Cyclin T: Three forms for different roles in physiological and pathological functions

被引:46
作者
De Luca, A
De Falco, M
Baldi, A
Paggi, MG
机构
[1] Regina Elena Inst Canc Res, Ctr Expt Res, Lab C, Dept Dev Therapeut Programs, I-00158 Rome, Italy
[2] Univ Naples Federico II, Dept Evolut & Comparat Biol, Naples, Italy
关键词
D O I
10.1002/jcp.10196
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cyclins are members of family of proteins involved in the cell cycle regulation. They are regulatory subunits of complexes with proteins called cyclin-dependent kinases (CDKs). There are three forms of cyclin T: cyclin T1, cyclin T2a, and T2b. All cyclin T contain an N-terminal "cyclin homology box," the most conserved region among different members of the cyclin family that serves to bind CDK9. In addition to the N-terminal cyclin domain, cyclin T contains a putative coiled-coil motif, a His-rich motif, and a C-terminal PEST sequence. The CDK9/cyclin T complex is able to activate gene expression in a catalytic-dependent manner, phosphorylating the carboxy-terminal domain (CTD) of RNA polymerase II. In addition, only cyclin T1 supports interactions between Tat and TAR. The interaction of Tat with cyclin T1 alters the conformation of Tat to enhance the affinity and specificity of the Tat:TAR interaction. On the other hand, CDK9/cyclin T2 complexes are involved in the regulation of terminal differentiation in muscle cells. (C) 2002 Wiley-Liss, Inc.
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页码:101 / 107
页数:7
相关论文
共 69 条
[1]  
Bagella L, 1998, J CELL PHYSIOL, V177, P206, DOI 10.1002/(SICI)1097-4652(199811)177:2<206::AID-JCP2>3.0.CO
[2]  
2-R
[3]  
Bazan JF, 1996, PROTEINS, V24, P1
[4]   REGULATION OF TRANSCRIPTIONAL ELONGATION BY RNA-POLYMERASE-II [J].
BENTLEY, DL .
CURRENT OPINION IN GENETICS & DEVELOPMENT, 1995, 5 (02) :210-216
[5]   Synergistic enhancement of both initiation and elongation by acidic transcription activation domains [J].
Blair, WS ;
Fridell, RA ;
Cullen, BR .
EMBO JOURNAL, 1996, 15 (07) :1658-1665
[6]   HIV-1 auxiliary proteins: Making connections in a dying cell [J].
Cullen, BR .
CELL, 1998, 93 (05) :685-692
[7]   THE ROLE OF MULTISITE PHOSPHORYLATION IN THE REGULATION OF RNA-POLYMERASE-II ACTIVITY [J].
DAHMUS, ME .
PROGRESS IN NUCLEIC ACID RESEARCH AND MOLECULAR BIOLOGY, VOL 48, 1994, 48 :143-179
[8]   PHOSPHORYLATION OF THE C-TERMINAL DOMAIN OF RNA-POLYMERASE-II [J].
DAHMUS, ME .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 1995, 1261 (02) :171-182
[9]  
De Falco G, 1998, J CELL PHYSIOL, V177, P501, DOI 10.1002/(SICI)1097-4652(199812)177:4<501::AID-JCP1>3.0.CO
[10]  
2-4