Christian Näke

University of Freiburg

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Klaus Harter

University of Tübingen

Christina Chaban

University of Tübingen

Katia Schütze

University of Tübingen

Jan Dittgen

Bayer (Germany)

Ben F. Holt

University of Oklahoma

Hironori Kaminaka

Tottori University

Petra Epple

University of North Carolina at Chapel Hill

Jeffery L. Dangl

University of North Carolina at Chapel Hill

Eberhard Schäfer

University of Freiburg

Thomas Merkle

University of Konstanz

Cooperative Institutions

University of Freiburg

University of Tübingen

University of Cologne

Centro de Astrobiología

Consejo Superior de Investigaciones Científicas

University of Rostock

University of North Carolina at Chapel Hill

Instituto Nacional de Técnica Aeroespacial

Institute of Plant Molecular Biology

Friedrich Miescher Institute

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AtbZIP10, an interaction partner of LSD1, regulates programmed cell death involved in disease resistance

Hironori Kaminaka Christian Näke Petra Epple Jan Dittgen Katia Schütze

10.14841/jspp.2005.0.398.0

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The single AmphiTrk receptor highlights increased complexity of neurotrophin signalling in vertebrates and suggests an early role in developing sensory neuroepidermal cells

Development (2005)

Èlia Benito‐Gutiérrez Christian Näke Marta Llovera Joan X. Comella Jordi García‐Fernàndez

Neurotrophins (Nt) and their tyrosine kinase Trk receptors play an essential role in the development and maintenance of the complex vertebrate nervous system. Invertebrate genome sequencing projects have suggested that the Nt/Trk system is a vertebrate innovation. We describe the isolation and characterisation of the amphioxus Trk receptor, AmphiTrk. Its ancestral link to vertebrate Trk receptors is supported by phylogenetic analysis and domain characterisation. The genomic structure of AmphiTrk strongly suggests that a ProtoTrk gene emerged by means of exon-shuffling prior to the cephalochordate/vertebrate split. We also examined the physiological response of AmphiTrk to vertebrate neurotrophins,and found that despite 500 million years of divergence, AmphiTrk transduces signals mediated by NGF, BDNF, NT3 and NT4. Markedly, AmphiTrk is able to activate survival and differentiation pathways, but fails to activate the PLCγ pathway, which is involved in synaptic plasticity in higher vertebrates. AmphiTrk is expressed during amphioxus embryogenesis in sensory neural precursors in the epidermis, which possesses single migratory cells. We propose that the duplication and divergence of the Nt/Trk system, in tandem with recruitment of the PLCγ pathway, may have provided the genetic basis for a key aspect of vertebrate evolution: the complexity of the nervous system.

Signalling

Signalling pathways

10.1242/dev.01803

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Citations (68)

A multi-array competitive immunoassay for the detection of broad-range molecular size organic compounds relevant for astrobiology

Planetary and Space Science (2006)

Patricia Fernández‐Calvo Christian Näke Luis A. Rivas Miriam García‐Villadangos Javier Gómez‐Elvira

Dichloromethane

10.1016/j.pss.2006.02.007

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Citations (32)

Isolation and characterization of four novel parsley proteins that interact with the transcriptional regulators CPRF1 and CPRF2

Molecular Genetics and Genomics (2001)

Alexander Rügner Hanns Frohnmeyer Christian Näke Frank Wellmer Stefan Kircher

Transcription

Homology

10.1007/s004380100502

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Citations (30)

bZIP10-LSD1 antagonism modulates basal defense and cell death in Arabidopsis following infection

Carolina Digital Repository (University of North Carolina at Chapel Hill) (2006)

Hironori Kaminaka Christian Näke Petra Epple Jan Dittgen Katia Schütze

Basal (medicine)

10.17615/5jj7-4325

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Citations (24)

bZIP10-LSD1 antagonism modulates basal defense and cell death in Arabidopsis following infection

The EMBO Journal (2006)

Hironori Kaminaka Christian Näke Petra Epple Jan Dittgen Katia Schütze

Basal (medicine)

10.1038/sj.emboj.7601312

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Citations (251)

Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation

The Plant Journal (2004)

Michael Walter Christina Chaban Katia Schütze Oliver Batistič Katrin Weckermann

Dynamic networks of protein-protein interactions regulate numerous cellular processes and determine the ability to respond appropriately to environmental stimuli. However, the investigation of protein complex formation in living plant cells by methods such as fluorescence resonance energy transfer has remained experimentally difficult, time consuming and requires sophisticated technical equipment. Here, we report the implementation of a bimolecular fluorescence complementation (BiFC) technique for visualization of protein-protein interactions in plant cells. This approach relies on the formation of a fluorescent complex by two non-fluorescent fragments of the yellow fluorescent protein brought together by association of interacting proteins fused to these fragments (Hu et al., 2002). To enable BiFC analyses in plant cells, we generated different complementary sets of expression vectors, which enable protein interaction studies in transiently or stably transformed cells. These vectors were used to investigate and visualize homodimerization of the basic leucine zipper (bZIP) transcription factor bZIP63 and the zinc finger protein lesion simulating disease 1 (LSD1) from Arabidopsis as well as the dimer formation of the tobacco 14-3-3 protein T14-3c. The interaction analyses of these model proteins established the feasibility of BiFC analyses for efficient visualization of structurally distinct proteins in different cellular compartments. Our investigations revealed a remarkable signal fluorescence intensity of interacting protein complexes as well as a high reproducibility and technical simplicity of the method in different plant systems. Consequently, the BiFC approach should significantly facilitate the visualization of the subcellular sites of protein interactions under conditions that closely reflect the normal physiological environment.

Bimolecular fluorescence complementation

Plant cell

Protein-fragment complementation assay

10.1111/j.1365-313x.2004.02219.x

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Citations (1,641)

Detection of abscisic‐acid‐binding proteins in the microsomal protein fraction of Arabidopsis thaliana with abscisic‐acid−protein conjugates used as affinity probes

European Journal of Biochemistry (1998)

Jacques Pédron Mathias Brault Christian Näke Émile Miginiac

A family of affinity probes has been generated to detect and purify abscisic-acid (ABA)-binding proteins, by coupling ABA onto carrier proteins (ovalbumin or BSA) through the C1 carboxyl group or the C4' carbonyl group of ABA. ELISA detection showed that these ABA-protein conjugates bound efficiently to the solubilized microsomal protein fraction of Arabidopsis thaliana, but not to the soluble protein fraction. Heat or proteolytic treatments inhibited the binding of the conjugates, indicating the protein nature of these binding sites. After membrane purification of the microsomes, the binding sites were found to be preferentially located in the plasma membrane fraction. The binding of the conjugates was independent of the nature of the carrier protein or the ABA-carrier protein linker, but was competitively inhibited with an anti-ABA mAb. Furthermore, the competitive inhibition of the binding of the conjugates with ABA, but not with the inactive ABA methyl ester analog, demonstrated the specificity of the binding and the saturability of the binding sites. The binding of the conjugates was strictly correlated to the ABA/carrier protein molar coupling ratio, confirming that the affinity of the conjugates to the ABA-binding proteins was enhanced by the increase in the probability of binding events. The experimental approach permits a new insight into the nature of membrane-associated ABA-binding proteins.

Linker

10.1046/j.1432-1327.1998.2520385.x

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Citations (43)