The Anp32 family of proteins containing leucine-rich repeats

被引:94
作者
Matilla, A
Radrizzani, M
机构
[1] UCL, Inst Child Hlth, London WC1N 1EH, England
[2] UBA, FCEyN, IIB, Fdn Inst Leloir, Buenos Aires, DF, Argentina
[3] ANLIS, Ctr Nacl Genet Med, Buenos Aires, DF, Argentina
关键词
Anp32; Lanp; Cpd1; leucine-rich repeats; signal transduction;
D O I
10.1080/14734220410019020
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Herein we describe the characteristic features of the Anp32 family represented by the cerebellar leucine-rich repeat protein (Lanp) and the cerebellar developmental-regulated protein 1 (Cpd1). The Anp32 family consists of 32 evolutionarily conserved proteins and is included within the superfamily of leucine-rich repeat (LRR) proteins characterized by the presence of tandem arrays of a LRR, a structural motif implicated in the mediation of protein protein interactions. We describe three novel human Anp32 proteins, reveal the evolutionary relationships of the members of the Anp32 family, provide insights into their biochemical and structural properties, and review their macromolecular interactions, substrate specificities, tissue distribution/expression patterns, and physiological and pathological roles. Recent findings indicate a conserved role of members of the Anp32 family during evolution in the modulation of cell signalling and transduction of gene expression to regulate the morphology and dynamics of the cytoskeleton, cell adhesion, neural development or cerebellar morphogenesis.
引用
收藏
页码:7 / 18
页数:12
相关论文
共 68 条
[31]  
Kins S, 2001, J BIOL CHEM, V276, P38193
[32]   Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A [J].
Kobe, B ;
Deisenhofer, J .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 264 (05) :1028-1043
[33]   The leucine-rich repeat as a protein recognition motif [J].
Kobe, B ;
Kajava, AV .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2001, 11 (06) :725-732
[34]   CRYSTAL-STRUCTURE OF PORCINE RIBONUCLEASE INHIBITOR, A PROTEIN WITH LEUCINE-RICH REPEATS [J].
KOBE, B ;
DEISENHOFER, J .
NATURE, 1993, 366 (6457) :751-756
[35]   Partial purification and characterization of a protein kinase that is activated by nuclear localization signal peptides [J].
Kurihara, T ;
Hori, M ;
Takeda, H ;
Inoue, M ;
Yoneda, Y .
FEBS LETTERS, 1996, 380 (03) :241-245
[36]   Protein phosphatase 2A inhibition induces cerebellar long-term depression and declustering of synaptic AMPA receptor [J].
Launey, T ;
Endo, S ;
Sakai, R ;
Harano, J ;
Ito, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (02) :676-681
[37]  
LETUNIC I, 2004, NUCLEIC ACIDS RES, V32
[38]   Molecular identification of I-1(PP2A), a novel potent heat-stable inhibitor protein of protein phosphatase 2A [J].
Li, M ;
Makkinje, A ;
Damuni, Z .
BIOCHEMISTRY, 1996, 35 (22) :6998-7002
[39]   PURIFICATION AND CHARACTERIZATION OF 2 POTENT HEAT-STABLE PROTEIN INHIBITORS OF PROTEIN PHOSPHATASE 2A FROM BOVINE KIDNEY [J].
LI, M ;
GUO, H ;
DAMUNI, Z .
BIOCHEMISTRY, 1995, 34 (06) :1988-1996
[40]   Protein phosphatase 2A and its B56 regulatory subunit inhibit Wnt signaling in Xenopus [J].
Li, XH ;
Yost, HJ ;
Virshup, DM ;
Seeling, JM .
EMBO JOURNAL, 2001, 20 (15) :4122-4131