Interaction of Vault Particles with Estrogen Receptor in the MCF-7 Breast Cancer Cell

doi:10.1083/jcb.141.6.1301

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J. Cell Biol., Volume 141, Number 6, June 15, 1998 1301-1310

Interaction of Vault Particles with Estrogen Receptor in the MCF-7 Breast Cancer Cell

Ciro Abbondanza, Valentina Rossi, Annarita Roscigno, Luigi Gallo, Angela Belsito, Giulio Piluso, Nicola Medici, Vincenzo Nigro, Anna Maria Molinari, Bruno Moncharmont, and Giovanni A. Puca

Istituto di Patologia generale ed Oncologia, Facoltà di Medicina e Chirurgia, Seconda Università degli studi di Napoli, I-80138 Naples, Italy

A 104-kD protein was coimmunoprecipitated with the estrogen receptor from the flowtrough of a phosphocellulose chromatographyof MCF-7 cell nuclear extract. mAbs to this protein identifiedseveral cDNA clones coding for the human 104-kD major vault protein.Vaults are large ribonucleoprotein particles of unknown functionpresent in all eukaryotic cells. They have a complex morphology,including several small molecules of RNA, but a single proteinspecies, the major vault protein, accounts for >70% of their mass.Their shape is reminiscent of the nucleopore central plug, butno proteins of known function have been described to interactwith them. Western blot analysis of vaults purified on sucrosegradient showed the presence of estrogen receptor co-migratingwith the vault peak. The AER317 antibody to estrogen receptorcoimmunoprecipitated the major vault protein and the vault RNAalso in the 20,000 g supernatant fraction. Reconstitution experimentsof estrogen receptor fragments with the major vault protein mappedthe site of the interaction between amino acids 241 and 280 ofhuman estrogen receptor, where the nuclear localization signalsequences are located. Estradiol treatment of cells increasedthe amount of major vault protein present in the nuclear extractand coimmunoprecipitated with estrogen receptor, whereas the anti-estrogenICI182,780 had no effect. The hormone-dependent interaction ofvaults with estrogen receptor was reproducible in vitro and wasprevented by sodium molybdate. Antibodies to progesterone andglucocorticoid receptors were able to coimmunoprecipitate themajor vault protein. The association of nuclear receptors withvaults could be related to their intracellular traffic.

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