CoChat
Sign Up
Cited by 298Cellular transport and secretionProtein Kinase Regulation and GTPase SignalingLipid Membrane Structure and Behavior

Pleckstrin homology (PH) domains and phosphoinositides

Open access
Lemmon, Mark A.·2007·Biochemical Society Symposium
DOI 10.1042/bss0740081PMC PMC3777418
Open this paper in CoChat — free account

Abstract

PH (pleckstrin homology) domains represent the 11th most common domain in the human proteome. They are best known for their ability to bind phosphoinositides with high affinity and specificity, although it is now clear that less than 10% of all PH domains share this property. Cases in which PH domains bind specific phosphoinositides with high affinity are restricted to those phosphoinositides that have a pair of adjacent phosphates in their inositol headgroup. Those that do not [PtdIns3P, PtdIns5P and PtdIns(3,5)P2] are instead recognized by distinct classes of domains including FYVE domains, PX (phox homology) domains, PHD (plant homeodomain) fingers and the recently identified PROPPINs (b-propellers that bind polyphosphoinositides). Of the 90% of PH domains that do not bind strongly and specifically to phosphoinositides, few are well understood. One group of PH domains appears to bind both phosphoinositides (with little specificity) and Arf (ADP-ribosylation factor) family small G-proteins, and are targeted to the Golgi apparatus where both phosphoinositides and the relevant Arfs are both present. Here, the PH domains may function as coincidence detectors. A central challenge in understanding the majority of PH domains is to establish whether the very low affinity phosphoinositide binding reported in many cases has any functional relevance. For PH domains from dynamin and from Dbl family proteins, this weak binding does appear to be functionally important, although its precise mechanistic role is unclear. In many other cases, it is quite likely that alternative binding partners are more relevant, and that the observed PH domain homology represents conservation of structural fold rather than function.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1042/bss0740081

Cites

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

  • PI3K generates PI(3,4,5)P3, a lipid with wide-ranging functions.

    “The second pathway is phosphoinositide-3-kinase (PI3K) to make PI(3,4,5)P3, a lipid with wide-ranging functions.”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [9]

    The Background links phosphoinositide 3-kinase signaling to PH domains that recognize PtdIns(3,4,5)P3 and describes several proteins that bind the lipid. It does not explicitly state that PI3K generates PtdIns(3,4,5)P3 or establish the lipid’s wide-ranging functions. (LLM, conf=0.78)

    Experimental — accuracy not yet measured

  • PLC hydrolysis of PI(4,5)P2 generates IP3 and DAG.

    “Phospholipase C (PLC) leads to the generation of two second messengers, inositol(1,4,5)trisphosphate (I(1,4,5)P3), known trigger for mobilising Ca2+ from endoplasmic reticulum (ER) stores and diacylglycerol (DAG), an activator for protein kinase C (PKC).”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [9]

    The Background discusses binding of the PLC-δ1 PH domain to PtdIns(4,5)P2 and Ins(1,4,5)P3, but does not say that PLC hydrolyses PtdIns(4,5)P2 to produce IP3 and DAG. Searches for diacylglycerol and the stated calcium-mobilisation pathway found no passage addressing those claims. (LLM, conf=0.72)

    Experimental — accuracy not yet measured

  • PI(4,5)P2 is a substrate for PLC and PI3K.

    “PI(4,5)P2 is a substrate for two signalling pathways.”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [9]

    The Background describes PtdIns(4,5)P2 binding to the PH domain of PLC-δ1 and discusses PH-domain recruitment following activation of PI3K signaling. It does not state that PtdIns(4,5)P2 is a substrate for PLC or PI3K (searched for substrate, hydrolysis, and phosphorylation). (LLM, conf=0.72)

    Experimental — accuracy not yet measured

  • IP3 mobilises Ca2+ from ER stores.

    “Phospholipase C (PLC) leads to the generation of two second messengers, inositol(1,4,5)trisphosphate (I(1,4,5)P3), known trigger for mobilising Ca2+ from endoplasmic reticulum (ER) stores and diacylglycerol (DAG), an activator for protein kinase C (PKC).”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [9]

    The Background discusses Ins(1,4,5)P3 binding to PH domains, but does not say that it mobilises Ca2+ from ER stores. Searches for calcium release, ER stores, and inositol trisphosphate as a second messenger found no passage addressing that action. No page numbers are supplied in our copy. (LLM, conf=0.73)

    Experimental — accuracy not yet measured

  • DAG activates PKC.

    “Phospholipase C (PLC) leads to the generation of two second messengers, inositol(1,4,5)trisphosphate (I(1,4,5)P3), known trigger for mobilising Ca2+ from endoplasmic reticulum (ER) stores and diacylglycerol (DAG), an activator for protein kinase C (PKC).”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [9]

    The Background discusses PLCδ PH-domain binding to phosphoinositides and identifies pleckstrin as a PKC substrate, but it does not say that DAG activates PKC. Searches for DAG, diacylglycerol, and PKC activation found no passage addressing that relationship. (LLM, conf=0.73)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The citation lists haven’t been fetched yet

References 85 · Cited by 298

Research works printed but not linked: 84

  1. [1]Haslam RJ, Koide HB, Hemmings BA. Nature. 1993;363:309–310. doi: 10.1038/363309b0. [DOI] [PubMed] [Google Scholar] · DOI
  2. [2]Mayer BJ, Ren R, Clark KL, Baltimore D. Cell. 1993;73:629–630. doi: 10.1016/0092-8674(93)90244-k. [DOI] [PubMed] [Google Scholar] · DOI
  3. [3]Tyers M, Rachubinski RA, Stewart MI, Varrichio AM, Shorr RGL, Haslam RJ, Harley CB. Nature. 1988;333:470–473. doi: 10.1038/333470a0. [DOI] [PubMed] [Google Scholar] · DOI
  4. [4]Yoon HS, Hajduk PJ, Petros AM, Olejniczak ET, Meadows RP, Fesik SW. Nature. 1994;369:672–675. doi: 10.1038/369672a0. [DOI] [PubMed] [Google Scholar] · DOI
  5. [5]Macias MJ, Musacchio A, Ponstingl H, Nilges M, Saraste M, Oschkinat H. Nature. 1994;369:675–677. doi: 10.1038/369675a0. [DOI] [PubMed] [Google Scholar] · DOI
  6. [6]Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. Nature. 1994;371:168–170. doi: 10.1038/371168a0. [DOI] [PubMed] [Google Scholar] · DOI
  7. [7]Lemmon MA, Ferguson KM, O’Brien R, Sigler PB, Schlessinger J. Proc Natl Acad Sci USA. 1995;92:10472–10476. doi: 10.1073/pnas.92.23.10472. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI · Paper page
  8. [8]Garcia P, Gupta R, Shah S, Morris AJ, Rudge SA, Scarlata S, Petrova V, McLaughlin S, Rebecchi MJ. Biochemistry. 1995;34:16228–16234. doi: 10.1021/bi00049a039. [DOI] [PubMed] [Google Scholar] · DOI
  9. [9]Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. Cell. 1995;83:1037–1046. doi: 10.1016/0092-8674(95)90219-8. [DOI] [PubMed] [Google Scholar] · DOI
  10. [10]Franke TF, Kaplan DR, Cantley LC, Toker A. Science. 1997;275:665–668. doi: 10.1126/science.275.5300.665. [DOI] [PubMed] [Google Scholar] · DOI
  11. [11]Fruman DA, Rameh LE, Cantley LC. Cell. 1999;97:817–820. doi: 10.1016/s0092-8674(00)80792-8. [DOI] [PubMed] [Google Scholar] · DOI
  12. [12]Baraldi E, Djinovic Carugo K, Hyvönen M, Lo Surdo P, Riley AM, Potter BVL, O’Brien R, Ladbury JE, Saraste M. Structure. 1999;7:449–460. doi: 10.1016/s0969-2126(99)80057-4. [DOI] [PubMed] [Google Scholar] · DOI
  13. [13]Ferguson KM, Kavran JM, Sankaran VG, Fournier E, Isakoff SJ, Skolnik EY, Lemmon MA. Mol Cell. 2000;6:373–384. doi: 10.1016/s1097-2765(00)00037-x. [DOI] [PubMed] [Google Scholar] · DOI
  14. [14]Lietzke SE, Bose S, Cronin T, Klarlund J, Chawla A, Czech MP, Lambright DG. Mol Cell. 2000;6:385–394. doi: 10.1016/s1097-2765(00)00038-1. [DOI] [PubMed] [Google Scholar] · DOI
  15. [15]DiNitto JP, Cronin TC, Lambright DG. Sci STKE. 2003;(213):re16. doi: 10.1126/stke.2132003re16. [DOI] [PubMed] [Google Scholar] · DOI
  16. [16]Lemmon MA. Traffic. 2003;4:201–213. doi: 10.1034/j.1600-0854.2004.00071.x. [DOI] [PubMed] [Google Scholar] · DOI
  17. [17]Rusten TE, Stenmark H. Nature Methods. 2006;3:251–258. doi: 10.1038/nmeth867. [DOI] [PubMed] [Google Scholar] · DOI
  18. [18]Letunic I, Copley RR, Pils B, Pinkert S, Schultz J, Bork P. Nucl Acids Res. 2006;34:D257–D260. doi: 10.1093/nar/gkj079. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  19. [19]Kavran JM, Klein DE, Lee A, Falasca M, Isakoff SJ, Skolnik EY, Lemmon MA. J Biol Chem. 1998;273:30497–30508. doi: 10.1074/jbc.273.46.30497. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  20. [20]Takeuchi H, Kanematsu T, Misumi Y, Sakane F, Konishi H, Kikkawa U, Watanabe Y, Katan M, Hirata M. Biochim Biophys Acta. 1997;1359:275–285. doi: 10.1016/s0167-4889(97)00109-2. [DOI] [PubMed] [Google Scholar] · DOI
  21. [21]Lemmon MA, Ferguson KM. Biochem J. 2000;350:1–18. [PMC free article] [PubMed] [Google Scholar]
  22. [22]Vandemark AP, Blanksma M, Ferris E, Heroux A, Hill CP, Formosa T. Mol Cell. 2006;22:363–374. doi: 10.1016/j.molcel.2006.03.025. [DOI] [PubMed] [Google Scholar] · DOI
  23. [23]Furst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. J Biol Chem. 2005;280:31276–31282. doi: 10.1074/jbc.M500541200. [DOI] [PubMed] [Google Scholar] · DOI
  24. [24]Gervais V, Lamour V, Jawhari A, Frindel F, Wasielewski E, Dubaele S, Egly JM, Thierry JC, Kieffer B, Poterszman A. Nat Struct Mol Biol. 2004;11:616–622. doi: 10.1038/nsmb782. [DOI] [PubMed] [Google Scholar] · DOI
  25. [25]Prehoda KE, Lee DJ, Lim WA. Cell. 1999;97:471–480. doi: 10.1016/s0092-8674(00)80757-6. [DOI] [PubMed] [Google Scholar] · DOI
  26. [26]Yu JW, Mendrola JM, Audhya A, Singh S, Keleti D, DeWald DB, Murray D, Emr SD, Lemmon MA. Mol Cell. 2004;13:677–688. doi: 10.1016/s1097-2765(04)00083-8. [DOI] [PubMed] [Google Scholar] · DOI
  27. [27]Klarlund JK, Guilherme A, Holik JJ, Virbasius A, Czech MP. Science. 1997;275:1927–1930. doi: 10.1126/science.275.5308.1927. [DOI] [PubMed] [Google Scholar] · DOI
  28. [28]Salim K, Bottomley MJ, Querfurth E, Zvelebil MJ, Gout I, Scaife R, Margolis RL, Gigg R, Smith CIE, Driscoll PC, Waterfield MD, Panayotou G. EMBO J. 1996;15:6241–6250. [PMC free article] [PubMed] [Google Scholar]
  29. [29]Dowler S, Currie RA, Downes CP, Alessi DR. Biochem J. 1999;342:7–12. [PMC free article] [PubMed] [Google Scholar]
  30. [30]Dowler S, Currie RA, Campbell DG, Deak M, Kular G, Downes CP, Alessi DR. Biochem J. 2000;351:19–31. doi: 10.1042/0264-6021:3510019. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  31. [31]Thomas CC, Dowler S, Deak M, Alessi DR, van Aalten DM. Biochem J. 2001;358:287–294. doi: 10.1042/0264-6021:3580287. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  32. [32]Baumeister MA, Martinu L, Rossman KL, Sondek J, Lemmon MA, Chou MM. J Biol Chem. 2003;278:11457–11464. doi: 10.1074/jbc.M211901200. [DOI] [PubMed] [Google Scholar] · DOI
  33. [33]Teo H, Gill DJ, Sun J, Perisic O, Veprintsev DB, Vallis Y, Emr SD, Williams RL. Cell. 2006;125:99–111. doi: 10.1016/j.cell.2006.01.047. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  34. [34]Cronin TC, DiNitto JP, Czech MP, Lambright DG. EMBO J. 2004;23:3711–3720. doi: 10.1038/sj.emboj.7600388. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  35. [35]Thomas C, Deak M, Alessi D, van Aalten D. Curr Biol. 2002;12:1256–1262. doi: 10.1016/s0960-9822(02)00972-7. [DOI] [PubMed] [Google Scholar] · DOI
  36. [36]Isakoff SJ, Cardozo T, Andreev J, Li Z, Ferguson KM, Abagyan R, Lemmon MA, Aronheim A, Skolnik EY. EMBO J. 1998;17:5374–5387. doi: 10.1093/emboj/17.18.5374. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI · Paper page
  37. [37]Corbin JA, Dirkx RA, Falke JJ. Biochemistry. 2004;43:16161–16173. doi: 10.1021/bi049017a. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  38. [38]Ellson CD, Andrews S, Stephens LR, Hawkins PT. J Cell Sci. 2002;115:1099–1105. doi: 10.1242/jcs.115.6.1099. [DOI] [PubMed] [Google Scholar] · DOI
  39. [39]Gillooly DJ, Simonsen A, Stenmark H. Biochem J. 2001;355:249–258. doi: 10.1042/0264-6021:3550249. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  40. [40]Yu JW, Lemmon MA. J Biol Chem. 2001;276:44179–44184. doi: 10.1074/jbc.M108811200. [DOI] [PubMed] [Google Scholar] · DOI
  41. [41]Kanai F, Liu H, Field SJ, Akbary H, Matsuo T, Brown GE, Cantley LC, Yaffe MB. Nat Cell Biol. 2001;3:675–678. doi: 10.1038/35083070. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  42. [42]Song X, Xu W, Zhang A, Huang G, Liang X, Virbasius JV, Czech MP, Zhou GW. Biochemistry. 2001;40:8940–8944. doi: 10.1021/bi0155100. [DOI] [PubMed] [Google Scholar] · DOI
  43. [43]Lee JS, Kim JH, Jang IH, Kim HS, Han JM, Kazlauskas A, Yagisawa H, Suh PG, Ryu SH. J Cell Sci. 2005;118:4405–4413. doi: 10.1242/jcs.02564. [DOI] [PubMed] [Google Scholar] · DOI
  44. [44]Misra S, Hurley JH. Cell. 1999;97:657–666. doi: 10.1016/s0092-8674(00)80776-x. [DOI] [PubMed] [Google Scholar] · DOI
  45. [45]Dumas JJ, Merithew E, Sudharshan E, Rajamani D, Hayes S, Lawe D, Corvera S, Lambright DG. Mol Cell. 2001;8:947–958. doi: 10.1016/s1097-2765(01)00385-9. [DOI] [PubMed] [Google Scholar] · DOI
  46. [46]Sankaran VG, Klein DE, Sachdeva MM, Lemmon MA. Biochemistry. 2001;40:8581–8587. doi: 10.1021/bi010425d. [DOI] [PubMed] [Google Scholar] · DOI
  47. [47]Kutateladze T, Overduin M. Science. 2001;291:1793–1796. doi: 10.1126/science.291.5509.1793. [DOI] [PubMed] [Google Scholar] · DOI
  48. [48]Stahelin RV, Long F, Diraviyam K, Bruzik KS, Murray D, Cho W. J Biol Chem. 2002;277:26379–26388. doi: 10.1074/jbc.M201106200. [DOI] [PubMed] [Google Scholar] · DOI
  49. [49]Gillooly DJ, Morrow IC, Lindsay M, Gould R, Bryant NJ, Gaullier JM, Parton RG, Stenmark H. EMBO J. 2000;19:4577–4588. doi: 10.1093/emboj/19.17.4577. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  50. [50]Stenmark H, Aasland R, Toh BH, D’Arrigo A. J Biol Chem. 1996;271:24048–24054. doi: 10.1074/jbc.271.39.24048. [DOI] [PubMed] [Google Scholar] · DOI
  51. [51]Bravo J, Karathanassis D, Pacold CM, Pacold ME, Ellson CD, Anderson KE, Butler PJ, Lavenir I, Perisic O, Hawkins PT, Stephens L, Williams RL. Mol Cell. 2001;8:829–839. doi: 10.1016/s1097-2765(01)00372-0. [DOI] [PubMed] [Google Scholar] · DOI
  52. [52]Stahelin RV, Burian A, Bruzik KS, Murray D, Cho W. J Biol Chem. 2003;278:14469–14479. doi: 10.1074/jbc.M212579200. [DOI] [PubMed] [Google Scholar] · DOI
  53. [53]Cheever ML, Sato TK, de Beer T, Kutateladze TG, Emr SD, Overduin M. Nat Cell Biol. 2001;3:613–618. doi: 10.1038/35083000. [DOI] [PubMed] [Google Scholar] · DOI
  54. [54]Whitley P, Reaves BJ, Hashimoto M, Riley AM, Potter BV, Holman GD. J Biol Chem. 2002 doi: 10.1074/jbc.M306864200. submitted for publication. [DOI] [PubMed] [Google Scholar] · DOI
  55. [55]Eugster A, Pecheur EI, Michel F, Winsor B, Letourneur F, Friant S. Mol Biol Cell. 2004;15:3031–3041. doi: 10.1091/mbc.E03-11-0793. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  56. [56]Friant S, Pecheur EI, Eugster A, Michel F, Lefkir Y, Nourrisson D, Letourneur F. Dev Cell. 2003;5:499–511. doi: 10.1016/s1534-5807(03)00238-7. [DOI] [PubMed] [Google Scholar] · DOI
  57. [57]Michell RH, Heath VL, Lemmon MA, Dove SK. Trends Biochem Sci. 2006;31:52–63. doi: 10.1016/j.tibs.2005.11.013. [DOI] [PubMed] [Google Scholar] · DOI
  58. [58]Narayan K, Lemmon MA. Methods. 2006 doi: 10.1016/j.ymeth.2006.05.006. in press. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  59. [59]Dove SK, Piper RC, McEwen RK, Yu JW, King MC, Hughes DC, Thuring J, Holmes AB, Cooke FT, Michell RH, Parker PJ, Lemmon MA. EMBO J. 2004;23:1922–1933. doi: 10.1038/sj.emboj.7600203. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  60. [60]Stromhaug PE, Reggiori F, Guan J, Wang CW, Klionsky DJ. Mol Biol Cell. 2004;15:3553–3566. doi: 10.1091/mbc.E04-02-0147. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  61. [61]Jeffries TR, Dove SK, Michell RH, Parker PJ. Mol Biol Cell. 2004;15:2652–2663. doi: 10.1091/mbc.E03-10-0732. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  62. [62]Gozani O, Karuman P, Jones DR, Ivanov D, Cha J, Lugovskoy AA, Baird CL, Zhu H, Field SJ, Lessnick SL, Villasenor J, Mehrotra B, Chen J, Rao VR, Brugge JS, Ferguson CG, Payrastre B, Myszka DG, Cantley LC, Wagner G, Divecha N, Prestwich GD, Yuan J. Cell. 2003;114:99–111. doi: 10.1016/s0092-8674(03)00480-x. [DOI] [PubMed] [Google Scholar] · DOI
  63. [63]Alvarez-Venegas R, Sadder M, Hlavacka A, Baluska F, Xia Y, Lu G, Firsov A, Sarath G, Moriyama H, Dubrovsky JG, Avramova Z. Proc Natl Acad Sci USA. 2006;103:6049–6054. doi: 10.1073/pnas.0600944103. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  64. [64]Cho W, Stahelin RV. Annu Rev Biophys Biomol Struct. 2005;34:119–151. doi: 10.1146/annurev.biophys.33.110502.133337. [DOI] [PubMed] [Google Scholar] · DOI
  65. [65]Tuzi S, Uekama N, Okada M, Yamaguchi S, Saito H, Yagisawa H. J Biol Chem. 2003;278:28019–28025. doi: 10.1074/jbc.M300101200. [DOI] [PubMed] [Google Scholar] · DOI
  66. [66]Varnai P, Lin X, Lee SB, Tuymetova G, Bondeva T, Spat A, Rhee SG, Hajnoczky G, Balla T. J Biol Chem. 2002;277:27412–27422. doi: 10.1074/jbc.M109672200. [DOI] [PubMed] [Google Scholar] · DOI
  67. [67]Flesch FM, Yu JW, Lemmon MA, Burger KN. Biochem J. 2005;389:435–441. doi: 10.1042/BJ20041721. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  68. [68]Levine TP, Munro S. Curr Biol. 2002;12:695–704. doi: 10.1016/s0960-9822(02)00779-0. [DOI] [PubMed] [Google Scholar] · DOI
  69. [69]Roy A, Levine TP. J Biol Chem. 2004;279:44683–44689. doi: 10.1074/jbc.M401583200. [DOI] [PubMed] [Google Scholar] · DOI
  70. [70]Levine TP, Munro S. Curr Biol. 1998;8:729–739. doi: 10.1016/s0960-9822(98)70296-9. [DOI] [PubMed] [Google Scholar] · DOI
  71. [71]Levine TP, Munro S. Mol Biol Cell. 2001;12:1633–1644. doi: 10.1091/mbc.12.6.1633. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  72. [72]Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, Kular GS, Daniele T, Marra P, Lucocq JM, De Matteis MA. Nat Cell Biol. 2004;6:393–404. doi: 10.1038/ncb1119. [DOI] [PubMed] [Google Scholar] · DOI
  73. [73]Blomberg N, Baraldi E, Nilges M, Saraste M. Trends Biochem Sci. 1999;24:441–445. doi: 10.1016/s0968-0004(99)01472-3. [DOI] [PubMed] [Google Scholar] · DOI
  74. [74]Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ. Science. 2003;300:1256–1262. doi: 10.1126/science.1082348. [DOI] [PubMed] [Google Scholar] · DOI
  75. [75]Stolt PC, Jeon H, Song HK, Herz J, Eck MJ, Blacklow SC. Structure. 2003;11:569–579. doi: 10.1016/s0969-2126(03)00068-6. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  76. [76]Yun M, Keshvara L, Park CG, Zhang YM, Dickerson JB, Zheng J, Rock CO, Curran T, Park HW. J Biol Chem. 2003;278:36572–36581. doi: 10.1074/jbc.M304384200. [DOI] [PubMed] [Google Scholar] · DOI
  77. [77]Audhya A, Loewith R, Parsons AB, Gao L, Tabuchi M, Zhou H, Boone C, Hall MN, Emr SD. EMBO J. 2004;23:3747–3757. doi: 10.1038/sj.emboj.7600384. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  78. [78]Rossman KL, Sondek J. Trends Biochem Sci. 2005;30:163–165. doi: 10.1016/j.tibs.2005.02.002. [DOI] [PubMed] [Google Scholar] · DOI
  79. [79]Worthylake DK, Rossman KL, Sondek J. Structure. 2004;12:1078–1086. doi: 10.1016/j.str.2004.03.021. [DOI] [PubMed] [Google Scholar] · DOI
  80. [80]Zheng J, Cahill SM, Lemmon MA, Fushman D, Schlessinger J, Cowburn D. J Mol Biol. 1996;255:14–21. doi: 10.1006/jmbi.1996.0002. [DOI] [PubMed] [Google Scholar] · DOI
  81. [81]Klein DE, Lee A, Frank DW, Marks MS, Lemmon MA. J Biol Chem. 1998;273:27725–27733. doi: 10.1074/jbc.273.42.27725. [DOI] [PubMed] [Google Scholar] · DOI
  82. [82]Achiriloaie M, Barylko B, Albanesi JP. Mol Cell Biol. 1999;19:1410–1415. doi: 10.1128/mcb.19.2.1410. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  83. [83]Lee A, Frank DW, Marks MS, Lemmon MA. Curr Biol. 1999;9:261–264. doi: 10.1016/s0960-9822(99)80115-8. [DOI] [PubMed] [Google Scholar] · DOI
  84. [84]Vallis Y, Wigge P, Marks B, Evans PR, McMahon HT. Curr Biol. 1999;9:257–260. doi: 10.1016/s0960-9822(99)80114-6. [DOI] [PubMed] [Google Scholar] · DOI

Authors
Lemmon, M. A.
Affiliations
University of Pennsylvania (US)
Corresponding author
Lemmon, Mark A.
ORCID
Lemmon, Mark A.
Venue
Biochemical Society Symposium
Publisher
Portland Press Ltd.
Published
2007-12-01
Volume
74
Issue
1
Pages
81
ISSN
  • 0067-8694 (ISSN-L)
  • 1744-1439
DOI
10.1042/bss0740081
PMC
PMC3777418
OpenAlex
W2068715852
Cited by
298
References
85
Citations by year
2026: 2 · 2025: 9 · 2024: 7 · 2023: 14 · 2022: 6 · 2021: 25 · 2020: 23 · 2019: 22 · 2018: 18 · 2017: 17 · 2016: 18 · 2015: 23 · 2014: 19 · 2013: 13 · 2012: 16
FWCI
128.63
Type
conference paper
Language
en
Open access
Locations
  • Biochemical Society Symposia (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institute of General Medical Sciences (GM056846, R01GM056846)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords
pleckstrin homology domain, phosphoinositides, phosphoinositide binding, Arf GTPases, Golgi apparatus targeting, coincidence detection, FYVE domain, PX domain, PHD finger, dynamin, low-affinity binding, protein domain evolution
MeSH terms
Binding Sites, Humans, Models, Molecular, Phosphatidylinositols, Protein Binding, Sensitivity and Specificity, Protein Structure, Tertiary

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