FAK and PYK2 interact with SAP90/PSD-95-Associated Protein-3

被引：19

作者：

Bongiorno-Borbone, L

Kadaré, G

Benfenati, F

Girault, JA ^{[1
]}

机构：

[1] INSERM U536, F-75005 Paris, France

[2] Univ Paris 06, F-75005 Paris, France

[3] Inst Fer Moulin, F-75005 Paris, France

[4] Univ Roma Tor Vergata, Dept Neurosci, I-00133 Rome, Italy

[5] Fdn S Luica, IRCCS, CERC, Rome, Italy

[6] Univ Genoa, Dept Expt Med, Sect Human Physiol, I-16132 Genoa, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 337卷 / 02期

关键词：

non-receptor tyrosine kinase; synapses; protein-protein interaction; post-synaptic densities; neurons; Src; GKAP;

D O I：

10.1016/j.bbrc.2005.09.099

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：

Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (PYK2) are two related non-receptor tyrosine kinases highly expressed in brain. Although they are both involved in synaptic plasticity, little is known about their specific neuronal partners. Using a yeast two-hybrid screen and GST pull-down assays we show that SAPAP3 (SAP90/PSD-95-Associated Protein-3) interacts with FAK (residues 676-840) and PYK2. The three proteins partly co-distribute in the same sucrose gradient fractions as the post-synaptic density protein PSD-95 and Src. Our results suggest that SAPAP3 is an anchoring protein for FAK and PYK2 in post-synaptic densities and may contribute to the synaptic function of these tyrosine kinases. (c) 2005 Elsevier Inc. All rights reserved.

引用

收藏

页码：641 / 646

页数：6

相关论文

共 32 条

[1] IDENTIFICATION AND CHARACTERIZATION OF A NOVEL RELATED ADHESION FOCAL TYROSINE KINASE (RAFTK) FROM MEGAKARYOCYTES AND BRAIN [J].

AVRAHAM, S ;

LONDON, R ;

FU, YG ;

OTA, S ;

HIREGOWDARA, D ;

LI, JZ ;

JIANG, SX ;

PASZTOR, LN ;

WHITE, RA ;

GROOPMAN, JE ;

AVRAHAM, H .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (46) :27742-27751

[2] Increased phosphorylation and redistribution of NMDA receptors between synaptic lipid rafts and post-synaptic densities following transient global ischemia in the rat brain [J].

Besshoh, S ;

Bawa, D ;

Teves, L ;

Wallace, MC ;

Gurd, JW .

JOURNAL OF NEUROCHEMISTRY, 2005, 93 (01) :186-194

[3] The translocation of focal adhesion kinase in brain synaptosomes is regulated by phosphorylation and actin assembly [J].

Bongiorno-Borbone, L ;

Onofri, F ;

Giovedì, S ;

Ferrari, R ;

Girault, JA ;

Benfenati, F .

JOURNAL OF NEUROCHEMISTRY, 2002, 81 (06) :1212-1222

[4] Alternatively spliced focal adhesion kinase in rat brain with increased autophosphorylation activity [J].

Burgaya, F ;

Toutant, M ;

Studler, JM ;

Costa, A ;

LeBert, M ;

Gelman, M ;

Girault, JA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (45) :28720-28725

[5] FAK and PYK2/CAKβ in the nervous system:: a link between neuronal activity, plasticity and survival? [J].

Girault, JA ;

Costa, A ;

Derkinderen, P ;

Studler, JM ;

Toutant, M .

TRENDS IN NEUROSCIENCES, 1999, 22 (06) :257-263

[6] FOCAL ADHESION PROTEIN-TYROSINE KINASE PHOSPHORYLATED IN RESPONSE TO CELL ATTACHMENT TO FIBRONECTIN [J].

HANKS, SK ;

CALALB, MB ;

HARPER, MC ;

PATEL, SK .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (18) :8487-8491

[7] Association of synapse-associated protein 90/postsynaptic density-95-associated protein (SAPAP) with neurofilaments [J].

Hirao, K ;

Hata, Y ;

Deguchi, M ;

Yao, I ;

Ogura, M ;

Rokukawa, C ;

Kawabe, H ;

Mizoguchi, A ;

Takai, Y .

GENES TO CELLS, 2000, 5 (03) :203-210

[8] CAKβ/Pyk2 kinase is a signaling link for induction of long-term potentiation in CA1 hippocampus [J].

Huang, YQ ;

Lu, WY ;

Ali, DW ;

Pelkey, KA ;

Pitcher, GM ;

Lu, YM ;

Aoto, H ;

Roder, JC ;

Sasaki, T ;

Salter, MW ;

MacDonald, JF .

NEURON, 2001, 29 (02) :485-496

[9] PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation [J].

Kadaré, G ;

Toutant, M ;

Formstecher, E ;

Corvol, JC ;

Carnaud, M ;

Boutterin, MC ;

Girault, JA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (48) :47434-47440

[10] GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules [J].

Kim, E ;

Naisbitt, S ;

Hsueh, YP ;

Rao, A ;

Rothschild, A ;

Craig, AM ;

Sheng, M .

JOURNAL OF CELL BIOLOGY, 1997, 136 (03) :669-678

← 1 2 3 4 →