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Cited by 66Protein Kinase Regulation and GTPase SignalingCellular transport and secretionCellular Mechanics and Interactions

Phosphoinositides in the regulation of actin cortex and cell migration

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Tsujita, Kazuya, Itoh, Toshiki·2015·Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
DOI 10.1016/j.bbalip.2014.10.011
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Abstract

In order for the cell to function well within a multicellular system, the mechanical properties of the plasma membrane need to meet two different requirements: cell shape maintenance and rearrangement. To achieve these goals, phosphoinositides play key roles in the regulation of the cortical actin cytoskeleton. PI(4,5)P₂is the most abundant phosphoinositide species in the plasma membrane. It maintains cell shape by linking the actin cortex to the membrane via interactions with Ezrin/Radixin/Moesin (ERM) proteins and class I myosins. Although the role of D3-phosphoinositides, such as PI(3,4,5)P₃, in actin-driven cell migration has been a subject of controversy, it becomes evident that the dynamic turnover of the phosphoinositide by the action of metabolizing enzymes, such as 5-phosphatases, is necessary. Recent studies have revealed an important role of PI(3,4)P₂in podosome/invadopodia formation, shedding new light on the actin-based organization of membrane structures regulated by phosphoinositide signaling. This article is part of a Special Issue entitled Phosphoinositides.

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  • Class I myosin family proteins are recruited to the membrane by PI(4,5)P2.

    “Similar to the ERM proteins, class I myosins are also recruited to the membrane by PI(4,5)P2 [90].”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [90]

    Section 1.2 says class 1 myosins bind PI(4,5)P2 and that their plasma-membrane localization “appears to be mediated” by it, supporting the proposed mechanism. The same section says it is not known whether depleting PI(4,5)P2 causes myosins to leave the membrane, so the unqualified statement that PI(4,5)P2 recruits them is stronger than the review's conclusion. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

  • The actin cytoskeleton provides rigidity to cells and is attached to the plasma membrane by ERM proteins.

    “The actin cytoskeleton provides rigidity to the cells and is attached to the plasma membrane by Ezrin, Radixin and Moesin, collectively known as ERM proteins [89,90].”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [90]

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Research works printed but not linked: 41

  1. H.L. Yin, P.A. Janmey, Phosphoinositide regulation of the actin cytoskeleton, Annual review of physiology, 65 (2003) 761-789.
  2. Y. Wang, R.I. Litvinov, X. Chen, T.L. Bach, L. Lian, B.G. Petrich, S.J. Monkley, Y. Kanaho, D.R. Critchley, T. Sasaki, M.J. Birnbaum, J.W. Weisel, J. Hartwig, C.S. Abrams, Loss of PIP5KIgamma, unlike other PIP5KI isoforms, impairs the integrity of the membrane cytoskeleton in murine megakaryocytes, The Journal of clinical investigation, 118 (2008) 812-819.
  3. K. Hamada, T. Shimizu, T. Matsui, S. Tsukita, T. Hakoshima, Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain, The EMBO journal, 19 (2000) 4449-4462.
  4. B.T. Fievet, A. Gautreau, C. Roy, L. Del Maestro, P. Mangeat, D. Louvard, M. Arpin, Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin, The Journal of cell biology, 164 (2004) 653-659.
  5. C. Barret, C. Roy, P. Montcourrier, P. Mangeat, V. Niggli, Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP(2)) binding site in the NH(2)-terminal domain of ezrin correlates with its altered cellular distribution, The Journal of cell biology, 151 (2000) 1067-1080.
  6. D. Raucher, M.P. Sheetz, Cell spreading and lamellipodial extension rate is regulated by membrane tension, The Journal of cell biology, 148 (2000) 127-136.
  7. S.M. Hayden, J.S. Wolenski, M.S. Mooseker, Binding of brush border myosin I to phospholipid vesicles, The Journal of cell biology, 111 (1990) 443-451.
  8. D.E. Hokanson, E.M. Ostap, Myo1c binds tightly and specifically to phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate, Proceedings of the National Academy of Sciences of the United States of America, 103 (2006) 3118-3123.
  9. R. Nambiar, R.E. McConnell, M.J. Tyska, Control of cell membrane tension by myosin-I, Proceedings of the National Academy of Sciences of the United States of America, 106 (2009) 11972-11977.
  10. T. Golub, P. Caroni, PI(4,5)P2-dependent microdomain assemblies capture microtubules to promote and control leading edge motility, The Journal of cell biology, 169 (2005) 151-165.
  11. S. Choi, N. Thapa, A.C. Hedman, Z. Li, D.B. Sacks, R.A. Anderson, IQGAP1 is a novel phosphatidylinositol 4,5 bisphosphate effector in regulation of directional cell migration, The EMBO journal, 32 (2013) 2617-2630.
  12. R. Rohatgi, H.Y. Ho, M.W. Kirschner, Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate, The Journal of cell biology, 150 (2000) 1299-1310.
  13. K. Takano, K. Toyooka, S. Suetsugu, EFC/F-BAR proteins and the N-WASP-WIP complex induce membrane curvature-dependent actin polymerization, The EMBO journal, 27 (2008) 2817-2828.
  14. C. Le Clainche, D. Schlaepfer, A. Ferrari, M. Klingauf, K. Grohmanova, A. Veligodskiy, D. Didry, D. Le, C. Egile, M.F. Carlier, R. Kroschewski, IQGAP1 stimulates actin assembly through the N-WASP-Arp2/3 pathway, The Journal of biological chemistry, 282 (2007) 426-435.
  15. Y. Sun, K. Ling, M.P. Wagoner, R.A. Anderson, Type I gamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration, The Journal of cell biology, 178 (2007) 297-308.
  16. R.A. Lacalle, R.M. Peregil, J.P. Albar, E. Merino, A.C. Martinez, I. Merida, S. Manes, Type I phosphatidylinositol 4-phosphate 5-kinase controls neutrophil polarity and directional movement, The Journal of cell biology, 179 (2007) 1539-1553.
  17. J.M. Serrador, J.L. Alonso-Lebrero, M.A. del Pozo, H. Furthmayr, R. Schwartz-Albiez, J. Calvo, F. Lozano, F. Sanchez-Madrid, Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization, The Journal of cell biology, 138 (1997) 1409-1423.
  18. J.H. Lee, T. Katakai, T. Hara, H. Gonda, M. Sugai, A. Shimizu, Roles of p-ERM and Rho-ROCK signaling in lymphocyte polarity and uropod formation, The Journal of cell biology, 167 (2004) 327-337.
  19. A.B. Jaffe, A. Hall, Rho GTPases: biochemistry and biology, Annual review of cell and developmental biology, 21 (2005) 247-269.
  20. D. Wessels, D.F. Lusche, S. Kuhl, P. Heid, D.R. Soll, PTEN plays a role in the suppression of lateral pseudopod formation during Dictyostelium motility and chemotaxis, Journal of cell science, 120 (2007) 2517-2531.
  21. J. van Rheenen, X. Song, W. van Roosmalen, M. Cammer, X. Chen, V. Desmarais, S.C. Yip, J.M. Backer, R.J. Eddy, J.S. Condeelis, EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells, The Journal of cell biology, 179 (2007) 1247-1259.
  22. K. Tsujita, T. Itoh, A. Kondo, M. Oyama, H. Kozuka-Hata, Y. Irino, J. Hasegawa, T. Takenawa, Proteome of acidic phospholipid-binding proteins: spatial and temporal regulation of Coronin 1A by phosphoinositides, The Journal of biological chemistry, 285 (2010) 6781-6789.
  23. R. Samaniego, L. Sanchez-Martin, A. Estecha, P. Sanchez-Mateos, Rho/ROCK and myosin II control the polarized distribution of endocytic clathrin structures at the uropod of moving T lymphocytes, Journal of cell science, 120 (2007) 3534-3543.
  24. R. Meili, C. Ellsworth, S. Lee, T.B. Reddy, H. Ma, R.A. Firtel, Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium, The EMBO journal, 18 (1999) 2092-2105.
  25. J.M. Haugh, F. Codazzi, M. Teruel, T. Meyer, Spatial sensing in fibroblasts mediated by 3' phosphoinositides, The Journal of cell biology, 151 (2000) 1269-1280.
  26. S. Funamoto, K. Milan, R. Meili, R.A. Firtel, Role of phosphatidylinositol 3' kinase and a downstream pleckstrin homology domain-containing protein in controlling chemotaxis in dictyostelium, The Journal of cell biology, 153 (2001) 795-810.
  27. Y. Kunisaki, A. Nishikimi, Y. Tanaka, R. Takii, M. Noda, A. Inayoshi, K. Watanabe, F. Sanematsu, T. Sasazuki, T. Sasaki, Y. Fukui, DOCK2 is a Rac activator that regulates motility and polarity during neutrophil chemotaxis, The Journal of cell biology, 174 (2006) 647-652.
  28. E.S. Welf, S. Ahmed, H.E. Johnson, A.T. Melvin, J.M. Haugh, Migrating fibroblasts reorient directionality by a metastable, PI3K-dependent mechanism, The Journal of cell biology, 197 (2012) 105-114.
  29. T. Shibata, M. Nishikawa, S. Matsuoka, M. Ueda, Modeling the self-organized phosphatidylinositol lipid signaling system in chemotactic cells using quantitative image analysis, Journal of cell science, 125 (2012) 5138-5150.
  30. Y. Arai, T. Shibata, S. Matsuoka, M.J. Sato, T. Yanagida, M. Ueda, Self-organization of the phosphatidylinositol lipids signaling system for random cell migration, Proceedings of the National Academy of Sciences of the United States of America, 107 (2010) 12399-12404.
  31. S. Dowler, R.A. Currie, D.G. Campbell, M. Deak, G. Kular, C.P. Downes, D.R. Alessi, Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities, The Biochemical journal, 351 (2000) 19-31.
  32. A. Hogan, Y. Yakubchyk, J. Chabot, C. Obagi, E. Daher, K. Maekawa, S.H. Gee, The phosphoinositol 3,4-bisphosphate-binding protein TAPP1 interacts with syntrophins and regulates actin cytoskeletal organization, The Journal of biological chemistry, 279 (2004) 53717-53724.
  33. J. Hasegawa, E. Tokuda, T. Tenno, K. Tsujita, H. Sawai, H. Hiroaki, T. Takenawa, T. Itoh, SH3YL1 regulates dorsal ruffle formation by a novel phosphoinositide-binding domain, The Journal of cell biology, 193 (2011) 901-916.
  34. W.A. Kimber, L. Trinkle-Mulcahy, P.C. Cheung, M. Deak, L.J. Marsden, A. Kieloch, S. Watt, R.T. Javier, A. Gray, C.P. Downes, J.M. Lucocq, D.R. Alessi, Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein MUPP1 in vivo, The Biochemical journal, 361 (2002) 525-536.
  35. W.A. Kimber, M. Deak, A.R. Prescott, D.R. Alessi, Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1, The Biochemical journal, 376 (2003) 525-535.
  36. M. Krause, E.W. Dent, J.E. Bear, J.J. Loureiro, F.B. Gertler, Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration, Annual review of cell and developmental biology, 19 (2003) 541-564.
  37. E.M. Lafuente, A.A. van Puijenbroek, M. Krause, C.V. Carman, G.J. Freeman, A. Berezovskaya, E. Constantine, T.A. Springer, F.B. Gertler, V.A. Boussiotis, RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion, Developmental cell, 7 (2004) 585-595.
  38. A.L. Law, A. Vehlow, M. Kotini, L. Dodgson, D. Soong, E. Theveneau, C. Bodo, E. Taylor, C. Navarro, U. Perera, M. Michael, G.A. Dunn, D. Bennett, R. Mayor, M. Krause, Lamellipodin and the Scar/WAVE complex cooperate to promote cell migration in vivo, The Journal of cell biology, 203 (2013) 673-689.
  39. Y.H. Bae, Z. Ding, T. Das, A. Wells, F. Gertler, P. Roy, Profilin1 regulates PI(3,4)P2 and lamellipodin accumulation at the leading edge thus influencing motility of MDA-MB-231 cells, Proceedings of the National Academy of Sciences of the United States of America, 107 (2010) 21547-21552.
  40. T. Oikawa, T. Itoh, T. Takenawa, Sequential signals toward podosome formation in NIH-src cells, The Journal of cell biology, 182 (2008) 157-169.
  41. P. Lock, C.L. Abram, T. Gibson, S.A. Courtneidge, A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate, The EMBO journal, 17 (1998) 4346-4357.

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Authors
Tsujita, K., & Itoh, T.
Affiliations
Biosignal Research Center, Kobe University (JP)
Corresponding author
  • Tsujita, Kazuya
  • Itoh, Toshiki
ORCID
Venue
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
Publisher
Elsevier BV
Published
2015-06
Volume
1851
Issue
6
Pages
824-831
ISSN
1388-1981 (ISSN-L)
DOI
10.1016/j.bbalip.2014.10.011
OpenAlex
W2034584476
Cited by
66
References
1
Citations by year
2026: 4 · 2025: 3 · 2024: 3 · 2023: 4 · 2022: 7 · 2021: 6 · 2020: 5 · 2019: 6 · 2018: 5 · 2017: 4 · 2016: 15 · 2015: 4
FWCI
0.73
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (publishedVersion)
  • PubMed (publishedVersion)
  • Institutional Repositories DataBase (IRDB) (submittedVersion)
  • Kobe University Repository Kernel (Kobe University) (submittedVersion, cc-by-nc-nd)
Funders
  • Japan Society for the Promotion of Science (25440085, 24570216)
  • Ministry of Education, Culture, Sports, Science, and Technology (24113715)
  • Uehara Memorial Foundation
  • Hyogo Science and Technology Association
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
phosphoinositides, actin cortex, cell migration, phosphatidylinositol 4,5-bisphosphate, ERM proteins, class I myosin, phosphatidylinositol 3,4,5-trisphosphate, PI(3,4)P2, podosomes, invadopodia, plasma membrane mechanics, cell shape
MeSH terms
Inositol Polyphosphate 5-Phosphatases, Ezrin, Cell Membrane, Cell Movement, Cytoskeletal Proteins, Gene Expression Regulation, Humans, Membrane Proteins, Microfilament Proteins, Actin Cytoskeleton, Myosins, Phosphatidylinositols, Phosphoric Monoester Hydrolases, Signal Transduction, Phosphatidylinositol 3-Kinases, Cell Shape, PTEN Phosphohydrolase

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