LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2

Phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulates at the leading edge of migrating cells and works, at least partially, as both a compass to indicate directionality and a hub for subsequent intracellular events. However, how PtdIns(3,4,5)P3 regulates the migratory machinery has n...

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Main Authors:	Takabayashi, Tetsuji, Xie, Min-Jue, Takeuchi, Seiji, Kawasaki, Motomi, Yagi, Hideshi, Okamoto, Masayuki, Rahman, Mohammad Tariqur, Malik, Fawzia, Kuroda, Kazuki, Kubota, Chikara, Fujieda, Shigeharu, Nagano, Takashi, Sato, Makoto
Format:	Article
Language:	English
Published:	American Society for Biochemistry and Molecular Biology Inc. 2010
Subjects:	RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry
Online Access:	http://irep.iium.edu.my/12444/ http://irep.iium.edu.my/12444/ http://irep.iium.edu.my/12444/ http://irep.iium.edu.my/12444/1/LL5B_Direct_the_translocation_of_filamin_A_sites.pdf

id	iium-12444
recordtype	eprints
spelling	iium-124442011-12-23T11:01:50Z http://irep.iium.edu.my/12444/ LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2 Takabayashi, Tetsuji Xie, Min-Jue Takeuchi, Seiji Kawasaki, Motomi Yagi, Hideshi Okamoto, Masayuki Rahman, Mohammad Tariqur Malik, Fawzia Kuroda, Kazuki Kubota, Chikara Fujieda, Shigeharu Nagano, Takashi Sato, Makoto RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry Phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulates at the leading edge of migrating cells and works, at least partially, as both a compass to indicate directionality and a hub for subsequent intracellular events. However, how PtdIns(3,4,5)P3 regulates the migratory machinery has not been fully elucidated. Here, we demonstrate a novel mechanism for efficient lamellipodium formation that depends on PtdIns(3,4,5)P3 and the reciprocal regulation of PtdIns(3,4,5)P3 itself. LL5β, whose subcellular localization is directed by membrane PtdIns(3,4,5)P3, recruits the actin-cross-linking protein Filamin A to the plasma membrane, where PtdIns(3,4,5)P3 accumulates, with the Filamin A-binding Src homology 2 domain-containing inositol polyphosphate 5-phosphatase 2 (SHIP2). A large and dynamic lamellipodium was formed in the presence of Filamin A and LL5β by the application of epidermal growth factor. Conversely, depletion of either Filamin A or LL5β or the overexpression of either an F-actin-cross-linking mutant of Filamin A or a mutant of LL5β without its PtdIns(3,4,5)P3-interacting region inhibited such events in COS-7 cells. Because F-actin initially polymerizes near the plasma membrane, it is likely that membrane-recruited Filamin A efficiently cross-links newly polymerized F-actin, leading to enhanced lamellipodium formation at the site of PtdIns(3,4,5)P3 accumulation. Moreover, we demonstrate that co-recruited SHIP2 dephosphorylates PtdIns(3,4,5)P3 at the same location. American Society for Biochemistry and Molecular Biology Inc. 2010 Article PeerReviewed application/pdf en http://irep.iium.edu.my/12444/1/LL5B_Direct_the_translocation_of_filamin_A_sites.pdf Takabayashi, Tetsuji and Xie, Min-Jue and Takeuchi, Seiji and Kawasaki, Motomi and Yagi, Hideshi and Okamoto, Masayuki and Rahman, Mohammad Tariqur and Malik, Fawzia and Kuroda, Kazuki and Kubota, Chikara and Fujieda, Shigeharu and Nagano, Takashi and Sato, Makoto (2010) LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2. Journal of Biological Chemistry, 285 (21). pp. 16155-16165. ISSN 0021-9258 (P), 1083-351X (O) http://dx.doi.org/10.1074/jbc.M109.081901 10.1074/jbc.M109.081901
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry
spellingShingle	RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry Takabayashi, Tetsuji Xie, Min-Jue Takeuchi, Seiji Kawasaki, Motomi Yagi, Hideshi Okamoto, Masayuki Rahman, Mohammad Tariqur Malik, Fawzia Kuroda, Kazuki Kubota, Chikara Fujieda, Shigeharu Nagano, Takashi Sato, Makoto LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2
description	Phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulates at the leading edge of migrating cells and works, at least partially, as both a compass to indicate directionality and a hub for subsequent intracellular events. However, how PtdIns(3,4,5)P3 regulates the migratory machinery has not been fully elucidated. Here, we demonstrate a novel mechanism for efficient lamellipodium formation that depends on PtdIns(3,4,5)P3 and the reciprocal regulation of PtdIns(3,4,5)P3 itself. LL5β, whose subcellular localization is directed by membrane PtdIns(3,4,5)P3, recruits the actin-cross-linking protein Filamin A to the plasma membrane, where PtdIns(3,4,5)P3 accumulates, with the Filamin A-binding Src homology 2 domain-containing inositol polyphosphate 5-phosphatase 2 (SHIP2). A large and dynamic lamellipodium was formed in the presence of Filamin A and LL5β by the application of epidermal growth factor. Conversely, depletion of either Filamin A or LL5β or the overexpression of either an F-actin-cross-linking mutant of Filamin A or a mutant of LL5β without its PtdIns(3,4,5)P3-interacting region inhibited such events in COS-7 cells. Because F-actin initially polymerizes near the plasma membrane, it is likely that membrane-recruited Filamin A efficiently cross-links newly polymerized F-actin, leading to enhanced lamellipodium formation at the site of PtdIns(3,4,5)P3 accumulation. Moreover, we demonstrate that co-recruited SHIP2 dephosphorylates PtdIns(3,4,5)P3 at the same location.
format	Article
author	Takabayashi, Tetsuji Xie, Min-Jue Takeuchi, Seiji Kawasaki, Motomi Yagi, Hideshi Okamoto, Masayuki Rahman, Mohammad Tariqur Malik, Fawzia Kuroda, Kazuki Kubota, Chikara Fujieda, Shigeharu Nagano, Takashi Sato, Makoto
author_facet	Takabayashi, Tetsuji Xie, Min-Jue Takeuchi, Seiji Kawasaki, Motomi Yagi, Hideshi Okamoto, Masayuki Rahman, Mohammad Tariqur Malik, Fawzia Kuroda, Kazuki Kubota, Chikara Fujieda, Shigeharu Nagano, Takashi Sato, Makoto
author_sort	Takabayashi, Tetsuji
title	LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2
title_short	LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2
title_full	LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2
title_fullStr	LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2
title_full_unstemmed	LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2
title_sort	ll5 directs the translocation of filamin a and ship2 to sites of phosphatidylinositol 3,4,5-triphosphate (ptdins(3,4,5)p3) accumulation, and ptdins(3,4,5)p3 localization is mutually modified by co-recruited ship2
publisher	American Society for Biochemistry and Molecular Biology Inc.
publishDate	2010
url	http://irep.iium.edu.my/12444/ http://irep.iium.edu.my/12444/ http://irep.iium.edu.my/12444/ http://irep.iium.edu.my/12444/1/LL5B_Direct_the_translocation_of_filamin_A_sites.pdf
first_indexed	2023-09-18T20:21:39Z
last_indexed	2023-09-18T20:21:39Z
_version_	1777408146862505984

LL5 directs the translocation of Filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2

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