P-selectin and CD63 use different mechanisms for delivery to Weibel-Palade bodies

被引:63
作者
Harrison-Lavoie, KJ
Michaux, G
Hewlett, L
Kaur, J
Hannah, MJ
Lui-Roberts, WWY
Norman, KE
Cutler, DF
机构
[1] UCL, Cell Biol Unit, MRC Lab Mol Cell Biol, London WC1E 6BT, England
[2] Univ Sheffield, No Gen Hosp, Ctr Clin Sci, Sheffield S5 7AU, S Yorkshire, England
基金
英国医学研究理事会;
关键词
AP-3; CD63; LRO; P-selectin; secretory granules; von Willebrand factor;
D O I
10.1111/j.1600-0854.2006.00415.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The biogenesis of endothelial-specific Weibel-Palade bodies (WPB) is poorly understood, despite their key role in both haemostasis and inflammation. Biogenesis of specialized organelles of haemopoietic cells is often adaptor protein complex 3-dependent (AP-3-dependent), and AP-3 has previously been shown to play a role in the trafficking of both WPB membrane proteins, P-selectin and CD63. However, WPB are thought to form at the trans Golgi network (TGN), which is inconsistent with a role for AP-3, which operates in post-Golgi trafficking. We have therefore investigated in detail the mechanisms of delivery of these two membrane proteins to WPB. We find that P-selectin is recruited to forming WPB in the trans-Golgi by AP-3-independent mechanisms that use sorting information within both the cytoplasmic tail and the lumenal domain of the receptor. In contrast, CD63 is recruited to already-budded WPB by an AP-3-dependent route. These different mechanisms of recruitment lead to the presence of distinct immature and mature populations of WPB in human umbilical vein endothelial cells (HUVEC).
引用
收藏
页码:647 / 662
页数:16
相关论文
共 51 条
[1]   Weibel-Palade body membrane proteins exhibit differential trafficking after exocytosis in endothelial cells [J].
Arribas, M ;
Cutler, DF .
TRAFFIC, 2000, 1 (10) :783-793
[2]   Sorting and storage during secretory granule biogenesis: looking backward and looking forward [J].
Arvan, P ;
Castle, D .
BIOCHEMICAL JOURNAL, 1998, 332 :593-610
[3]   Lysosomal targeting of P-selectin is mediated by a novel sequence within its cytoplasmic tail [J].
Blagoveshchenskaya, AD ;
Norcott, JP ;
Cutler, DF .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (05) :2729-2737
[4]   A complex web of signal-dependent trafficking underlies the triorganellar distribution of P-selectin in neuroendocrine PC12 cells [J].
Blagoveshchenskaya, AD ;
Hewitt, EW ;
Cutler, DF .
JOURNAL OF CELL BIOLOGY, 1999, 145 (07) :1419-1433
[5]   Selective and signal-dependent recruitment of membrane proteins to secretory granules formed by heterologously expressed von Willebrand factor [J].
Blagoveshchenskaya, AD ;
Hannah, MJ ;
Allen, S ;
Cutler, DF .
MOLECULAR BIOLOGY OF THE CELL, 2002, 13 (05) :1582-1593
[6]   Biochemical analyses of trafficking with horseradish peroxidase-tagged chimeras [J].
Blagoveshchenskaya, AD ;
Cutler, DF .
APPLICATIONS OF CHIMERIC GENES AND HYBRID PROTEINS PT B: CELL BIOLOGY AND PHYSIOLOGY, 2000, 327 :45-60
[7]   Secretory lysosomes [J].
Blott, EJ ;
Griffiths, GM .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2002, 3 (02) :122-131
[8]  
BONFANTI R, 1989, BLOOD, V73, P1109
[9]   Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH [J].
Colomer, V ;
Kicska, GA ;
Rindler, MJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (01) :48-55
[10]   AP-3 adaptor functions in targeting P-selectin to secretory granules in endothelial cells [J].
Daugherty, BL ;
Straley, KS ;
Sanders, JM ;
Phillips, JW ;
Disdier, M ;
McEver, RP ;
Green, SA .
TRAFFIC, 2001, 2 (06) :406-413