CoChat
Sign Up
Cited by 1,419

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Membrane recognition by phospholipid-binding domains

Lemmon, Mark A.·2008·Nature Reviews Molecular Cell Biology
DOI 10.1038/nrm2328
Open this paper in CoChat — free account

Abstract

Many different globular domains bind to the surfaces of cellular membranes, or to specific phospholipid components in these membranes, and this binding is often tightly regulated. Examples include pleckstrin homology and C2 domains, which are among the largest domain families in the human proteome. Crystal structures, binding studies and analyses of subcellular localization have provided much insight into how members of this diverse group of domains bind to membranes, what features they recognize and how binding is controlled. A full appreciation of these processes is crucial for understanding how protein localization and membrane topography and trafficking are regulated in cells.

Overview

Integrity signals

Registry

Crossref · 10.1038/nrm2328

Cites

4 of 4 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 114

  1. Sheetz, M. P., Sable, J. E. & Dobereiner, H. G. Continuous membrane–cytoskeleton adhesion requires continuous accommodation to lipid and cytoskeleton dynamics. Annu. Rev. Biophys. Biomol. Struct. 35, 417–434 (2006). · DOI
  2. Di Paolo, G. & De Camilli, P. Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651–657 (2006). · DOI · Paper page
  3. Teruel, M. N. & Meyer, T. Translocation and reversible localization of signaling proteins: a dynamic future for signal transduction. Cell 103, 181–184 (2000). · DOI
  4. Behnia, R. & Munro, S. Organelle identity and the signposts for membrane traffic. Nature 438, 597–604 (2005). · DOI
  5. Stephens, L., McGregor, A. & Hawkins, P. in Biology of Phosphoinositides (ed. Cockcroft, S.) (Oxford Univ. Press, Oxford, UK, 2000).
  6. Colon-Gonzalez, F. & Kazanietz, M. G. C1 domains exposed: from diacylglycerol binding to protein–protein interactions. Biochim. Biophys. Acta 1761, 827–837 (2006). This review and references 11, 30, 39, 48, 62, 66 and 77 comprise a valuable set of recent reviews with more detail on each of the phospholipid-binding domains described here. · DOI · Paper page
  7. Lemmon, M. A. & Ferguson, K. M. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350, 1–18 (2000). · DOI
  8. Oancea, E., Teruel, M. N., Quest, A. F. & Meyer, T. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J. Cell Biol. 140, 485–498 (1998). · DOI
  9. Várnai, P. & Balla, T. Live cell imaging of phosphoinositide dynamics with fluorescent protein domains. Biochim. Biophys. Acta 1761, 957–967 (2006). · DOI
  10. Zhang, G., Kazanietz, M. G., Blumberg, P. M. & Hurley, J. H. Crystal structure of the Cys2 activator-binding domain of protein kinase Cδ in complex with phorbol ester. Cell 81, 917–924 (1995). One of the earliest structural views of how a specific membrane-targeting domain functions. · DOI
  11. Kazanietz, M. G., Barchi, J. J., Omichinski, J. G. & Blumberg, P. M. Low affinity binding of phorbol esters to protein kinase C and its recombinant cysteine-rich region in the absence of phospholipids J. Biol. Chem. 270, 14679–14684 (1995). · DOI
  12. Harlan, J. E., Hajduk, P. J., Yoon, H. S. & Fesik, S. W. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 371, 168–170 (1994). First report that some PH domains can bind phosphoinositides. · DOI
  13. Lemmon, M. A., Ferguson, K. M., O'Brien, R., Sigler, P. B. & Schlessinger, J. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl Acad. Sci. USA 92, 10472–10476 (1995). · DOI · Paper page
  14. Garcia, P. et al. The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes. Biochemistry 34, 16228–16234 (1995). · DOI
  15. Hirose, K., Kadowaki, S., Tanabe, M., Takeshima, H. & Iino, M. Spatiotemporal dynamics of inositol 1,4,5-trisphosphate that underlies complex Ca2+ mobilization patterns. Science 284, 1527–1530 (1999). · DOI
  16. Kavran, J. M. et al. Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains. J. Biol. Chem. 273, 30497–30508 (1998). · DOI · Paper page
  17. Ferguson, K. M., Lemmon, M. A., Schlessinger, J. & Sigler, P. B. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037–1046 (1995). First structural view of specific phosphoinositide binding by a protein domain. · DOI
  18. Flesch, F. M., Yu, J. W., Lemmon, M. A. & Burger, K. N. C. Membrane activity of the phospholipase C-δ1 pleckstrin homology (PH) domain. Biochem. J. 389, 435–441 (2005). · DOI
  19. Fukuda, M., Kojima, T., Kabayama, H. & Mikoshiba, K. Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J. Biol. Chem. 271, 30303–30306 (1996). · DOI
  20. Salim, K. et al. Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. EMBO J. 15, 6241–6250 (1996). · DOI
  21. Klarlund, J. K. et al. Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275, 1927–1930 (1997). · DOI
  22. Franke, T. F., Kaplan, D. R., Cantley, L. C. & Toker, A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275, 665–668 (1997). References 24 and 25 were instrumental in establishing PH domains as effector domains of PI3K signalling. · DOI
  23. Venkateswarlu, K., Oatey, P. B., Tavare, J. M. & Cullen, P. J. Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase. Curr. Biol. 8, 463–466 (1998). · DOI
  24. Lindvall, J. M. et al. Bruton's tyrosine kinase: cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling. Immunol. Rev. 203, 200–215 (2005). · DOI
  25. Carpten, J. D. et al. A transforming mutation in the pleckstrin homology domain of AKT1 in cancer. Nature 448, 439–444 (2007). Describes important pathological consequences of the promotion of aberrant membrane association by a PH domain. · DOI
  26. Huang, Y. H. et al. Positive regulation of Itk PH domain function by soluble IP4 . Science 316, 886–889 (2007). · DOI
  27. DiNitto, J. P. & Lambright, D. G. Membrane and juxtamembrane targeting by PH and PTB domains. Biochim. Biophys. Acta 1761, 850–867 (2006). · DOI
  28. Isakoff, S. J. et al. Identification and analysis of PH domain-containing targets of phosphatidylinositol 3-kinase using a novel in vivo assay in yeast. EMBO J. 17, 5374–5387 (1998). · DOI · Paper page
  29. Ferguson, K. M. et al. Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains. Mol. Cell 6, 373–384 (2000). · DOI
  30. Ceccarelli, D. F. et al. Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9. J. Biol. Chem. 282, 13864–13874 (2007). · DOI
  31. Hyvönen, M. et al. Structure of the binding site for inositol phosphates in a PH domain. EMBO J. 14, 4676–4685 (1995). · DOI
  32. Slagsvold, T. et al. Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain. J. Biol. Chem. 280, 19600–19606 (2005). · DOI
  33. Teo, H. et al. ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes. Cell 125, 99–111 (2006). Structurally illustrates an unexpected occurrence of a split PH domain that also binds phosphoinositides. · DOI · Paper page
  34. Yu, J. W. et al. Genome-wide analysis of membrane targeting by S. cerevisiae pleckstrin homology domains. Mol. Cell 13, 677–688 (2004). Provides a valuable perspective on the likely diversity of PH domain function. · DOI
  35. Lemmon, M. A. Pleckstrin homology domains: not just for phosphoinositides. Biochem. Soc. Trans. 32, 707–711 (2004). · DOI
  36. Kutateladze, T. G. Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain. Biochim. Biophys. Acta 1761, 868–877 (2006). · DOI
  37. Misra, S. & Hurley, J. H. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell 97, 657–666 (1999). · DOI
  38. Dumas, J. J. et al. Multivalent endosome targeting by homodimeric EEA1. Mol. Cell 8, 947–958 (2001). · DOI
  39. Kutateladze, T. & Overduin, M. Structural mechanism of endosome docking by the FYVE domain. Science 291, 1793–1796 (2001). · DOI
  40. Stahelin, R. V. et al. Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem. 277, 26379–26388 (2002). · DOI
  41. Gillooly, D. J. et al. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J. 19, 4577–4588 (2000). · DOI · Paper page
  42. Hayakawa, A. et al. Structural basis for endosomal targeting by FYVE domains. J. Biol. Chem. 279, 5958–5966 (2004). · DOI
  43. Ponting, C. P. Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains? Plant Prot. Sci. 5, 2353–2357 (1996). · DOI · Paper page
  44. Ellson, C. D., Andrews, S., Stephens, L. R. & Hawkins, P. T. The PX domain: a new phosphoinositide-binding module. J. Cell Sci. 115, 1099–1105 (2002). · DOI
  45. Seet, L. F. & Hong, W. The Phox (PX) domain proteins and membrane traffic. Biochim. Biophys. Acta 1761, 878–896 (2006). · DOI
  46. Yu, J. W. & Lemmon, M. A. All Phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate. J. Biol. Chem. 276, 44179–44184 (2001). · DOI
  47. Kanai, F. et al. The PX domains of p47phox and p40phox bind to lipid products of PI(3)K. Nature Cell Biol. 3, 675–678 (2001). · DOI · Paper page
  48. Song, X. et al. Phox homology domains specifically bind phosphatidylinositol phosphates. Biochemistry 40, 8940–8944 (2001). · DOI
  49. Bravo, J. et al. The crystal structure of the PX domain from p40phox bound to phosphatidylinositol 3-phosphate. Mol. Cell 8, 829–839 (2001). · DOI
  50. Ellson, C. D. et al. PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40phox. Nature Cell Biol. 3, 679–682 (2001). · DOI
  51. Xu, Y., Hortsman, H., Seet, L., Wong, S. H. & Hong, W. SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P. Nature Cell Biol. 3, 658–666 (2001). · DOI
  52. Zhong, Q. et al. Determinants of the endosomal localization of sorting nexin 1. Mol. Biol. Cell 16, 2049–2057 (2005). · DOI
  53. Seaman, M. N., McCaffery, J. M. & Emr, S. D. A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J. Cell Biol. 142, 665–681 (1998). · DOI · Paper page
  54. Seaman, M. N. & Williams, H. P. Identification of the functional domains of yeast sorting nexins Vps5p and Vps17p. Mol. Biol. Cell 13, 2826–2840 (2002). · DOI · Paper page
  55. Michell, R. H., Heath, V. L., Lemmon, M. A. & Dove, S. K. Phosphatidylinositol 3,5-bisphosphate: metabolism and cellular functions. Trends Biochem. Sci. 31, 52–63 (2006). · DOI
  56. Dove, S. K. et al. Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors. EMBO J. 23, 1922–1933 (2004). · DOI
  57. Jeffries, T. R., Dove, S. K., Michell, R. H. & Parker, P. J. PtdIns-specific MPR pathway association of a novel WD40 repeat protein, WIPI49. Mol. Biol. Cell 15, 2652–2663 (2004). · DOI
  58. Stromhaug, P. E., Reggiori, F., Guan, J., Wang, C. W. & Klionsky, D. J. Atg21 is a phosphoinositide binding protein required for efficient lipidation and localization of Atg8 during uptake of aminopeptidase I by selective autophagy. Mol. Biol. Cell 15, 3553–3566 (2004). · DOI
  59. Stace, C. L. & Ktistakis, N. T. Phosphatidic acid- and phosphatidylserine-binding proteins. Biochim. Biophys. Acta 1761, 913–926 (2006). Provides a valuable review of the characteristics of phosphatidic acid-binding sequences. · DOI
  60. Zhao, C., Du, G., Skowronek, K., Frohman, M. A. & Bar-Sagi, D. Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos. Nature Cell Biol. 9, 706–712 (2007).
  61. Karathanassis, D. et al. Binding of the PX domain of p47phox to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J. 21, 5057–5068 (2002). · DOI · Paper page
  62. Loewen, C. J. et al. Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid. Science 304, 1644–1647 (2004). Describes an intriguing mechanism of transcription-factor inhibition by sequestration at specific extranuclear membranes. · DOI
  63. Cho, W. & Stahelin, R. V. Membrane binding and subcellular targeting of C2 domains. Biochim. Biophys. Acta 1761, 838–849 (2006). · DOI
  64. Murray, D. & Honig, B. Electrostatic control of the membrane targeting of C2 domains. Mol. Cell 9, 145–154 (2002). · DOI
  65. Verdaguer, N., Corbalan-Garcia, S., Ochoa, W. F., Fita, I. & Gomez-Fernandez, J. C. Ca2+ bridges the C2 membrane-binding domain of protein kinase Cα directly to phosphatidylserine. EMBO J. 18, 6329–6338 (1999). · DOI
  66. Davletov, B., Perisic, O. & Williams, R. L. Calcium-dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synaptotagmin binds membranes electrostatically. J. Biol. Chem. 273, 19093–19096 (1998). · DOI
  67. Sánchez-Bautista, S., Marin-Vicente, C., Gómez-Fernandez, J. C. & Corbalán-Garcia, S. The C2 domain of PKCα is a Ca2+-dependent PtdIns(4,5)P2 sensing domain: a new insight into an old pathway. J. Mol. Biol. 362, 901–914 (2006). · DOI
  68. Gerke, V., Creutz, C. E. & Moss, S. E. Annexins: linking Ca2+ signalling to membrane dynamics. Nature Rev. Mol. Cell Biol. 6, 449–461 (2005). · DOI
  69. Swairjo, M. A., Concha, N. O., Kaetzel, M. A., Dedman, J. R. & Seaton, B. A. Ca2+-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nature Struct. Biol. 2, 968–974 (1995). · DOI
  70. Rescher, U., Ruhe, D., Ludwig, C., Zobiack, N. & Gerke, V. Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J. Cell Sci. 117, 3473–3480 (2004). · DOI
  71. Zwaal, R. F., Comfurius, P. & Bevers, E. M. Lipid–protein interactions in blood coagulation. Biochim. Biophys. Acta 1376, 433–453 (1998). · DOI
  72. Huang, M. et al. Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins. Nature Struct. Biol. 10, 751–756 (2003). · DOI
  73. Macedo-Ribeiro, S. et al. Crystal structures of the membrane-binding C2 domain of human coagulation factor V. Nature 402, 434–439 (1999). · DOI
  74. Itoh, T. & De Camilli, P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim. Biophys. Acta 1761, 897–912 (2006). · DOI · Paper page
  75. Ford, M. G. et al. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 291, 1051–1055 (2001). · DOI · Paper page
  76. Itoh, T. et al. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 291, 1047–1051 (2001). · DOI · Paper page
  77. Collins, B. M., McCoy, A. J., Kent, H. M., Evans, P. R. & Owen, D. J. Molecular architecture and functional model of the endocytic AP2 complex. Cell 109, 523–535 (2002). · DOI · Paper page
  78. Stahelin, R. V. et al. Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. J. Biol. Chem. 278, 28993–28999 (2003). · DOI
  79. Zimmerberg, J. & Kozlov, M. M. How proteins produce cellular membrane curvature. Nature Rev. Mol. Cell Biol. 7, 9–19 (2006). Valuable perspectives on physical processes that are involved in inducing membrane curvature. · DOI
  80. Martens, S., Kozlov, M. M. & McMahon, H. T. How synaptotagmin promotes membrane fusion. Science 316, 1205–1208 (2007). · DOI · Paper page
  81. Takei, K., Slepnev, V. I., Haucke, V. & De Camilli, P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nature Cell Biol. 1, 33–39 (1999). · DOI
  82. Farsad, K. et al. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J. Cell Biol. 155, 193–200 (2001). · DOI
  83. Peter, B. J. et al. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303, 495–499 (2004). First structure of a BAR domain, which led to the current notion that these are sensors (or inducers) of membrane curvature. · DOI · Paper page
  84. Zimmerberg, J. & McLaughlin, S. Membrane curvature: how BAR domains bend bilayers. Curr. Biol. 14, R250–R252 (2004). · DOI
  85. Masuda, M. et al. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J. 25, 2889–2897 (2006). · DOI
  86. Gallop, J. L. et al. Mechanism of endophilin N-BAR domain-mediated membrane curvature. EMBO J. 25, 2898–2910 (2006). · DOI
  87. Henne, W. M. et al. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 15, 839–852 (2007). · DOI
  88. Shimada, A. et al. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell 129, 761–772 (2007). · DOI
  89. Chitu, V. & Stanley, E. R. Pombe Cdc15 homology (PCH) proteins: coordinators of membrane–cytoskeletal interactions. Trends Cell Biol. 17, 145–156 (2007). · DOI
  90. Itoh, T. et al. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev. Cell 9, 791–804 (2005). · DOI
  91. Tsujita, K. et al. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J. Cell Biol. 172, 269–279 (2006). · DOI
  92. Millard, T. H. et al. Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. EMBO J. 24, 240–250 (2005). · DOI
  93. Mattila, P. K. et al. Missing-in-metastasis and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain-like mechanism. J. Cell Biol. 176, 953–964 (2007). · DOI
  94. Klein, D. E., Lee, A., Frank, D. W., Marks, M. S. & Lemmon, M. A. The pleckstrin homology domains of dynamin isoforms require oligomerization for high affinity phosphoinositide binding. J. Biol. Chem. 273, 27725–27733 (1998). · DOI
  95. Carlton, J. G. & Cullen, P. J. Coincidence detection in phosphoinositide signaling. Trends Cell Biol. 15, 540–547 (2005). Informative survey of mechanisms for coincidence detection in membrane binding. · DOI
  96. Carlton, J. et al. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Curr. Biol. 14, 1791–1800 (2004). · DOI · Paper page
  97. Liu, Q. et al. CAPRI and RASAL impose different modes of information processing on Ras due to contrasting temporal filtering of Ca2+. J. Cell Biol. 170, 183–190 (2005). · DOI
  98. Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211–225 (2000). · DOI · Paper page
  99. Godi, A. et al. FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nature Cell Biol. 6, 393–404 (2004). · DOI
  100. Levine, T. P. & Munro, S. Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components. Curr. Biol. 12, 695–704 (2002). One of the first papers to suggest that certain PH domains may bind simultaneously to phospholipid and protein targets. · DOI
  101. Tanford, C. The Hydrophobic Effect (Wiley, New York, 1980).
  102. Stephens, L. R., Jackson, T. R. & Hawkins, P. T. Agonist-stimulated synthesis of phosphatidylinositol(3,4,5)-trisphosphate: a new intracellular signalling system? Biochim. Biophys. Acta 1179, 27–75 (1993). · DOI
  103. Morris, J. B., Hinchliffe, K. A., Ciruela, A., Letcher, A. J. & Irvine, R. F. Thrombin stimulation of platelets causes an increase in phosphatidylinositol 5-phosphate revealed by mass assay. FEBS Lett. 475, 57–60 (2000). · DOI
  104. Pendaries, C. et al. Emerging roles of phosphatidylinositol monophosphates in cellular signaling and trafficking. Adv. Enzyme Regul. 45, 201–214 (2005). · DOI
  105. Mitra, P. et al. A novel phosphatidylinositol(3,4,5)P3 pathway in fission yeast. J. Cell Biol. 166, 205–211 (2004). · DOI
  106. Maffucci, T., Brancaccio, A., Piccolo, E., Stein, R. C. & Falasca, M. Insulin induces phosphatidylinositol-3-phosphate formation through TC10 activation. EMBO J. 22, 4178–4189 (2003). · DOI
  107. Pettitt, T. R., Dove, S. K., Lubben, A., Calaminus, S. D. & Wakelam, M. J. Analysis of intact phosphoinositides in biological samples. J. Lipid Res. 47, 1588–1596 (2006). · DOI
  108. Narayan, K. & Lemmon, M. A. Determining selectivity of phosphoinositide-binding domains. Methods 39, 122–133 (2006). · DOI
  109. Dowler, S. et al. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 351, 19–31 (2000). · DOI
  110. Gozani, O. et al. The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor. Cell 114, 99–111 (2003). · DOI
  111. Weissenhorn, W. Crystal structure of the endophilin-A1 BAR domain. J. Mol. Biol. 351, 653–661 (2005). · DOI
  112. Letunic, I. et al. SMART 5: domains in the context of genomes and networks. Nucleic Acids Res. 34, D257–D260 (2006). · DOI
  113. Bhattacharyya, R. P., Remenyi, A., Yeh, B. J. & Lim, W. A. Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu. Rev. Biochem. 75, 655–680 (2006). · DOI
  114. Fuentes-Prior, P., Fujikawa, K. & Pratt, K. P. New insights into binding interfaces of coagulation factors V and VIII and their homologues — lessons from high resolution crystal structures. Curr. Protein Pept. Sci. 3, 313–339 (2002). · DOI

Cited by

Sorted by citations

Metadata

Authors
Lemmon, M. A.
Venue
Nature Reviews Molecular Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2008-02
Volume
9
Issue
2
Pages
99-111
ISSN
  • 1471-0072
  • 1471-0080
DOI
10.1038/nrm2328
Cited by
1,419
References
4
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review