosuke Senju, Tadaomi Takenawa, Shiro Suetsugu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c4391e489ed84242bae46b73f36a5be2
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spelling	oai:doaj.org-article:c4391e489ed84242bae46b73f36a5be22021-11-18T07:51:51ZIRSp53 mediates podosome formation via VASP in NIH-Src cells.1932-620310.1371/journal.pone.0060528https://doaj.org/article/c4391e489ed84242bae46b73f36a5be22013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23555988/?tool=EBIhttps://doaj.org/toc/1932-6203Podosomes are cellular "feet," characterized by F-actin-rich membrane protrusions, which drive cell migration and invasion into the extracellular matrix. Small GTPases that regulate the actin cytoskeleton, such as Cdc42 and Rac are central regulators of podosome formation. The adaptor protein IRSp53 contains an I-BAR domain that deforms membranes into protrusions and binds to Rac, a CRIB motif that interacts with Cdc42, an SH3 domain that binds to many actin cytoskeletal regulators with proline-rich peptides including VASP, and the C-terminal variable region by splicing. However, the role of IRSp53 and VASP in podosome formation had been unclear. Here we found that the knockdown of IRSp53 by RNAi attenuates podosome formation and migration in Src-transformed NIH3T3 (NIH-Src) cells. Importantly, the differences in the IRSp53 C-terminal splicing isoforms did not affect podosome formation. Overexpression of IRSp53 deletion mutants suggested the importance of linking small GTPases to SH3 binding partners. Interestingly, VASP physically interacted with IRSp53 in NIH-Src cells and was essential for podosome formation. These data highlight the role of IRSp53 as a linker of small GTPases to VASP for podosome formation.Tsukasa OikawaHitomi OkamuraFranziska DietrichYosuke SenjuTadaomi TakenawaShiro SuetsuguPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 3, p e60528 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tsukasa Oikawa Hitomi Okamura Franziska Dietrich Yosuke Senju Tadaomi Takenawa Shiro Suetsugu IRSp53 mediates podosome formation via VASP in NIH-Src cells.
description	Podosomes are cellular "feet," characterized by F-actin-rich membrane protrusions, which drive cell migration and invasion into the extracellular matrix. Small GTPases that regulate the actin cytoskeleton, such as Cdc42 and Rac are central regulators of podosome formation. The adaptor protein IRSp53 contains an I-BAR domain that deforms membranes into protrusions and binds to Rac, a CRIB motif that interacts with Cdc42, an SH3 domain that binds to many actin cytoskeletal regulators with proline-rich peptides including VASP, and the C-terminal variable region by splicing. However, the role of IRSp53 and VASP in podosome formation had been unclear. Here we found that the knockdown of IRSp53 by RNAi attenuates podosome formation and migration in Src-transformed NIH3T3 (NIH-Src) cells. Importantly, the differences in the IRSp53 C-terminal splicing isoforms did not affect podosome formation. Overexpression of IRSp53 deletion mutants suggested the importance of linking small GTPases to SH3 binding partners. Interestingly, VASP physically interacted with IRSp53 in NIH-Src cells and was essential for podosome formation. These data highlight the role of IRSp53 as a linker of small GTPases to VASP for podosome formation.
format	article
author	Tsukasa Oikawa Hitomi Okamura Franziska Dietrich Yosuke Senju Tadaomi Takenawa Shiro Suetsugu
author_facet	Tsukasa Oikawa Hitomi Okamura Franziska Dietrich Yosuke Senju Tadaomi Takenawa Shiro Suetsugu
author_sort	Tsukasa Oikawa
title	IRSp53 mediates podosome formation via VASP in NIH-Src cells.
title_short	IRSp53 mediates podosome formation via VASP in NIH-Src cells.
title_full	IRSp53 mediates podosome formation via VASP in NIH-Src cells.
title_fullStr	IRSp53 mediates podosome formation via VASP in NIH-Src cells.
title_full_unstemmed	IRSp53 mediates podosome formation via VASP in NIH-Src cells.
title_sort	irsp53 mediates podosome formation via vasp in nih-src cells.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/c4391e489ed84242bae46b73f36a5be2
work_keys_str_mv	AT tsukasaoikawa irsp53mediatespodosomeformationviavaspinnihsrccells AT hitomiokamura irsp53mediatespodosomeformationviavaspinnihsrccells AT franziskadietrich irsp53mediatespodosomeformationviavaspinnihsrccells AT yosukesenju irsp53mediatespodosomeformationviavaspinnihsrccells AT tadaomitakenawa irsp53mediatespodosomeformationviavaspinnihsrccells AT shirosuetsugu irsp53mediatespodosomeformationviavaspinnihsrccells
_version_	1718422879456985088

IRSp53 mediates podosome formation via VASP in NIH-Src cells.

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