Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M410752200 on December 14, 2004

J. Biol. Chem., Vol. 280, Issue 8, 7309-7316, February 25, 2005
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
280/8/7309    most recent
M410752200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wernick, N. L. B.
Right arrow Articles by Simister, N. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wernick, N. L. B.
Right arrow Articles by Simister, N. E.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Recognition of the Tryptophan-based Endocytosis Signal in the Neonatal Fc Receptor by the µ Subunit of Adaptor Protein-2*

Naomi L. B. Wernick{ddagger}, Volker Haucke§, and Neil E. Simister{ddagger}

From the {ddagger}Rosenstiel Center for Basic Biomedical Sciences and Department of Biology, Brandeis University, Waltham, Massachusetts 02254-9110 and the §Free University Berlin, Institute of Chemistry-Biochemistry, Takustrasse 6, Berlin 14195, Germany

Endocytosis of membrane proteins is typically mediated by signals present in their cytoplasmic domains. These signals usually contain an essential tyrosine or pair of leucine residues. Both tyrosine- and dileucine-based endocytosis signals are recognized by the adaptor complex AP-2. The best understood of these interactions occurs between the tyrosine-based motif, YXX{Phi}, and the µ2 subunit of AP-2. We recently reported a tryptophan-based endocytosis signal, WLSL, contained within the cytoplasmic domain of the neonatal Fc receptor. This signal resembles YXX{Phi}. We have investigated the mechanism by which the tryptophan-based signal is recognized. Both interaction assays in vitro and endocytosis assays in vivo show that µ2 binds the tryptophan-based signal. Furthermore, the WLSL sequence binds the same site as YXX{Phi}. Unlike the WXXF motif, contained in stonin 2 and other endocytic proteins, WLSL does not bind the {alpha} subunit of AP-2. These observations reveal a functional similarity between the tryptophan-based endocytosis signal and the YXX{Phi} motif, and an unexpected versatility of µ2 function.


Received for publication, September 17, 2004 , and in revised form, December 7, 2004.

* This work was supported by National Institutes of Health Grant HD27691. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Brandeis University MS 029, Waltham, MA 02254-9110. Tel.: 781-736-4952; Fax: 781-736-2405; E-mail: simister{at}brandeis.edu.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. Y. Cha, S. Maddileti, N. Mitin, T. K. Harden, and C. J. Der
Aberrant Receptor Internalization and Enhanced FRS2-dependent Signaling Contribute to the Transforming Activity of the Fibroblast Growth Factor Receptor 2 IIIb C3 Isoform
J. Biol. Chem., March 6, 2009; 284(10): 6227 - 6240.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
L. Ye, X. Liu, S. N. Rout, Z. Li, Y. Yan, L. Lu, T. Kamala, N. K. Nanda, W. Song, S. K. Samal, et al.
The MHC Class II-Associated Invariant Chain Interacts with the Neonatal Fc{gamma} Receptor and Modulates Its Trafficking to Endosomal/Lysosomal Compartments
J. Immunol., August 15, 2008; 181(4): 2572 - 2585.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
G. Vidarsson, A. M. Stemerding, N. M. Stapleton, S. E. Spliethoff, H. Janssen, F. E. Rebers, M. de Haas, and J. G. van de Winkel
FcRn: an IgG receptor on phagocytes with a novel role in phagocytosis
Blood, November 15, 2006; 108(10): 3573 - 3579.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
E. E. Newton, Z. Wu, and N. E. Simister
Characterization of basolateral-targeting signals in the neonatal Fc receptor
J. Cell Sci., June 1, 2005; 118(11): 2461 - 2469.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement