Constitutive association of the proapoptotic protein Bim with Bcl-2-related proteins on mitochondria in T cells | Zendy

Yanan Zhu | Zendy; Bradley Jay Swanson | Zendy; Michael Wang | Zendy; David A. Hildeman | Zendy; Brian C. Schaefer | Zendy; Xinqi Liu | Zendy; Hiroyuki Suzuki | Zendy; Katsuyoshi Mihara | Zendy; John W. Kappler | Zendy; Philippa Marrack | Zendy

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Constitutive association of the proapoptotic protein Bim with Bcl-2-related proteins on mitochondria in T cells

Author(s) -

Yanan Zhu,

Bradley Jay Swanson,

Michael Wang,

David A. Hildeman,

Brian C. Schaefer,

Xinqi Liu,

Hiroyuki Suzuki,

Katsuyoshi Mihara,

John W. Kappler,

Philippa Marrack

Publication year - 2004

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.0402293101

Subject(s) - microtubule , mitochondrion , microbiology and biotechnology , apoptosis , bcl 2 family , function (biology) , in vitro , biology , dynein , chemistry , programmed cell death , genetics

Apoptosis in activated T cells in vivo requires the proapoptotic Bcl-2 family member Bim. We show here that, despite its ability to bind LC8, a component of the microtubule dynein motor complex, most of the Bim in both healthy and apoptotic T cells is associated with mitochondria, not microtubules. In healthy resting T cells Bim is bound to the antiapoptotic proteins Bcl-2 and Bcl-x(L). In activated T cells, levels of Bcl-2 fall, and Bim is associated more with Bcl-x(L) and less with Bcl-2. Our results indicate that, in T cells, Bim function is regulated by interaction with Bcl-2 family members on mitochondria rather than by sequestration to the microtubules.

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