Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15 - PubMed (original) (raw)

. 1997 Dec 26;272(52):33430-4.

doi: 10.1074/jbc.272.52.33430.

Affiliations

• PMID: 9407139
• DOI: 10.1074/jbc.272.52.33430

Free article

Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15

P Cupers et al. J Biol Chem. 1997.

Free article

Abstract

The recently discovered localization of epidermal growth factor receptor pathway substrate clone 15 (Eps15) to plasma membrane clathrin-coated pits and its constitutive association with the endocytic clathrin adaptor protein complex, AP-2, strongly suggest that Eps15 has an important role in the pathway of clathrin-dependent endocytic traffic. We report here that Eps15 forms dimers and tetramers of distinct shape. The Eps15 dimer is an elongated molecule, 32 nm in length. There is a globular "head" at one end of the molecule and an extended "stalk" of 25 nm which is kinked at about 17 nm away from the head. In the Eps15 dimer, two subunits are arranged parallel to each other, so that the head corresponds to two side by side copies of the N-terminal region I, which contains the three Eps15 homology domains. The proximal part of the stalk is the coiled-coil central region II containing 20 heptad repeats. The kink is at the boundary between region II and the C-terminal region III, which contains the AP-2 binding site, 15 aspartic-proline-phenylalanine repeats, and proline-rich Src homology domain ligand sites. The Eps15 tetramer has a "dumbbell" shape, approximately 31 nm in length; it is formed by the anti-parallel association of two Eps15 dimers. Formation of these Eps15 tetramers appears to require contacts between regions I of one dimer and regions III of a second apposing dimer. The extended shapes of the Eps15 dimers and tetramers suggest how Eps15 oligomers are located in the clathrin coat. We discuss the implications for accessibility to partners and for proposed functions of Eps15.

PubMed Disclaimer

Similar articles

• Association and colocalization of Eps15 with adaptor protein-2 and clathrin.
  van Delft S, Schumacher C, Hage W, Verkleij AJ, van Bergen en Henegouwen PM. van Delft S, et al. J Cell Biol. 1997 Feb 24;136(4):811-21. doi: 10.1083/jcb.136.4.811. J Cell Biol. 1997. PMID: 9049247 Free PMC article.
• Mapping of Eps15 domains involved in its targeting to clathrin-coated pits.
  Benmerah A, Poupon V, Cerf-Bensussan N, Dautry-Varsat A. Benmerah A, et al. J Biol Chem. 2000 Feb 4;275(5):3288-95. doi: 10.1074/jbc.275.5.3288. J Biol Chem. 2000. PMID: 10652316
• Eps15 is recruited to the plasma membrane upon epidermal growth factor receptor activation and localizes to components of the endocytic pathway during receptor internalization.
  Torrisi MR, Lotti LV, Belleudi F, Gradini R, Salcini AE, Confalonieri S, Pelicci PG, Di Fiore PP. Torrisi MR, et al. Mol Biol Cell. 1999 Feb;10(2):417-34. doi: 10.1091/mbc.10.2.417. Mol Biol Cell. 1999. PMID: 9950686 Free PMC article.
• Epidermal growth factor pathway substrate 15, Eps15.
  Salcini AE, Chen H, Iannolo G, De Camilli P, Di Fiore PP. Salcini AE, et al. Int J Biochem Cell Biol. 1999 Aug;31(8):805-9. doi: 10.1016/s1357-2725(99)00042-4. Int J Biochem Cell Biol. 1999. PMID: 10481267 Review.
• Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases.
  Waterman H, Yarden Y. Waterman H, et al. FEBS Lett. 2001 Feb 16;490(3):142-52. doi: 10.1016/s0014-5793(01)02117-2. FEBS Lett. 2001. PMID: 11223029 Review.

Cited by

• Clathrin-dependent endocytosis.
  Mousavi SA, Malerød L, Berg T, Kjeken R. Mousavi SA, et al. Biochem J. 2004 Jan 1;377(Pt 1):1-16. doi: 10.1042/BJ20031000. Biochem J. 2004. PMID: 14505490 Free PMC article. Review.
• Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly.
  Schmid EM, Ford MG, Burtey A, Praefcke GJ, Peak-Chew SY, Mills IG, Benmerah A, McMahon HT. Schmid EM, et al. PLoS Biol. 2006 Sep;4(9):e262. doi: 10.1371/journal.pbio.0040262. PLoS Biol. 2006. PMID: 16903783 Free PMC article.
• UIM domain-dependent recruitment of the endocytic adaptor protein Eps15 to ubiquitin-enriched endosomes.
  Gucwa AL, Brown DA. Gucwa AL, et al. BMC Cell Biol. 2014 Sep 27;15:34. doi: 10.1186/1471-2121-15-34. BMC Cell Biol. 2014. PMID: 25260758 Free PMC article.
• Molecular dissection of Rab11 binding from coiled-coil formation in the Rab11-FIP2 C-terminal domain.
  Wei J, Fain S, Harrison C, Feig LA, Baleja JD. Wei J, et al. Biochemistry. 2006 Jun 6;45(22):6826-34. doi: 10.1021/bi052655o. Biochemistry. 2006. PMID: 16734419 Free PMC article.
• C-terminal domains implicated in the functional surface expression of potassium channels.
  Jenke M, Sánchez A, Monje F, Stühmer W, Weseloh RM, Pardo LA. Jenke M, et al. EMBO J. 2003 Feb 3;22(3):395-403. doi: 10.1093/emboj/cdg035. EMBO J. 2003. PMID: 12554641 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Elsevier Science

• Other Literature Sources

  • The Lens - Patent Citations Database

• Research Materials

  • NCI CPTC Antibody Characterization Program

• Miscellaneous

  • NCI CPTAC Assay Portal