The Anaphase Promoting Complex Induces Substrate Degradation during Neuronal Differentiation

被引:32
作者
Harmey, Dympna [1 ]
Smith, Anthony [1 ]
Simanski, Scott [1 ]
Moussa, Carole Zaki [1 ]
Ayad, Nagi G. [1 ]
机构
[1] Scripps Res Inst, Dept Canc Biol, Jupiter, FL 33458 USA
关键词
CELL-CYCLE EXIT; S-PHASE ENTRY; UBIQUITIN LIGASE; POSTMITOTIC NEURONS; AXONAL GROWTH; MITOSIS; ACCUMULATION; PROTEOLYSIS; PROTEIN; SKP2;
D O I
10.1074/jbc.M804944200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
The anaphase promoting complex (APC) is an E3 ubiquitin ligase required for the metaphase-to-anaphase transition and mitotic exit. However, APC also plays roles in G(1), where it is regulated by Cdh1, and APC activity has also been detected in differentiated and non-proliferating cells, suggesting that it may play roles outside the cell cycle. Here, we report that disrupting APC(Cdh1) activity inhibits neurite outgrowth of both PC12 pheochromocytoma cells and primary cerebellar granule cells. APC(Cdh1) activity dramatically increases as PC12 cells differentiate in response to nerve growth factor. Furthermore, a key target degraded by APC(Cdh1) following nerve growth factor treatment is the F-box protein Skp2, and APC(Cdh1)-mediated destruction of Skp2 is essential for proper terminal differentiation of neuronal precursors.
引用
收藏
页码:4317 / 4323
页数:7
相关论文
共 35 条
[1]
Cdh1/Hct1-APC is essential for the survival of postmitotic neurons [J].
Almeida, A ;
Bolaños, JP ;
Moreno, S .
JOURNAL OF NEUROSCIENCE, 2005, 25 (36) :8115-8121
[2]
Degradation of origin recognition complex large subunit by the anaphase-promoting complex in Drosophila [J].
Araki, M ;
Wharton, RP ;
Tang, ZY ;
Yu, HT ;
Asano, M .
EMBO JOURNAL, 2003, 22 (22) :6115-6126
[3]
Identification of ubiquitin ligase substrates by in vitro expression cloning [J].
Ayad, NG ;
Rankin, S ;
Ooi, D ;
Rape, M ;
Kirschner, MW .
UBIQUITIN AND PROTEIN DEGRADATION, PT B, 2005, 399 :404-+
[4]
RETRACTED: Treatment of PC12 cells with nerve growth factor induces proteasomal degradation of T-cadherin that requires tyrosine phosphorylation of its cadherin domain (Retracted article. See vol. 293, pg. 3590, 2018) [J].
Bai, Shoumei ;
Datta, Jharna ;
Jacob, Samson T. ;
Ghoshal, Kalpana .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (37) :27171-27180
[5]
Control of the SCFSkp2-Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase [J].
Bashir, T ;
Dorrello, NV ;
Amador, V ;
Guardavaccaro, D ;
Pagano, M .
NATURE, 2004, 428 (6979) :190-193
[6]
Retinoblastoma protein and anaphase-promoting complex physically interact and functionally cooperate during cell-cycle exit [J].
Binne, Ulrich K. ;
Classon, Marie K. ;
Dick, Frederick A. ;
Wei, Wenyi ;
Rape, Michael ;
Kaelin, William G., Jr. ;
Naar, Anders M. ;
Dyson, Nicholas J. .
NATURE CELL BIOLOGY, 2007, 9 (02) :225-U140
[7]
The proteolysis of mitotic cyclins in mammalian cells persists from the end of mitosis until the onset of S phase [J].
Brandeis, M ;
Hunt, T .
EMBO JOURNAL, 1996, 15 (19) :5280-5289
[8]
SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27 [J].
Carrano, AC ;
Eytan, E ;
Hershko, A ;
Pagano, M .
NATURE CELL BIOLOGY, 1999, 1 (04) :193-199
[9]
Retinoic acid downregulates Rae1 leading to APCCdh1 activation and neuroblastoma SH-SY5Y differentiation [J].
Cuende, J. ;
Moreno, S. ;
Bolanos, J. P. ;
Almeida, A. .
ONCOGENE, 2008, 27 (23) :3339-3344
[10]
p27Kip1 alters the response of cells to mitogen and is part of a cell-intrinsic timer that arrests the cell cycle and initiates differentiation [J].
Durand, B ;
Fero, ML ;
Roberts, JM ;
Raff, MC .
CURRENT BIOLOGY, 1998, 8 (08) :431-440