Home Ricerca Sedi Chi siamo Organigramma Personale Contatti Didattica Login Documenti EN
Progetti in evidenza
INCIPIT
(Link esterno)

ISTAPCA
(1174 visite)

Fondo Europeo Pesca
(587 visite)

Euro-BioImaging
(Link esterno)

Fondazione Veronesi
(Link esterno)

LightDyNAmics
(1045 visite)

 INMiND
(1157 visite)

Instruct-IT
(Link esterno)

 PRIN
(1291 visite)

 eHealthNet
(1059 visite)

Ponrec
(1002 visite)

MFAG Grant
(1095 visite)

MERIT
(Link esterno)


Collegamenti



A biophysical characterization of the folded domains of KCTD12: insights into interaction with the GABA(B2) receptor (109 visite)

Correale S, Esposito C, Pirone L, Vitagliano L, Di Gaetano S, Pedone E

Journal Of Molecular Recognition (ISSN: 0952-3499, 0952-2349), 2013 Oct; 26(10): 488-495.

Tipo di articolo: Journal Article,

Impact factor: 2.337

Impact factor a 5 anni: 2.483


Parole chiave: Cd Spectroscopy, Gabab2 Receptor, Interaction Studies, Kctd12, Oligomerization State, Peptide Design, 4 Aminobutyric Acid A Receptor, Gabrr2 Protein, Human, Kctd12 Protein, Recombinant Protein, Amino Acid Sequence, Article, Binding Site, Chemistry, Escherichia Coli, Genetics, Molecular Cloning, Molecular Genetics, Protein Binding, Protein Domain, Protein Folding, Protein Multimerization, Protein Secondary Structure, Molecular Sequence Data, Protein Interaction Domains And Motifs, Protein Structure,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84883301541&partnerID=40&md5=f159f67fb1883c95f33be9ace58b0e75

Recent investigations have shown that members of the KCTD family play important roles in fundamental biological processes. Despite their roles, very limited information is available on their structures and molecular organization. By combining different experimental and theoretical techniques, we have here characterized the two folded domains of KCTD12, an integral component and modulator of the GABA (B2) receptor. Secondary prediction methods and CD spectroscopy have shown that the N-terminal domain KCTD12 (BTB) assumes an / structure, whereas the C-terminal domain KCTD12 (H1) is predominantly characterized by a -structure. Binding assays indicate that the two domains independently expressed show a good affinity for each other. This suggests that the overall protein is likely endowed with a rather compact structure with two interacting structured domains joint by a long disordered region. Notably, both KCTD12 (BTB) and KCTD12 (H1) are tetrameric when individually expressed. This finding could modify the traditional view that ascribes only to POZ/BTB domain a specific oligomerization role. The first quantification of the affinity of KCTD12 (POZ/BTB) for the C-terminal region of GABA (B2) shows that it falls in the low micromolar range. Interestingly, we also demonstrate that a GABA (B2) -related peptide is able to bind KCTD12 (BTB) with a very high affinity. This peptide may represent a useful tool for modulating KCTD12/GABA (B2) interaction in vitro and may also constitute the starting point for the development of peptidomimetic compounds with a potential for therapeutic applications. Copyright (c) 2013 John Wiley & Sons, Ltd
*** IBB - CNR ***

Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, 80134 Napoli, Italy

Kedrion S. p. A, 80029 S. Antimo, Napoli, Italy

DFM Scarl, via Mezzocannone 16, 80134 Napoli, Italy

Institute of Crystallography, CNR, 70126 Bari, Italy

Kedrion S.p.A, 80029 S. Antimo, Napoli, Italy
Apic, G., Gough, J., Teichmann, S. A., Domain combinations in archaeal, eubacterial and eukaryotic proteomes (2001) J. Mol. Biol., 310, pp. 311-32

Azizieh, R., Orduz, D., Van Bogaert, P., Bouschet, T., Rodriguez, W., Schiffmann, S. N., Pirson, I., Abramowicz, M. J., Progressive myoclonic epilepsy-associated gene KCTD7 is a regulator of potassium conductance in neurons (2011) Mol. Neurobiol., 44, pp. 111-121

Bartoi, T., Rigbolt, K. T., Du, D., Kohr, G., Blagoev, B., Kornau, H. C., GABAB receptor constituents revealed by tandem affinity purification from transgenic mice (2010) J. Biol. Chem., 285, pp. 20625-20633

Bayon, Y., Trinidad, A. G., De La Puerta, M. L., Del Carmen, R. M., Bogetz, J., Rojas, A., De Pereda, J. M., Alonso, A., KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases (2008) FEBS J., 275, pp. 3900-3910

Berthold, J., Schenkova, K., Ramos, S., Miura, Y., Furukawa, M., Aspenstrom, P., Rivero, F., (2008) Exp. Cell Res., 314, pp. 3453-3465. , Characterization of RhoBTB-dependent Cul3 ubiquitin ligase complexes - evidence for an autoregulatory mechanism

Canettieri, G., Di Marcotullio, L., Greco, A., Coni, S., Antonucci, L., Infante, P., Pietrosanti, L., Gulino, A., Histone deacetylase and Cullin3-REN (KCTD11) ubiquitin ligase interplay regulates Hedgehog signalling through Gli acetylation (2010) Nat. Cell Biol., 12, pp. 132-142

Chen, Y., Yang, Z., Meng, M., Zhao, Y., Dong, N., Yan, H., Liu, L., Shao, F., Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement (2009) Mol. Cell, 35, pp. 841-855

Correale, S., Pirone, L., Di Marcotullio, L., De Smaele, E., Greco, A., Mazza, D., Moretti, M., Pedone, E. M., Molecular organization of the cullin E3 ligase adaptor KCTD11 (2011) Biochimie, 93, pp. 715-724

De Smaele, E., Di Marcotullio, L., Moretti, M., Pelloni, M., Occhione, M. A., Infante, P., Cucchi, D., Gulino, A., Identification and characterization of KCASH2 and KCASH3, 2 novel Cullin3 adaptors suppressing histone deacetylase and Hedgehog activity in medulloblastoma (2011) Neoplasia, 13, pp. 374-385

Dementieva, I. S., Tereshko, V., McCrossan, Z. A., Solomaha, E., Araki, D., Xu, C., Grigorieff, N., Goldstein, S. A., Pentameric assembly of potassium channel tetramerization domain-containing protein 5 (2009) J. Mol. Biol., 387, pp. 175-191

Gassmann, M., Bettler, B., Regulation of neuronal GABA (B) receptor functions by subunit composition (2012) Nat. Rev. Neurosci., 13, pp. 380-394

Golzio, C., Willer, J., Talkowski, M. E., Oh, E. C., Taniguchi, Y., Jacquemont, S., Reymond, A., Katsanis, N., KCTD13 is a major driver of mirrored neuroanatomical phenotypes of the 16p11. 2 copy number variant (2012) Nature, 485, pp. 363-367

Hayasaki, H., Sohma, Y., Kanbara, K., Otsuki, Y., Heterogenous GABA (B) receptor-mediated pathways are involved in the local GABAergic system of the rat trigeminal ganglion: Possible involvement of KCTD proteins (2012) Neuroscience, 218, pp. 344-358

Hu, X., Yan, F., Wang, F., Yang, Z., Xiao, L., Li, L., Xiang, S., Zhang, J., TNFAIP1 interacts with KCTD10 to promote the degradation of KCTD10 proteins and inhibit the transcriptional activities of NF-kappaB and AP-1 (2012) Mol. Biol. Rep., 39, pp. 9911-9919

Huang, T., Xu, J., Xiang, J., Lu, Y., Chen, R., Huang, L., Xiao, G., Sun, G., PrPC interacts with potassium channel tetramerization domain containing 1 (KCTD1) protein through the PrP (51-136) region containing octapeptide repeats (2012) Biochem. Biophys. Res. Commun., 417, pp. 182-186

Kikuta, K., Gotoh, M., Kanda, T., Tochigi, N., Shimoda, T., Hasegawa, T., Katai, H., Kondo, T., Pfetin as a prognostic biomarker in gastrointestinal stromal tumor: Novel monoclonal antibody and external validation study in multiple clinical facilities (2010) Jpn. J. Clin. Oncol., 40, pp. 60-72

Limauro, D., Saviano, M., Galdi, I., Rossi, M., Bartolucci, S., Pedone, E., Sulfolobus solfataricus protein disulphide oxidoreductase: Insight into the roles of its redox sites (2009) Protein Eng des Sel, 22, pp. 19-26

Longhi, S., Receveur-Brechot, V., Karlin, D., Johansson, K., Darbon, H., Bhella, D., Yeo, R., Canard, B., The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein (2003) J. Biol. Chem., 278, pp. 18638-18648

Pirone, L., Correale, S., De Paola, I., Zaccaro, L., De Simone, G., Vitagliano, L., Pedone, E., Di Gaetano, S., Design, synthesis and characterization of a peptide able to bind proteins of the KCTD family: Implications for KCTD-cullin 3 recognition (2011) J. Pept. Sci., 17, pp. 373-376

Schwenk, J., Metz, M., Zolles, G., Turecek, R., Fritzius, T., Bildl, W., Tarusawa, E., Bettler, B., Native GABA (B) receptors are heteromultimers with a family of auxiliary subunits (2010) Nature, 465, pp. 231-235

Seddik, R., Jungblut, S. P., Silander, O. K., Rajalu, M., Fritzius, T., Besseyrias, V., Jacquier, V., Bettler, B., Opposite Effects of KCTD Subunit Domains on GABAB Receptor-mediated Desensitization (2012) J. Biol. Chem., 287, pp. 39869-39877

Stogios, P. J., Downs, G. S., Jauhal, J. J., Nandra, S. K., Prive, G. G., Sequence and structural analysis of BTB domain proteins (2005) Genome Biol., 6, pp. R82

Suehara, Y., Kondo, T., Seki, K., Shibata, T., Fujii, K., Gotoh, M., Hasegawa, T., Hirohashi, S., Pfetin as a prognostic biomarker of gastrointestinal stromal tumors revealed by proteomics (2008) Clin. Cancer Res., 14, pp. 1707-1717

Ward, J. J., McGuffin, L. J., Bryson, K., Buxton, B. F., Jones, D. T., The DISOPRED server for the prediction of protein disorder (2004) Bioinformatics, 20 (13), pp. 2138-2139

Williams, M. J., Almen, M. S., Fredriksson, R., Schioth, H. B., What model organisms and interactomics can reveal about the genetics of human obesity (2012) Cell. Mol. Life Sci., 69, pp. 3819-3834

Dementieva, I.S., Tereshko, V., McCrossan, Z.A., Solomaha, E., Araki, D., Xu, C., Grigorieff, N., Goldstein, S.A., Pentameric assembly of potassium channel tetramerization domain-containing protein 5 (2009) J. Mol. Biol., 387, pp. 175-191

Stogios, P.J., Downs, G.S., Jauhal, J.J., Nandra, S.K., Prive, G.G., Sequence and structural analysis of BTB domain proteins (2005) Genome Biol., 6, pp. R82

Ward, J.J., McGuffin, L.J., Bryson, K., Buxton, B.F., Jones, D.T., The DISOPRED server for the prediction of protein disorder (2004) Bioinformatics, 20 (13), pp. 2138-2139

Williams, M.J., Almen, M.S., Fredriksson, R., Schioth, H.B., What model organisms and interactomics can reveal about the genetics of human obesity (2012) Cell. Mol. Life Sci., 69, pp. 3819-3834

Nessun risultato.
Nessun risultato.

Contiene: [X]      Estesa         Autori: [X]      Tipo di lavoro: [X]
Data iniziale: Data finale: [X]      Sede: Affiliazione IBB     
    
[Pulisci modulo]
Mercurio FA, Di Natale C, Pirone L, Scognamiglio PL, Marasco D, Pedone EM, Saviano M, Leone M
* Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam (125 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2015; 16(11): 1629-1636.
Dettagli    Esporta in BibTeX    Esporta in EndNote

Stelitano V, Brandt A, Fernicola S, Franceschini S, Giardina G, Pica A, Rinaldo S, Sica F, Cutruzzola F
* Probing the activity of diguanylate cyclases and c-di-GMP phosphodiesterases in real-time by CD spectroscopy (128 visite)
Nucleic Acids Res (ISSN: 0305-1048, 0305-5104, 1362-4962), 2013 Apr; 41(7): e79-e79.
Dettagli    Esporta in BibTeX    Esporta in EndNote

Roviello GN, Crescenzo C, Capasso D, Di Gaetano S, Franco S, Bucci EM, Pedone C
* Synthesis of a novel Fmoc-protected nucleoaminoacid for the solid phase assembly of 4-piperidyl glycine/L-arginine-containing nucleopeptides and preliminary RNA interaction studies (121 visite)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2010 Sep; 39(3): 795-800.
Dettagli    Esporta in BibTeX    Esporta in EndNote



3 Records (2 escludendo Abstract e Conferenze).
Impact factor totale: 11.144 (6.956 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 13.604 (6.441 escludendo Abstract e Conferenze).







    Esporta in BibTeX    Esporta in EndNote

Ultima modifica di Marco Comerci in data Thursday 19 March 2015, 12:41:30
109 visite. Ultima visita in data Saturday 27 October 2018, 14:14:03

Webmaster and developer: Marco Comerci
Per problemi e suggerimenti: adminibb.cnr.it
Ultimo aggiornamento: Monday 12 November 2018, 16:59:37