HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science 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 ISI Web of Science (1) Citing Articles via Google Scholar Google Scholar Articles by Kusner, L. Articles by Carlin, C. Search for Related Content PubMed PubMed Citation Articles by Kusner, L. Articles by Carlin, C.

PROTEIN AND VESICLE TRAFFICKING, CYTOSKELETON

Potential role for a novel AP180-related protein during endocytosis in MDCK cells

¹Department of Physiology and Biophysics and ²Case Western Reserve University Cancer Center, School of Medicine, Case Western Reserve University, and ³Rainbow Center for Childhood Polycystic Kidney Disease at Rainbow Babies and Children's Hospital of Cleveland, Cleveland, Ohio 44106

Submitted 27 February 2003 ; accepted in final form 17 June 2003

Clathrin assembly protein, AP180, was originally identified as a brain-specific protein localized to the presynaptic junction. AP180 acts to limit vesicle size and maintain a pool of releasable synaptic vesicles during rapid recycling. In this study, we show that polarized epithelial Madin-Darby canine kidney (MDCK) cells express two AP180-related proteins: the ubiquitously expressed 62-kDa clathrin assembly lymphoid myeloid leukemia (CALM, AP180-2) protein and a novel high-molecular-weight homolog that we have named AP180-3. Sequence analysis of AP180-3 expressed in MDCK cells shows high homology to AP180 from rat brain. AP180-3 contains conserved motifs found in brain-specific AP180, including the epsin NH₂-terminal homology (ENTH) domain, the binding site for the -subunit of AP-2, and DLL repeats. Our studies show that AP180-3 from MDCK cells forms complexes with AP-2 and clathrin and that membrane recruitment of these complexes is modulated by phosphorylation. We demonstrate by immunohistochemistry that AP180-3 is localized to cytoplasmic vesicles in MDCK cells and is also present in tubule epithelial cells from mouse kidney. We observed by immunodetection that a high-molecular-weight AP180-related protein is expressed in numerous cells in addition to MDCK cells.

clathrin assembly lympoid myeloid leukemia; kidney epithelial cells; epsin NH₂-terminal homology domain; DLL repeats; clathrin; AP-2

This article has been cited by other articles:

				J. Z. Rappoport, S. Kemal, A. Benmerah, and S. M. Simon Dynamics of clathrin and adaptor proteins during endocytosis Am J Physiol Cell Physiol, November 1, 2006; 291(5): C1072 - C1081. [Abstract] [Full Text] [PDF]