QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 30 March 2004
doi: 10.1242/jcs.01062

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.01062v1 117/10/2051    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Barth, M. Articles by Holstein, S. E. H. Search for Related Content PubMed PubMed Citation Articles by Barth, M. Articles by Holstein, S. E. H. Social Bookmarking                         What's this?

Identification and functional characterization of Arabidopsis AP180, a binding partner of plant C-adaptin

University of Heidelberg, Department of Cell Biology, Heidelberg Institute for Plant Sciences, 69120 Heidelberg, Im Neuenheimer Feld 230, Germany

^* Author for correspondence (e-mail: susanne_h.holstein{at}urz.uni-heidelberg.de)

Accepted 17 December 2003

Clathrin-mediated endocytosis is a well-studied uptake mechanism for nutrients and signalling receptors in mammalian cells that depends on the coordinated interaction of coat proteins and endocytic network proteins to perform the internalization. In this process AP180 promotes the assembly of clathrin triskelia into coated membrane patches at the plasma membrane, while -adaptin interacts with various network proteins that are in turn required for the budding of the coated pits. The process of clathrin-mediated endocytosis in plants has not been dissected at the molecular level, nor have the members of an analogous uptake machinery been functionally described. In this respect, we have investigated the AP180 and -adaptin orthologs from Arabidopsis thaliana: At-AP180 and At-C-Ad. Both plant proteins display the same structural features as their mammalian counterparts and fulfill the same basic functions. To identify their interacting partners, the ear region of At-C-Ad and the C-terminal region of At-AP180 were used as fusion proteins in pull-down experiments and plasmon-resonance measurements. At-C-Ad binds several mammalian endocytic proteins, and its interaction with At-AP180 requires the DPF motif. At-AP180 functions as a clathrin assembly protein that promotes the formation of cages with an almost uniform size distribution. Deletion of the single DLL motif abolished the assembly activity of At-AP180 almost completely, but did not affect its binding to triskelia, suggesting the existence of additional binding determinants.

Key words: -Adaptin, AP180, Network-proteins, Endocytic clathrin-machinery, Clathrin reassembly

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

This article has been cited by other articles:

				D. G. Robinson, L. Jiang, and K. Schumacher The Endosomal System of Plants: Charting New and Familiar Territories Plant Physiology, August 1, 2008; 147(4): 1482 - 1492. [Full Text] [PDF]

				C. A. Konopka, S. K. Backues, and S. Y. Bednarek Dynamics of Arabidopsis Dynamin-Related Protein 1C and a Clathrin Light Chain at the Plasma Membrane PLANT CELL, May 1, 2008; 20(5): 1363 - 1380. [Abstract] [Full Text] [PDF]

				J. Samaj, F. Baluska, B. Voigt, M. Schlicht, D. Volkmann, and D. Menzel Endocytosis, Actin Cytoskeleton, and Signaling Plant Physiology, July 1, 2004; 135(3): 1150 - 1161. [Full Text] [PDF]