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Items: 1 to 20 of 123

1.

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.

Mol Biol Cell. 1999 Feb;10(2):417-34.

2.

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.

J Cell Biol. 1997 Feb 24;136(4):811-21. Erratum in: J Cell Biol 1997 Apr 7;137(1):259.

3.

Ligand-induced clathrin-mediated endocytosis of the keratinocyte growth factor receptor occurs independently of either phosphorylation or recruitment of eps15.

Belleudi F, Visco V, Ceridono M, Leone L, Muraro R, Frati L, Torrisi MR.

FEBS Lett. 2003 Oct 23;553(3):262-70.

4.
5.

An endosomally localized isoform of Eps15 interacts with Hrs to mediate degradation of epidermal growth factor receptor.

Roxrud I, Raiborg C, Pedersen NM, Stang E, Stenmark H.

J Cell Biol. 2008 Mar 24;180(6):1205-18. doi: 10.1083/jcb.200708115.

6.

Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis.

Confalonieri S, Salcini AE, Puri C, Tacchetti C, Di Fiore PP.

J Cell Biol. 2000 Aug 21;150(4):905-12.

7.

Recycling of the epidermal growth factor receptor is mediated by a novel form of the clathrin adaptor protein Eps15.

Chi S, Cao H, Wang Y, McNiven MA.

J Biol Chem. 2011 Oct 7;286(40):35196-208. doi: 10.1074/jbc.M111.247577. Epub 2011 Aug 8.

8.

Clathrin, adaptors and eps15 in endosomes containing activated epidermal growth factor receptors.

Sorkina T, Bild A, Tebar F, Sorkin A.

J Cell Sci. 1999 Feb;112 ( Pt 3):317-27.

9.

AP-2/Eps15 interaction is required for receptor-mediated endocytosis.

Benmerah A, Lamaze C, Bègue B, Schmid SL, Dautry-Varsat A, Cerf-Bensussan N.

J Cell Biol. 1998 Mar 9;140(5):1055-62.

10.

c-Cbl directs EGF receptors into an endocytic pathway that involves the ubiquitin-interacting motif of Eps15.

de Melker AA, van der Horst G, Borst J.

J Cell Sci. 2004 Oct 1;117(Pt 21):5001-12. Epub 2004 Sep 21.

11.

eps15 and eps15R are essential components of the endocytic pathway.

Carbone R, Fré S, Iannolo G, Belleudi F, Mancini P, Pelicci PG, Torrisi MR, Di Fiore PP.

Cancer Res. 1997 Dec 15;57(24):5498-504.

12.

The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2.

Benmerah A, Gagnon J, Bègue B, Mégarbané B, Dautry-Varsat A, Cerf-Bensussan N.

J Cell Biol. 1995 Dec;131(6 Pt 2):1831-8.

13.

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

Cupers P, ter Haar E, Boll W, Kirchhausen T.

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

14.

Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery.

Martina JA, Bonangelino CJ, Aguilar RC, Bonifacino JS.

J Cell Biol. 2001 May 28;153(5):1111-20.

15.

Eps15 mediates vesicle trafficking from the trans-Golgi network via an interaction with the clathrin adaptor AP-1.

Chi S, Cao H, Chen J, McNiven MA.

Mol Biol Cell. 2008 Aug;19(8):3564-75. doi: 10.1091/mbc.E07-10-0997. Epub 2008 Jun 4.

16.

Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits.

Tebar F, Sorkina T, Sorkin A, Ericsson M, Kirchhausen T.

J Biol Chem. 1996 Nov 15;271(46):28727-30.

17.

Distinct recruitment of Eps15 via Its coiled-coil domain is required for efficient down-regulation of the met receptor tyrosine kinase.

Parachoniak CA, Park M.

J Biol Chem. 2009 Mar 27;284(13):8382-94. doi: 10.1074/jbc.M807607200. Epub 2008 Dec 24.

18.

Assembly of clathrin coats disrupts the association between Eps15 and AP-2 adaptors.

Cupers P, Jadhav AP, Kirchhausen T.

J Biol Chem. 1998 Jan 23;273(4):1847-50.

19.

Epidermal growth factor pathway substrate 15, Eps15.

Salcini AE, Chen H, Iannolo G, De Camilli P, Di Fiore PP.

Int J Biochem Cell Biol. 1999 Aug;31(8):805-9. Review.

PMID:
10481267
20.

STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes.

Bache KG, Raiborg C, Mehlum A, Stenmark H.

J Biol Chem. 2003 Apr 4;278(14):12513-21. Epub 2003 Jan 27.

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