CoChat
Sign Up
Cited by 22

The DOI matches its Crossref record.

A Rugged Energy Landscape Mechanism for Trapping of Transmembrane Receptors during Endocytosis

Licht, Stuart S., Sonnleitner, Alois, Weiss, Shimon, Schultz, Peter G.·2003·Biochemistry
DOI 10.1021/bi026059v
Open this paper in CoChat — free account

Abstract

Efficient clathrin-mediated endocytosis of transmembrane receptors requires that clathrin-coated pits retain the receptors long enough to allow vesicle formation and internalization. In many cases, however, the receptors can exhibit mean lifetimes in coated pits much shorter than the lifetime of the pit at the plasma membrane. A rugged energy landscape for binding, which produces a broad distribution of residence times, ensures a significant probability of times much greater than the mean and would allow efficient trapping of proteins in these cases. We used fluorescence correlation spectroscopy and total internal reflection microscopy to measure the kinetics of movement of a C5a receptor-yellow fluorescent protein fusion in living cells. These experiments demonstrate that clusters of trapped receptors exhibit fluctuations in fluorescence intensity that vary in time scale over 2 orders of magnitude. Most of the variation in intensity is likely due to the motion of the receptors in the plane of the plasma membrane, although it is not possible to rule out a small contribution from motion orthogonal to the plane of the membrane. The broad time scale distribution of the intensity fluctuations is consistent with a rugged energy landscape mechanism for trapping of the receptors. This mechanism, which allows efficient trapping to coexist with rapid exchange, may also be relevant to other biological processes involving binding in heterogeneous chemical environments.

Overview

Integrity signals

Registry

Crossref · 10.1021/bi026059v

Cites

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

No references could be resolved yet.

Research works printed but not linked: 65

  1. Schmid S. L., 1997, Annu. Rev. Biochem., 66, 10.1146/annurev.biochem.66.1.511 · DOI
  2. Kirchhausen T., 1999, Annu. Rev. Cell Dev. Biol., 15, 10.1146/annurev.cellbio.15.1.705 · DOI · Paper page
  3. Gaidarov I., 1999, Nat. Cell Biol., 1, 7, 10.1038/8971 · DOI
  4. Miller K., 1991, Cell 65, 621−632
  5. Wiley H. S., 1982, J. Biol. Chem., 257, 10.1016/S0021-9258(18)34709-4 · DOI
  6. Moore R. H., 1999, Eur. J. Pharmacol., 369, 10.1016/S0014-2999(99)00055-2 · DOI
  7. Zwart D. E., 1996, J. Biol. Chem., 271, 10.1074/jbc.271.2.907 · DOI
  8. Orci L., 1978, Exp. Cell Res., 113, 13, 10.1016/0014-4827(78)90081-2 · DOI
  9. Fire E., 1991, J. Cell Biol., 115, 10.1083/jcb.115.6.1585 · DOI
  10. Barak L. S., 1997, Mol. Pharmacol. 51, 177−184
  11. Goldstein B., 1981, Proc. Natl. Acad. Sci. U.S.A. 78, 5695−5698
  12. Katzir Z., 1994, J. Biol. Chem., 269, 10.1016/S0021-9258(17)31842-2 · DOI
  13. Umenishi F., 2000, Biophys. J., 78, 10.1016/S0006-3495(00)76661-6 · DOI
  14. Gilboa L., 1995, J. Biol. Chem., 270, 10.1074/jbc.270.13.7061 · DOI
  15. Fire E., 1995, J. Biol. Chem., 270, 10.1074/jbc.270.36.21075 · DOI
  16. Petrelli A., 2002, Nature 416, 187−190
  17. Farsad K., 2001, J. Cell Biol., 155, 10.1083/jcb.200107075 · DOI
  18. Schmidt A., 1999, Nature 401, 133−141
  19. Scher H., 1991, Phys. Today, 26−34
  20. Pfister G., 1978, Adv. Phys., 27, 747, 10.1080/00018737800101474 · DOI
  21. Nagle J. F., 1992, Biophys. J., 63, 10.1016/S0006-3495(92)81602-8 · DOI
  22. Axelrod D., 2001, Traffic 2, 764−774
  23. Naik N., 1997, J. Cell Sci., 110, 10.1242/jcs.110.19.2381 · DOI
  24. Wilde M. W., 1989, J. Biol. Chem., 264
  25. Servant G., 1999, Mol. Biol. Cell 10, 1163−1178
  26. Hansen S. H., 1993, J. Cell Biol., 121, 72, 10.1083/jcb.121.1.61 · DOI
  27. Schwille P., 1999, Cytometry 36, 176−182
  28. Schwille P., 2000, Proc. Natl. Acad. Sci. U.S.A. 97, 151−156
  29. Steyer J. A., 1997, Nature 388, 474−478
  30. Funatsu T., 1995, Nature 374, 555−559
  31. Axelrod D., 1989, Methods Cell Biol. 30, 245−270
  32. Stanley H. E., 1994, D 16, 1339−1356.
  33. Hoop B., 2000, J. Membr. Biol., 177, 10.1007/s002320010001 · DOI
  34. Buldyrev S. V., 1995, Phys. Rev. E, 51, 10.1103/PhysRevE.51.5084 · DOI
  35. Peng C. K., 1994, Phys. Rev. E, 49
  36. Heneghan C., 2000, Phys. Rev. E, 62, 10.1103/PhysRevE.62.6103 · DOI
  37. Neher E., 1977, Annu. Rev. Biophys. Bioeng., 6, 10.1146/annurev.bb.06.060177.002021 · DOI
  38. Widengren J., 1998, Cell. Mol. Biol. 44, 857−879
  39. Brock R., 1998, Cell. Mol. Biol. 44, 847−856
  40. Neptune E. R., 1997, Proc. Natl. Acad. Sci. U.S.A. 94, 14489−14494
  41. Korlach J., 1999, Proc. Natl. Acad. Sci. U.S.A., 96, 9966, 10.1073/pnas.96.15.8461 · DOI
  42. Hansen S. H., 1993, J. Cell Biol., 121, 72, 10.1083/jcb.121.1.61 · DOI
  43. Heuser J., 1980, J. Cell Biol., 84, 10.1083/jcb.84.3.560 · DOI
  44. Sever S., 2000, J. Cell Biol., 150, 10.1083/jcb.150.5.1137 · DOI
  45. Sheets E. D., 1997, Biochemistry 36, 12449−12458
  46. Edidin M., 1991, J. Cell Biol., 112, 10.1083/jcb.112.6.1143 · DOI
  47. Elson E. L., 1979, J. Supramol. Struct., 12
  48. Bouchard J.-P., 1990, Phys. Rep. 195, 127−293
  49. Gilbert T. L., 2001, Biochemistry 40, 3467−3475
  50. Bereiter-Hahn J., 1979, J. Cell Biol., 82, 10.1083/jcb.82.3.767 · DOI
  51. Damke H., 2001, Mol. Biol. Cell 12, 2578−2589
  52. Brown C. M., 1998, J. Cell Sci., 111
  53. Nossal R., 2001, Traffic 2, 138−147
  54. Chou T., 2001, Biophys. J., 80, 10.1016/S0006-3495(01)76086-9 · DOI
  55. Schmid S. L., 1990, J. Cell Biol., 111, 10.1083/jcb.111.6.2307 · DOI
  56. Frauenfelder H., 1991, Science 254, 1598−1603
  57. Wennmalm S., 1999, Chem. Phys., 247, 67, 10.1016/S0301-0104(99)00125-1 · DOI
  58. Edman L., 1999, Chem. Phys., 247, 22, 10.1016/S0301-0104(99)00098-1 · DOI
  59. Lu H. P., 1998, Science 282
  60. Hopfield J. J., 1974, Proc. Natl. Acad. Sci. U.S.A. 71, 4135−4139
  61. McKeithan T. W., 1995, Proc. Natl. Acad. Sci. U.S.A. 92, 5042−5046
  62. Grakoui A., 1999, Science, 285, 221, 10.1126/science.285.5425.221 · DOI
  63. Cole N. B., 1996, Science 273, 797−801
  64. McNally J. G., 2000, Science 287, 1262−1265
  65. Abbreviations R, C5a receptor

Cited by

Sorted by citations

Metadata

Authors
Licht, S. S., Sonnleitner, A., Weiss, S., & Schultz, P. G.
Affiliations
Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, Division of Materials Science, Lawrence Berkeley National Laboratory, Berkeley, California 94720, Department of Chemistry and Biochemistry and Department of Physiology, University of California at Los Angeles, Los Angeles, California 90024, and Genomics Institute of the Novartis Research Foundation, San Diego, California 92121
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2003-02-20
Volume
42
Issue
10
Pages
2916-2925
ISSN
  • 0006-2960
  • 1520-4995
DOI
10.1021/bi026059v
Cited by
22
References
0
Language
en

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