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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Identification of FBXO25-interacting proteins using an integrated proteomics approach

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Autor(es):
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Teixeira, Felipe R. ; Yokoo, Sami ; Gartner, Carlos A. [1] ; Manfiolli, Adriana O. ; Baqui, Munira M. A. ; Assmann, Eliana M. [2] ; Maragno, Ana Leticia G. C. ; Yu, Huijun [3] ; de Lanerolle, Primal [3] ; Kobarg, Joerg [2] ; Gygi, Steven P. [1] ; Gomes, Marcelo Damario [4]
Número total de Autores: 12
Afiliação do(s) autor(es):
[1] Harvard Univ, Harvard Med Sch, Dept Cell Biol, Boston, MA 02115 - USA
[2] Ctr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias, Campinas, SP - Brazil
[3] Univ Illinois, Dept Physiol & Biophys, Chicago, IL 60680 - USA
[4] USP, Fac Med Ribeirao Preto, Dept Bioquim & Imunol, BR-14049900 Ribeirao Preto, SP - Brazil
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Fonte: PROTEOMICS; v. 10, n. 15, p. 2746-2757, JUL 2010.
Citações Web of Science: 7
Resumo

FBXO25 is one of the 68 human F-box proteins that serve as specificity factors for a family of ubiquitin ligases composed of s-phase-kinase associated protein 1, really interesting new gene-box 1, Cullin 1, and F-box protein (SCF1) that are involved in targeting proteins for destruction across the ubiquitin proteasome system. We recently reported that the FBXO25 protein accumulates in novel subnuclear structures named FBXO25-associated nuclear domains (FAND). Combining two-step affinity purification followed by MS with a classical two-hybrid screen, we identified 132 novel potential FBXO25 interacting partners. One of the identified proteins, beta-actin, physically interacts through its N-terminus with FBXO25 and is enriched in the FBXO25 nuclear compartments. Inhibitors of actin polymerization promote a significant disruption of FAND, indicating that they are compartments influenced by the organizational state of actin in the nucleus. Furthermore, FBXO25 antibodies interfered with RNA polymerase II transcription in vitro. Our results open new perspectives for the understanding of this novel compartment and its nuclear functions. (AU)

Processo FAPESP: 06/58140-9 - Identificacao de substratos e cofatores da ubiquitina ligase scffbxo25.
Beneficiário:Marcelo Damário Gomes
Modalidade de apoio: Auxílio à Pesquisa - Regular