Caspase-8 promotes cell motility and calpain activity under nonapoptotic conditions

被引:112
作者
Helfer, B
Boswell, BC
Finlay, D
Cipres, A
Vuori, K
Kang, TB
Wallach, D
Dorfleutner, A
Lahti, JM
Flynn, DC
Frisch, SM
机构
[1] W Virginia Univ, Babb Randolph Canc Ctr, Morgantown, WV 26506 USA
[2] W Virginia Univ, Dept Biochem, Morgantown, WV 26506 USA
[3] Burnham Inst, La Jolla, CA 92037 USA
[4] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
[5] St Jude Childrens Hosp, Dept Genet & Tumor Cell Biol, Memphis, TN 38105 USA
关键词
D O I
10.1158/0008-5472.CAN-05-4183
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Significant caspase-8 activity has been found in normal and certain tumor cells, suggesting that caspase-8 possesses an alternative, nonapoptotic function that may contribute to tumor progression. In this article, we report that caspase-8 promotes cell motility. In particular, caspase-8 is required for the optimal activation of calpains, Rac, and lamellipodial assembly. This represents a novel nonapoptotic function of caspase-8 acting at the intersection of the caspase-8 and calpain proteolytic pathways to coordinate cell death versus cell motility signaling.
引用
收藏
页码:4273 / 4278
页数:6
相关论文
共 58 条
[11]   MEKK1 regulates calpain-dependent proteolysis of focal adhesion proteins for rear-end detachment of migrating fibroblasts [J].
Cuevas, BD ;
Abell, AN ;
Witowsky, JA ;
Yujiri, T ;
Johnson, NL ;
Kesavan, K ;
Ware, M ;
Jones, PL ;
Weed, SA ;
DeBiasi, RL ;
Oka, Y ;
Tyler, KL ;
Johnson, GL .
EMBO JOURNAL, 2003, 22 (13) :3346-3355
[12]   Fas-induced proteolytic activation and intracellular redistribution of the stress-signaling kinase MEKK1 [J].
Deak, JC ;
Cross, JV ;
Lewis, M ;
Qian, YY ;
Parrott, LA ;
Distelhorst, CW ;
Templeton, DJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (10) :5595-5600
[13]   Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts [J].
Dourdin, N ;
Bhatt, AK ;
Dutt, P ;
Greer, PA ;
Arthur, JSC ;
Elce, JS ;
Huttenlocher, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (51) :48382-48388
[14]   Isoform specific function of calpain 2 in regulating membrane protrusion [J].
Franco, S ;
Perrin, B ;
Huttenlocher, A .
EXPERIMENTAL CELL RESEARCH, 2004, 299 (01) :179-187
[15]   Regulating cell migration: calpains make the cut [J].
Franco, SJ ;
Huttenlocher, A .
JOURNAL OF CELL SCIENCE, 2005, 118 (17) :3829-3838
[16]   Cytokinesis failure generating tetraploids promotes tumorigenesis in p53-null cells [J].
Fujiwara, T ;
Bandi, M ;
Nitta, M ;
Ivanova, EV ;
Bronson, RT ;
Pellman, D .
NATURE, 2005, 437 (7061) :1043-1047
[17]  
Fulda S, 1998, INT J CANCER, V76, P105
[18]   A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration [J].
Geisbrecht, ER ;
Montell, DJ .
CELL, 2004, 118 (01) :111-125
[19]   Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway [J].
Glading, A ;
Chang, P ;
Lauffenburger, DA ;
Wells, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (04) :2390-2398
[20]   Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation [J].
Glading, A ;
Bodnar, RJ ;
Reynolds, IJ ;
Shiraha, H ;
Satish, L ;
Potter, DA ;
Blair, HC ;
Wells, A .
MOLECULAR AND CELLULAR BIOLOGY, 2004, 24 (06) :2499-2512