STAM/EAST/Hbp adapter proteins - integrators of signalling pathways

被引:42
作者
Lohi, O
Lehto, VP [1 ]
机构
[1] Univ Oulu, Dept Pathol, PL 5000, FIN-90014 Oulu, Finland
[2] Univ Tampere, Dept Pediat, PL 2000, FIN-33521 Tampere, Finland
关键词
adapter; EAST; endocytosis; Hbp; receptor; STAM;
D O I
10.1016/S0014-5793(01)03079-4
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
STAM/EAST/Hbp family of proteins consists of eight members well conserved from yeast to mammals. The basic domain architecture is comprised of an N-terminal Vps27, Hrs and STAM homology domain, a ubiquitin-interacting motif and a central Src homology-3 domain. Vertebrate members also carry an immunoreceptor tyrosine-based activation motif. STAM/EAST/Hbp proteins become tyrosine-phosphorylated by a variety of cytokines and growth factors. STAM 1 and STAM 2A are involved in cytokine-mediated signalling for DNA synthesis and e-myc induction. EAST and STAM 2A/Hbp play a role in receptor-mediated endo- and exocytosis and probably also in the regulation of actin cytoskeleton. Knockout experiments implicate a role for STAM 1 in neural cell survival. A picture is emerging of STAM/EAST/Hbp proteins acting as integrators of thus far mechanistically disparate cellular signalling events. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:287 / 290
页数:4
相关论文
共 33 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 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
[3]  
Carbone R, 1997, CANCER RES, V57, P5498
[4]   Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor [J].
Chin, LS ;
Raynor, MC ;
Wei, XL ;
Chen, HQ ;
Li, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (10) :7069-7078
[5]   MODULAR BINDING DOMAINS IN SIGNAL-TRANSDUCTION PROTEINS [J].
COHEN, GB ;
REN, RB ;
BALTIMORE, D .
CELL, 1995, 80 (02) :237-248
[6]   Yeast Eps15-like endocytic protein, Pan1p, activates the Arp2/3 complex [J].
Duncan, MC ;
Cope, MJTV ;
Goode, BL ;
Wendland, B ;
Drubin, DG .
NATURE CELL BIOLOGY, 2001, 3 (07) :687-690
[7]   STAM2, a new member of the STAM family, binding to the Janus kinases [J].
Endo, K ;
Takeshita, T ;
Kasai, H ;
Sasaki, Y ;
Tanaka, N ;
Asao, H ;
Kikuchi, K ;
Yamada, M ;
Chen, M ;
O'Shea, JJ ;
Sugamura, K .
FEBS LETTERS, 2000, 477 (1-2) :55-61
[8]   Phosphorylation of a 72-kDa protein in PDGF-stimulated cells which forms complex with c-Crk, c-Fyn and Eps15 [J].
Hansen, K ;
Ronnstrand, L ;
ClaessonWelsh, L ;
Heldin, CH .
FEBS LETTERS, 1997, 409 (02) :195-200
[9]   A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems [J].
Hofmann, K ;
Falquet, L .
TRENDS IN BIOCHEMICAL SCIENCES, 2001, 26 (06) :347-350