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Exp Cell Res ; 278(2): 133-45, 2002 Aug 15.
Artigo em Inglês | MEDLINE | ID: mdl-12169269

RESUMO

Using an antiserum directed against marginal band associated proteins of chicken erythrocytes we isolated clones encoding the chicken homolog of 14.7K-interacting protein 2 (FIP-2), a protein potentially involved in tumor necrosis factor-alpha/nuclear factor-kappaB signaling, from a chicken erythroblast cDNA library. We found that chicken FIP-2 was expressed in a variety of tissues and cell types, but unlike its human counterpart, alternative splicing does not appear to take place. Analysis of intracellular localization revealed that FIP-2 was concentrated at the Golgi apparatus in most cells. Perturbation of the Golgi structure without loss of Golgi function (by treatment with nocodazole) resulted in a retention of FIP-2 at the dispersed Golgi fragments. In contrast, disruption of both Golgi structure and function (by brefeldin A) led to a loss of FIP-2 from Golgi membranes. Remarkably, during erythroblast differentiation FIP-2 was found to translocate from the Golgi to the marginal band. Our results support the hypothesis of a function of the Golgi apparatus in signal transduction. Moreover, our results raise the possibility that the marginal band of chicken erythrocytes, in addition to its role in morphogenesis, has a function in signal transduction and that FIP-2 is in some way involved in its formation.


Assuntos
Proteínas de Transporte/metabolismo , Eritroblastos/citologia , Eritroblastos/metabolismo , Complexo de Golgi/metabolismo , Microtúbulos/metabolismo , Sequência de Aminoácidos , Animais , Proteínas de Transporte/fisiologia , Diferenciação Celular , Galinhas , Eritroblastos/química , Complexo de Golgi/fisiologia , Quinase I-kappa B , Microscopia de Fluorescência , Microtúbulos/fisiologia , Dados de Sequência Molecular , Proteínas Serina-Treonina Quinases , Transporte Proteico , Alinhamento de Sequência , Transdução de Sinais
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