{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T12:11:13Z","timestamp":1791202273730,"version":"4.2.0"},"reference-count":27,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,2,22]],"date-time":"2005-02-22T00:00:00Z","timestamp":1109030400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[2005,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Bim is an essential regulator of lymphoid system homeostasis and appears essential for B cell apoptosis induction. The mechanism by which Bim isoforms are held in an inactive form remains poorly documented in normal B cells. In the current study, we demonstrated that in normal tonsil B cells the three major Bim isoforms are strongly associated with the anti\u2010apoptotic Bcl\u20102 family members Mcl\u20101, Bcl\u20102 and Bcl\u2010x<jats:sub>L<\/jats:sub>. On the other hand, only a weak association of BimEL and L with the dynein LC8 chain has been found. In addition, there is no free Bim in normal B cells. Moreover, subcellular fractionation demonstrated that Bim and the anti\u2010apoptotic counterparts are localized preferentially in the mitochondria\u2010rich fraction. The fact that most Bim was found in this fraction supports the hypothesis that it is sequestered by anti\u2010apoptotic molecules in mitochondria where its pro\u2010apoptotic activity is controlled. Of interest, BimS is essentially complexed to Mcl\u20101 and the Mcl\u20101\/Bim complex is the most abundant among the three types of complexes. This supports the idea that this complex is critical for the control of B cell death. In conclusion, these results favor a model in which Bim release from anti\u2010apoptotic proteins is a critical event for initiation of apoptosis.<\/jats:p>","DOI":"10.1002\/eji.200425878","type":"journal-article","created":{"date-parts":[[2005,2,22]],"date-time":"2005-02-22T09:50:04Z","timestamp":1109065804000},"page":"971-976","source":"Crossref","is-referenced-by-count":52,"title":["Endogenous association of Bim BH3\u2010only protein with Mcl\u20101, Bcl\u2010x<sub>L<\/sub> and Bcl\u20102 on mitochondria in human B cells"],"prefix":"10.1002","volume":"35","author":[{"given":"Patricia","family":"Gomez\u2010Bougie","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R\u00e9gis","family":"Bataille","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martine","family":"Amiot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,2,22]]},"reference":[{"key":"e_1_2_7_1_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature02067"},{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.286.5445.1735"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/415922a"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20030411"},{"key":"e_1_2_7_5_2","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1210\/mend.12.9.0166","article-title":"BOD (Bcl\u20102\u2010related ovarian death gene) is an ovarian BH3 domain\u2010containing proapoptotic Bcl\u20102 protein capable of dimerization with diverse antiapoptotic Bcl\u20102 members.","volume":"12","author":"Hsu S. 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