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Angaben zur Quelle [Bearbeiten]

Autor     Juha Saarikangas, Hongxia Zhao, Pekka Lappalainen
Titel    Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides
Zeitschrift    Physiological Reviews
Ausgabe    90
Datum    1. Januar 2010
Nummer    1
Seiten    259-289
DOI    10.1152/physrev.00036.2009
URL    http://physrev.physiology.org/content/90/1/259.full-text.pdf+html

Literaturverz.   

ja
Fußnoten    ja
Fragmente    3


Fragmente der Quelle:
[1.] Shg/Fragment 034 13 - Diskussion
Zuletzt bearbeitet: 2014-11-02 01:28:17 Hindemith
Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Saarikangas et al 2010, Schutzlevel sysop, Shg

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Seite: 34, Zeilen: 13-33
Quelle: Saarikangas et al 2010
Seite(n): 263, 270, Zeilen: 263: li.Sp. 51-52 - re.Sp. 1-17; 270: re.Sp. 26-28 - 271: li.Sp. 1 ff.
The organization and dynamics of the actin cytoskeleton are regulated by membrane phosphoinositides at several levels. First, many actin-binding proteins directly interact with phosphoinositides, which regulate the activity and/or subcellular localization of these proteins. Among different PIs, PIP2 is the best-characterized regulator of the actin cytoskeleton. PIP2 interacts directly with several actin-binding proteins and regulates their activities [Hilpela P, et al.2004, Sechi AS, Wehland J. 2000, Sheetz MP, et al. 2006, Yamaguchi H, et al. 2009]. Typically, PIP2 inhibits those actin-binding proteins that promote actin filament disassembly and activates proteins that induce actin filament assembly. Second, phosphoinositides control the subcellular localization of larger scaffolding proteins that are involved in the interplay between the actin cytoskeleton and plasma membrane or intracellular membrane organelles. Finally, proteins controlling the activity of Rho family small GTPases are in many cases regulated by plasma membrane phosphoinositides. The RhoA GTPase has a pronounced role in the formation and regulation of focal adhesion complexes and contractile actomyosin bundles such as stress fibers [Pelham RJ, et al. 1994]. RhoA induces actin polymerization at focal adhesions by activating the Dia1 formin and inhibits actin filament disassembly by initiating a signaling cascade that leads to phosphorylation and subsequent inactivation of the ADF/cofilin family of actin filament severing/depolymerizing proteins through the action of LIM kinases [Hotulainen P, Lappalainen P. 2006, Mahaffy [RE, Pollard TD. 2008, Watanabe N, et al. 1999, Vardouli et al 2005].]

Hilpela P, Vartiainen MK, Lappalainen P. (2004). Regulation of the actin cytoskeleton by PI(4,5)P2 and PI(3,4,5)P3. Curr Top Microbiol Immunol 282: 117–163.

Hotulainen P, Lappalainen P. (2006). Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173: 383–394.

Mahaffy RE, Pollard TD. (2008). Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry 47: 6460–6467.

Pelham RJ, Chang F. (2002). Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 419: 82–86.

Sechi AS, Wehland J. (2000).The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P2 influences cytoskeletal protein activity at the plasma membrane. J Cell Sci 113: 3685–3695.

Sheetz MP, Sable JE, Dobereiner HG. (2006). Continuous membrane-cytoskeleton adhesion requires continuous accommodation to lipid and cytoskeleton dynamics. Annu Rev Biophys Biomol Struct 35: 417–434.

Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S. (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1: 136–143.

Yamaguchi H, Shiraishi M, Fukami K, Tanabe A, Ikeda-Matsuo Y, Naito Y, Sasaki Y. (2009). MARCKS regulates lamellipodia formation induced by IGF-I via association with PIP2 and beta-actin at membrane microdomains. J Cell Physiol 220: 748–755.

[Seite 263]

II. REGULATION OF ACTIN DYNAMICS BY PHOSPHOINOSITIDES

The organization and dynamics of the actin cytoskeleton are regulated by membrane phosphoinositides at several levels. First, many actin-binding proteins directly interact with phosphoinositides, which regulate the activity and/or subcellular localization of these proteins. Second, phosphoinositides control the subcellular localization of larger scaffolding proteins that are involved in the interplay between the actin cytoskeleton and plasma membrane or intracellular membrane organelles. Finally, proteins controlling the activity of Rho family small GTPases are in many cases regulated by plasma membrane phosphoinositides.

Among different PIs, PI(4,5)P2 is the best-characterized regulator of the actin cytoskeleton. PI(4,5)P2 interacts directly with several actin-binding proteins and regulates their activities (23, 141, 330, 332, 397). Typically, PI(4,5)P2 inhibits those actin-binding proteins that promote actin filament disassembly and activates proteins that induce actin filament assembly.

[Seite 270]

A. Rho Family GTPases

The RhoA GTPase has a pronounced role in the formation and regulation of focal adhesion complexes and contractile actomyosin bundles such as stress fibers (288, 308). RhoA induces actin polymerization at focal adhesions by activating the Dia1 formin and inhibits actin filament disassembly by initiating a signaling cascade that leads to phosphorylation and subsequent inactivation of the ADF/cofilin family of actin filament severing/depolymerizing proteins through the action of LIM kinases (146, 230, 383).


23. Bittar EE. (Editor). Advances in Molecular and Cell Biology. New York: Elsevier, 2006.

141. Hilpela P, Vartiainen MK, Lappalainen P. Regulation of the actin cytoskeleton by PI(4,5)P2 and PI(3,4,5)P3. Curr Top Microbiol Immunol 282: 117–163, 2004.

146. Hotulainen P, Lappalainen P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173: 383–394, 2006.

230. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285: 895–898, 1999.

231. Mahaffy RE, Pollard TD. Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry 47: 6460–6467, 2008.

288. Pelham RJ, Chang F. Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 419: 82–86, 2002.

308. Ridley AJ, Hall A. Signal transduction pathways regulating Rhomediated stress fibre formation: requirement for a tyrosine kinase. EMBO J 13: 2600–2610, 1994.

330. Sechi AS, Wehland J. The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P2 influences cytoskeletal protein activity at the plasma membrane. J Cell Sci 113: 3685–3695, 2000.

332. Sheetz MP, Sable JE, Dobereiner HG. Continuous membrane-cytoskeleton adhesion requires continuous accommodation to lipid and cytoskeleton dynamics. Annu Rev Biophys Biomol Struct 35: 417–434, 2006.

383. Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1: 136–143, 1999.

397. Yamaguchi H, Shiraishi M, Fukami K, Tanabe A, Ikeda-Matsuo Y, Naito Y, Sasaki Y. MARCKS regulates lamellipodia formation induced by IGF-I via association with PIP2 and beta-actin at membrane microdomains. J Cell Physiol 220: 748–755, 2009.

Anmerkungen

Ohne Hinweis auf eine Übernahme.

Im Literaturverzeichnis von Shg findet sich keine Referenz für "Vardouli et al 2005". Beim Versuch, die Referenz [230] zu kopieren, hat sich Shg vertan und stattdessen die unter [231] stehende Referenz übernommen.

Sichter
(Graf Isolan), SleepyHollow02

[2.] Shg/Fragment 035 01 - Diskussion
Zuletzt bearbeitet: 2014-11-02 01:26:58 Hindemith
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Quelle: Saarikangas et al 2010
Seite(n): 271, Zeilen: li.Sp. 1-9
[RhoA induces actin polymerization at focal adhesions by activating the Dia1 formin and inhibits actin filament disassembly by initiating a signaling cascade that leads to phosphorylation and subsequent inactivation of the ADF/cofilin family of actin filament severing/depolymerizing proteins through the action of LIM kinases [Hotulainen P, Lappalainen P. 2006, Mahaffy] RE, Pollard TD. 2008, Watanabe N, et al. 1999, Vardouli et al 2005]. Furthermore, RhoA promotes contractility by activating the myosin light-chain kinase through ROCK kinase [Totsukawa G, et al. 2000].

Hotulainen P, Lappalainen P. (2006). Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173: 383–394.

Mahaffy RE, Pollard TD. (2008). Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry 47: 6460–6467.

Totsukawa G, Yamakita Y, Yamashiro S, Hartshorne DJ, Sasaki Y, Matsumura F. (2000). Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J Cell Biol 150: 797–806.

Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S. (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1: 136–143.

RhoA induces actin polymerization at focal adhesions by activating the Dia1 formin and inhibits actin filament disassembly by initiating a signaling cascade that leads to phosphorylation and subsequent inactivation of the ADF/cofilin family of actin filament severing/depolymerizing proteins through the action of LIM kinases (146, 230, 383). Furthermore, RhoA promotes contractility by activating the myosin light-chain kinase through ROCK kinase (364).

146. Hotulainen P, Lappalainen P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173: 383–394, 2006.

230. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285: 895–898, 1999.

231. Mahaffy RE, Pollard TD. Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry 47: 6460–6467, 2008.

364. Totsukawa G, Yamakita Y, Yamashiro S, Hartshorne DJ, Sasaki Y, Matsumura F. Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J Cell Biol 150: 797–806, 2000.

383. Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1: 136–143, 1999.

Anmerkungen

Ohne Hinweis auf eine Übernahme. Schließt die auf der vorangegangenen Seite begonnene Übernahme ab.

Im Literaturverzeichnis von Shg findet sich keine Referenz für "Vardouli et al 2005". Beim Versuch, die Referenz [230] zu kopieren, hat sich Shg vertan und stattdessen die unter [231] stehende Referenz übernommen.

Sichter
(Graf Isolan), SleepyHollow02

[3.] Shg/Fragment 080 02 - Diskussion
Zuletzt bearbeitet: 2014-11-01 12:36:34 SleepyHollow02
Fragment, Gesichtet, KeineWertung, SMWFragment, Saarikangas et al 2010, Schutzlevel, Shg

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Quelle: Saarikangas et al 2010
Seite(n): 259, Zeilen: 30-31
Polymerization of actin filaments against cellular membranes provides the force for a number of cellular processes such as migration, morphogenesis, and endocytosis [Saarikangas J, et al.2010].

Saarikangas J, Zhao H, Lappalainen P. (2010). Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol Rev. Jan;90(1):259-89.

Polymerization of actin filaments against cellular membranes provides the force for a number of cellular processes such as migration, morphogenesis, and endocytosis.
Anmerkungen

Art und Umfang der Übernahme bleiben ungekennzeichnet.

Sichter
(Graf Isolan), SleepyHollow02

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