Hrs and Hbp: Possible regulators of endocytosis and exocytosis

被引:33
作者
Komada, M [1 ]
Kitamura, N [1 ]
机构
[1] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Sci Biol, Midori Ku, Yokohama, Kanagawa 2268501, Japan
关键词
Hrs; Hbp; endocytosis; exocytosis; FYVE domain; VHS domain; phosphatidylinositol; 3-phosphate; early endosome;
D O I
10.1006/bbrc.2001.4441
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The molecular mechanisms of endocytosis and exocytosis are not yet fully understood. Hrs and Hbp, two tightly associated proteins in eukaryotic cells, have been implicated in these cellular processes. Hrs is homologous to Vps27p, an endosomal protein required for vacuolar and endocytic trafficking in yeast. Hrs is localized to early endosomes and is required for the normal morphology of early endosomes in mammalian cells. Hrs also associates with proteins implicated in endocytosis and exocytosis such as SNAP-25 and Eps15. Hrs treatment inhibits neurotransmitter release in permeabilized neuronal cells and its overexpression inhibits internalization of transferrin; Overexpression of dominant-negative Hbp mutants inhibits ligand-induced downregulation of growth factor/receptor complexes and immunoglobulin E receptor-triggered degranulation of secretory granules in mast cells. These observations suggest an important role for the Hrs/Hbp protein complex in vesicular trafficking during endocytosis and exocytosis. (C) 2001 Academic Press.
引用
收藏
页码:1065 / 1069
页数:5
相关论文
共 32 条
[1]   Hrs is associated with STAM, a signal-transducing adaptor molecule - Its suppressive effect on cytokine-induced cell growth [J].
Asao, H ;
Sasaki, Y ;
Arita, T ;
Tanaka, N ;
Endo, K ;
Kasai, H ;
Takeshita, T ;
Endo, Y ;
Fujita, T ;
Sugamura, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (52) :32785-32791
[2]   Hrs-2 is an ATPase implicated in calcium-regulated secretion [J].
Bean, AJ ;
Seifert, R ;
Chen, YA ;
Sacks, R ;
Scheller, RH .
NATURE, 1997, 385 (6619) :826-829
[3]   Hrs-2 regulates receptor-mediated endocytosis via interactions with Eps15 [J].
Bean, AJ ;
Davanger, S ;
Chou, MF ;
Gerhardt, B ;
Tsujimoto, S ;
Chang, YC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (20) :15271-15278
[4]   Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains [J].
Burd, CG ;
Emr, SD .
MOLECULAR CELL, 1998, 2 (01) :157-162
[5]   FYVE fingers bind Ptdins(3)P [J].
Gaullier, JM ;
Simonsen, A ;
D'Arrigo, A ;
Bremnes, B ;
Stenmark, H ;
Aasland, R .
NATURE, 1998, 394 (6692) :432-433
[6]   Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells [J].
Guo, ZH ;
Turner, C ;
Castle, D .
CELL, 1998, 94 (04) :537-548
[7]   Early endosomal localization of hrs requires a sequence within the proline- and glutamine-rich region but not the FYVE finger [J].
Hayakawa, A ;
Kitamura, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (38) :29636-29642
[8]   The PCI domain: a common theme in three multiprotein complexes [J].
Hofmann, K ;
Bucher, P .
TRENDS IN BIOCHEMICAL SCIENCES, 1998, 23 (06) :204-205
[9]   A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP [J].
Kato, M ;
Miyazawa, K ;
Kitamura, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (48) :37481-37487
[10]  
KOMADA M, 1995, MOL CELL BIOL, V15, P6213