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Type: Artigo de periódico
Title: Human FEZ1 has characteristics of a natively unfolded protein and dimerizes in solution
Author: Lanza, DCF
Silva, JC
Assmann, EM
Quaresma, AJC
Bressan, GC
Torriani, IL
Kobarg, J
Abstract: The fasciculation and elongation protein Zeta 1 (FEZ1) is the mammalian orthologue of the Caenorhabditis elegans protein UNC-76, which is necessary for axon growth. Human FEZ1 interacts with Protein Kinase C (PKC) and several regulatory proteins involved in functions ranging from microtubule associated transport to transcriptional regulation. Theoretical prediction, circular dichroism, fluorescence spectroscopy, and limited proteolysis of recombinant FEZ1 suggest that it contains disordered regions, especially in its N-terminal region, and that it may belong to the group of natively unfolded proteins. Small angle X-ray scattering experiments indicated a mainly disordered conformation, proved that FEZ1 is a dimer of elongated shape and provided overall dimensional parameters for the protein. In vitro pull down experiments confirmed these results and demonstrated that dimerization involves the N-terminus. Ab-initio 3D low resolution models of the full-length conformation of the dimeric constructs 6xHis-FEZ1(1-392) and 6xHis-FEZ1(1-227) were obtained. Furthermore, we performed in vitro phosphorylation assays of FEZ1 with PKC. The phosphorylation occur-red mainly in its C-terminal region, and does not cause any significant conformational changes, but nonetheless inhibited its interaction with the FEZ1 interacting domain of the protein CLASP2 in vitro. The C terminus of FEZ1 has been reported to bind to several interacting proteins. This suggests that FEZ1 binding and transport function of interacting proteins may be subject to regulation by phosphorylation.
Subject: SAXS
protein-protein interactions
microtubular transport
circular dichroism
limited proteolysis
axonal transport
Country: EUA
Editor: Wiley-liss
Citation: Proteins-structure Function And Bioinformatics. Wiley-liss, v. 74, n. 1, n. 104, n. 121, 2009.
Rights: fechado
Identifier DOI: 10.1002/prot.22135
Date Issue: 2009
Appears in Collections:Unicamp - Artigos e Outros Documentos

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