Characterization of KIBRA, a novel WW domain-containing protein

被引：125

作者：

Kremerskothen, J

Plaas, C

Büther, K

Finger, I

Veltel, S

Matanis, T

Liedtke, T

Barnekow, A

机构：

[1] Univ Munster, Dept Expt Tumorbiol, D-48149 Munster, Germany

[2] Univ Munster, Inst Anat, AG Mol Neurobiol, D-48149 Munster, Germany

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 300卷 / 04期

关键词：

WW domain; PPxY motif; C2; domain; calcium binding; phage display; synaptic architecture;

D O I：

10.1016/S0006-291X(02)02945-5

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：

In a yeast two hybrid screen with the human isoform of Dendrin (KIAA0749), a putative modulator of the postsynaptic cytoskeleton, we isolated a cDNA coding for a novel protein, KIBRA, possessing two amino-terminal WW domains, an internal C-2-like domain and a carboxy-terminal glutamic acid-rich stretch. Northern blot analysis revealed that the expression of KIBRA mRNA was predominately found in kidney and brain. In vitro interaction studies revealed that the first KIBRA WW domain binds specifically to PPxY motifs. Transient transfection of monkey kidney cells with constructs encoding Myc-tagged KIBRA displayed a cytoplasmic localization and a perinuclear enrichment of the protein. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：862 / 867

页数：6

共 22 条

[1] MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains [J].