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New York, NY, United States

Rhône Group is a global private equity firm, specializing in mergers and acquisitions, leveraged buyouts, recapitalizations, and partnerships with particular focus on European and trans-Atlantic investments. Rhône also offers financial advisory services, strategic alliances, joint partnerships, and business valuation services. Rhone Group was listed in 2013 to 2014 by Preqin as the 'Most Consistent Performing Private Equity Fund Manager' based on both its multiple and IRR of all 3 funds in the top quartile ranking.Rhône is headquartered at Rockefeller Plaza in New York City, with additional offices in London and Paris. Rhône was founded in 1995 by Robert Agostinelli and Steven Langman. The pair have been managing Rhône since inception. The company tends to invests in energy, materials, industrials, retailing, consumer staples, healthcare, and financial sectors. The company is a U.S. Securities and Exchange Commission Registered Investment Advisor. Investors include government and private sector pension and retirement funds, charitable foundations, university endowments, insurance companies, family savings and sovereign wealth funds. Focusing primarily on investments in European and trans-Atlantic companies. Wikipedia.

Rhône Group | Date: 2006-04-21

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Ichim G.,Rhone Group | Mola M.,Rhone Group | Finkbeiner M.G.,Rhone Group | Cros M.-P.,Rhone Group | And 2 more authors.
Oncogene | Year: 2014

Chromosomes are dynamic structures that must be reversibly condensed and unfolded to accommodate mitotic division and chromosome segregation. Histone modifications are involved in the striking chromatin reconfiguration taking place during mitosis. However, the mechanisms that regulate activity and function of histone-modifying factors as cells enter and exit mitosis are poorly understood. Here, we show that the anaphase-promoting complex or cyclosome (APC/C) is involved in the mitotic turnover of TRRAP (TRansformation/ tRanscription domain-Associated Protein), a common component of histone acetyltransferase (HAT) complexes, and that the pre-mitotic degradation of TRRAP is mediated by the APC/C ubiquitin ligase activators Cdc20 and Cdh1. Ectopic expression of both Cdh1 and Cdc20 reduced the levels of coexpressed TRRAP protein and induced its ubiquitination. TRRAP overexpression or stabilization induces multiple mitotic defects, including lagging chromosomes, chromosome bridges and multipolar spindles. In addition, lack of sister chromatid cohesion and impaired chromosome condensation were found after TRRAP overexpression or stabilization. By using a truncated form of TRRAP, we show that mitotic delay is associated with a global histone H4 hyperacetylation induced by TRRAP overexpression. These results demonstrate that the chromatin modifier TRRAP is targeted for destruction in a cell cycle-dependent fashion. They also suggest that degradation of TRRAP by the APC/C is necessary for a proper condensation of chromatin and proper chromosome segregation. Chromatin compaction mediated by histone modifiers may represent a fundamental arm for APC/C orchestration of the mitotic machinery. © 2014 Macmillan Publishers Limited.

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