Annexin XIIIb associates with lipid microdomains to function in apical delivery

被引:150
作者
Lafont, F
Lecat, S
Verkade, P
Simons, K
机构
[1] European Mol Biol Lab, Cell Biol & Biophys Programme, D-69012 Heidelberg, Germany
[2] Max Planck Inst Mol Cell Biol & Genet, Dresden, Germany
关键词
cholesterol; exocytosis; MDCK; polarity; raft;
D O I
10.1083/jcb.142.6.1413
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A member of the annexin XIII sub-family, annexin XIIIb, has been implicated in the apical exocytosis of epithelial kidney cells. Annexins are phospholipid-binding proteins that have been suggested to be involved in membrane trafficking events although their actual physiological function remains open. Unlike the other annexins, annexin XIIIs are myristoylated, Here, we show by immunoelectron microscopy that annexin XIIIb is localized to the trans-Golgi network (TGN), vesicular carriers and the apical cell surface. Polarized apical sorting involves clustering of apical proteins into dynamic sphingolipid-cholesterol rafts. We now provide evidence for the raft association of annexin XIIIb, Using in vitro assays and either myristoylated or unmyristoylated recombinant annexin XIIIb, we demonstrate that annexin XIIIb in its native myristoylated form stimulates specifically apical transport whereas the unmyristoylated form inhibits this route, Moreover, we show that formation of apical carriers from the TGN is inhibited by an anti-annexin XIIIb antibody whereas it is stimulated by myristoylated recombinant annexin XIIIb, These results suggest that annexin XIIIb directly participates in apical delivery.
引用
收藏
页码:1413 / 1427
页数:15
相关论文
共 81 条
[1]   On the origin of sphingolipid/cholesterol-rich detergent-insoluble cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes [J].
Ahmed, SN ;
Brown, DA ;
London, E .
BIOCHEMISTRY, 1997, 36 (36) :10944-10953
[2]   A ROLE FOR CALPACTIN IN CALCIUM-DEPENDENT EXOCYTOSIS IN ADRENAL CHROMAFFIN CELLS [J].
ALI, SM ;
GEISOW, MJ ;
BURGOYNE, RD .
NATURE, 1989, 340 (6231) :313-315
[3]   DEVELOPMENT OF CELL-SURFACE POLARITY IN THE EPITHELIAL MADIN-DARBY CANINE KIDNEY (MDCK) CELL-LINE [J].
BALCAROVASTANDER, J ;
PFEIFFER, SE ;
FULLER, SD ;
SIMONS, K .
EMBO JOURNAL, 1984, 3 (11) :2687-2694
[4]   SEMI-INTACT CELLS PERMEABLE TO MACROMOLECULES - USE IN RECONSTITUTION OF PROTEIN-TRANSPORT FROM THE ENDOPLASMIC-RETICULUM TO THE GOLGI-COMPLEX [J].
BECKERS, CJM ;
KELLER, DS ;
BALCH, WE .
CELL, 1987, 50 (04) :523-534
[5]   RELEASE OF PUTATIVE EXOCYTIC TRANSPORT VESICLES FROM PERFORATED MDCK CELLS [J].
BENNETT, MK ;
WANDINGERNESS, A ;
SIMONS, K .
EMBO JOURNAL, 1988, 7 (13) :4075-4085
[6]  
Benz J, 1997, BIOL CHEM, V378, P177
[7]   CHARACTERIZATION OF CA-2+-DEPENDENT PHOSPHOLIPID BINDING, VESICLE AGGREGATION AND MEMBRANE-FUSION BY ANNEXINS [J].
BLACKWOOD, RA ;
ERNST, JD .
BIOCHEMICAL JOURNAL, 1990, 266 (01) :195-200
[8]   Myristoylation [J].
Boutin, JA .
CELLULAR SIGNALLING, 1997, 9 (01) :15-35
[9]   Structure of detergent-resistant membrane domains: Does phase separation occur in biological membranes? [J].
Brown, DA ;
London, E .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1997, 240 (01) :1-7
[10]   SORTING OF GPI-ANCHORED PROTEINS TO GLYCOLIPID-ENRICHED MEMBRANE SUBDOMAINS DURING TRANSPORT TO THE APICAL CELL-SURFACE [J].
BROWN, DA ;
ROSE, JK .
CELL, 1992, 68 (03) :533-544