KIBRA is a novel substrate for protein kinase Cξ

被引：88

作者：

Büther, K ^{[1
]}

Plaas, C ^{[1
]}

Barnekow, A ^{[1
]}

Kremerskothen, J ^{[1
]}

机构：

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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 317卷 / 03期

关键词：

KIBRA; WW domain; PKC; synaptic plasticity; phosphorylation;

D O I：

10.1016/j.bbrc.2004.03.107

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：

WW domain-containing proteins are found in all eukaryotic cells and they are involved in the regulation of a wide variety of cellular functions. We recently identified the neuronal protein KIBRA as novel member of this family of signal transducers. In this report, we describe the identification of protein kinase C (PKC) zeta as a KIBRA-interacting protein. PKCzeta is known to play an important role in synaptic plasticity and memory formation but its specific targets are not well known. Our Studies presented here revealed that KIBRA is a novel substrate for PKCzeta and suggest that PKCzeta phosphorylation may regulate the cellular function of KIBRA. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：703 / 707

页数：5

共 18 条

[1] Memory enhancement and formation by atypical PKM activity in Drosophila melanogaster
Drier, EA
Tello, MK
Cowan, M
Wu, P
Blace, N
Sacktor, TC
Yin, JCP
[J]. NATURE NEUROSCIENCE, 2002, 5 (04) : 316 - 324
[2] Towards prediction of cognate complexes between the WW domain and proline-rich ligands
Einbond, A
Sudol, M
[J]. FEBS LETTERS, 1996, 384 (01): : 1 - 8
[3] Dimerization of the Polycomb-group protein Mel-18 is regulated by PKC phosphorylation
Fujisaki, S
Ninomiya, Y
Ishihara, H
Miyazaki, M
Kanno, R
Asahara, T
Kanno, M
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 300 (01) : 135 - 140
[4] Prominent dendritic localization in forebrain neurons of a novel mRNA and its product, dendrin
Herb, A
Wisden, W
Catania, MV
Marechal, D
Dresse, A
Seeburg, PH
[J]. MOLECULAR AND CELLULAR NEUROSCIENCE, 1997, 8 (05) : 367 - 374
[5] Protein kinase Mζ synthesis from a brain mRNA encoding an independent protein kinase Cζ catalytic domain -: Implications for the molecular mechanism of memory
Hernandez, AI
Blace, N
Crary, JF
Serrano, PA
Leitges, M
Libien, JM
Weinstein, G
Tcherapanov, A
Sacktor, TC
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (41) : 40305 - 40316
[6] Protein kinase Cζ (PKCζ):: Activation mechanisms and cellular functions
Hirai, T
Chida, K
[J]. JOURNAL OF BIOCHEMISTRY, 2003, 133 (01) : 1 - 7
[7] The WW domain: Linking cell signalling to the membrane cytoskeleton
Ilsley, JL
Sudol, M
Winder, SJ
[J]. CELLULAR SIGNALLING, 2002, 14 (03) : 183 - 189
[8] Identification of human autoantigen La/SS-B as BC1/BC200 RNA-binding protein
Kremerskothen, J
Nettermann, M
Op De Bekke, A
Bachmann, M
Brosius, J
[J]. DNA AND CELL BIOLOGY, 1998, 17 (09) : 751 - 759
[9] Characterization of KIBRA, a novel WW domain-containing protein
Kremerskothen, J
Plaas, C
Büther, K
Finger, I
Veltel, S
Matanis, T
Liedtke, T
Barnekow, A
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2003, 300 (04) : 862 - 867
[10] The atypical protein kinase Cs - Functional specificity mediated by specific protein adapters
Moscat, J
Diaz-Meco, MT
[J]. EMBO REPORTS, 2000, 1 (05) : 399 - 403

← 1 2 →