A novel role for XIAP in copper homeostasis through regulation of MURR1

被引:177
作者
Burstein, E
Ganesh, L
Dick, RD
van de Sluis, B
Wilkinson, JC
Klomp, LWJ
Wijmenga, C
Brewer, GJ
Nabel, GJ
Duckett, CS
机构
[1] Univ Michigan, Sch Med, Dept Pathol, Ann Arbor, MI 48109 USA
[2] Univ Michigan, Sch Med, Dept Internal Med, Ann Arbor, MI USA
[3] Univ Michigan, Sch Med, Dept Human Genet, Ann Arbor, MI USA
[4] Univ Michigan, Sch Med, Dept Biomed Genet, Ann Arbor, MI USA
[5] NIAID, Vaccine Res Ctr, NIH, Bethesda, MD 20892 USA
关键词
copper; MURR1; ubiquitin; XIAP;
D O I
10.1038/sj.emboj.7600031
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
XIAP is a potent suppressor of apoptosis that directly inhibits specific members of the caspase family of cysteine proteases. Here we demonstrate a novel role for XIAP in the control of intracellular copper levels. XIAP was found to interact with MURR1, a factor recently implicated in copper homeostasis. XIAP binds to MURR1 in a manner that is distinct from that utilized by XIAP to bind caspases, and consistent with this, MURR1 did not affect the antiapoptotic properties of XIAP. However, cells and tissues derived from Xiap-deficient mice were found to contain reduced copper levels, while suppression of MURR1 resulted in increased intracellular copper in cultured cells. Consistent with these opposing effects, XIAP was observed to negatively regulate MURR1 protein levels by the formation of K48 polyubiquitin chains on MURR1 that promote its degradation. These findings represent the first described phenotypic alteration in Xiap-deficient mice and demonstrate that XIAP can function through MURR1 to regulate copper homeostasis.
引用
收藏
页码:244 / 254
页数:11
相关论文
共 48 条
[1]   Ubiquitin: not just for proteasomes anymore [J].
Aguilar, RC ;
Wendland, B .
CURRENT OPINION IN CELL BIOLOGY, 2003, 15 (02) :184-190
[2]   XIAP inhibition of caspase-3 preserves its association with the Apaf-1 apoptosome and prevents CD95-and Bax-induced apoptosis [J].
Bratton, SB ;
Lewis, J ;
Butterworth, M ;
Duckett, C ;
Cohen, GM .
CELL DEATH AND DIFFERENTIATION, 2002, 9 (09) :881-892
[3]   Structural basis of caspase-7 inhibition by XIAP [J].
Chai, JJ ;
Shiozaki, E ;
Srinivasula, SM ;
Wu, Q ;
Dataa, P ;
Alnemri, ES ;
Shi, YG .
CELL, 2001, 104 (05) :769-780
[4]   AN APOPTOSIS-INHIBITING BACULOVIRUS GENE WITH A ZINC FINGER-LIKE MOTIF [J].
CROOK, NE ;
CLEM, RJ ;
MILLER, LK .
JOURNAL OF VIROLOGY, 1993, 67 (04) :2168-2174
[5]   Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain [J].
Deng, L ;
Wang, C ;
Spencer, E ;
Yang, LY ;
Braun, A ;
You, JX ;
Slaughter, C ;
Pickart, C ;
Chen, ZJ .
CELL, 2000, 103 (02) :351-361
[6]   X-linked IAP is a direct inhibitor of cell-death proteases [J].
Deveraux, QL ;
Takahashi, R ;
Salvesen, GS ;
Reed, JC .
NATURE, 1997, 388 (6639) :300-304
[7]   Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition [J].
Du, CY ;
Fang, M ;
Li, YC ;
Li, L ;
Wang, XD .
CELL, 2000, 102 (01) :33-42
[8]   Induction of nuclear factor kappa B by the CD30 receptor is mediated by TRAF1 and TRAF2 [J].
Duckett, CS ;
Gedrich, RW ;
Gilfillan, MC ;
Thompson, CB .
MOLECULAR AND CELLULAR BIOLOGY, 1997, 17 (03) :1535-1542
[9]   Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c [J].
Duckett, CS ;
Li, F ;
Wang, Y ;
Tomaselli, KJ ;
Thompson, CB ;
Armstrong, RC .
MOLECULAR AND CELLULAR BIOLOGY, 1998, 18 (01) :608-615
[10]   A NOVEL GENETIC SYSTEM TO DETECT PROTEIN PROTEIN INTERACTIONS [J].
FIELDS, S ;
SONG, OK .
NATURE, 1989, 340 (6230) :245-246