Vertebrate GLD2 poly(A) polymerases in the germline and the brain

被引:82
作者
Rouhana, L
Wang, LT
Buter, N
Kwak, JE
Schiltz, CA
Gonzalez, T
Kelley, AE
Landry, CF
Wickens, M [1 ]
机构
[1] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA
[2] Univ Wisconsin, Genet Lab, Madison, WI 53706 USA
[3] Univ Wisconsin, Dept Psychiat, Madison, WI 53706 USA
关键词
poly(A) polymerase; GLD2; translational control;
D O I
10.1261/rna.2630205
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
Cytoplasmic polyadenylation is important in the control of mRNA stability and translation, and for early animal development and synaptic plasticity. Here, we focus on vertebrate poly(A) polymerases that are members of the recently described GLD2 family. We identify and characterize two closely related GLD2 proteins in Xenopus oocytes, and show that they possess PAP activity in vivo and in vitro and that they bind known polyadenylation factors and mRNAs known to receive poly(A) during development. We propose that at least two distinct polyadenylation complexes exist in Xenopus oocytes, one of which contains GLD2; the other, maskin and Pumilio. GLD2 protein interacts with the polyadenylation factor, CPEB, in a conserved manner. mRNAs that encode GLD2 in mammals are expressed in many tissues. In the brain, mouse, and human GLD2 mRNAs are abundant in anatomical regions necessary for long-term cognitive and emotional learning. In the hippocampus, mouse GLD2 mRNA colocalizes with CPEB1 and Pumilio1 mRNAs, both of which are likely involved in synaptic plasticity. We suggest that mammalian GLD2 poly(A) polymerases are important in synaptic translation, and in polyadenylation throughout the soma.
引用
收藏
页码:1117 / 1130
页数:14
相关论文
共 67 条
[1]   Selective modulation of some forms of Schaffer collateral-CA1 synaptic plasticity in mice with a disruption of the CPEB-1 gene [J].
Alarcon, JM ;
Hodgman, R ;
Theis, M ;
Huang, YS ;
Kandel, ER ;
Richter, JD .
LEARNING & MEMORY, 2004, 11 (03) :318-327
[2]   Phosphoesterase domains associated with DNA polymerases of diverse origins [J].
Aravind, L ;
Koonin, EV .
NUCLEIC ACIDS RESEARCH, 1998, 26 (16) :3746-3752
[3]  
BALLANTYNE S, 1995, RNA, V1, P64
[4]   A dependent pathway of cytoplasmic polyadenylation reactions linked to cell cycle control by c-mos and CDK1 activation [J].
Ballantyne, S ;
Daniel, DL ;
Wickens, M .
MOLECULAR BIOLOGY OF THE CELL, 1997, 8 (08) :1633-1648
[5]   Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation [J].
Barnard, DC ;
Ryan, K ;
Manley, JL ;
Richter, JD .
CELL, 2004, 119 (05) :641-651
[6]   Binding specificity and mRNA targets of a C-elegans PUF protein, FBF-1 [J].
Bernstein, D ;
Hook, B ;
Hajarnavis, A ;
Opperman, L ;
Wickens, M .
RNA, 2005, 11 (04) :447-458
[7]   NUCLEAR POLYADENYLATION FACTORS RECOGNIZE CYTOPLASMIC POLYADENYLATION ELEMENTS [J].
BILGER, A ;
FOX, CA ;
WAHLE, E ;
WICKENS, M .
GENES & DEVELOPMENT, 1994, 8 (09) :1106-1116
[8]  
Dehlin E, 1996, MOL CELL BIOL, V16, P468
[9]  
Dickson KS, 1999, MOL CELL BIOL, V19, P5707
[10]   Poly(A) polymerase and the regulation of cytoplasmic polyadenylation [J].
Dickson, KS ;
Thompson, SR ;
Gray, NK ;
Wickens, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (45) :41810-41816