期刊
IMMUNITY
卷 26, 期 2, 页码 177-190出版社
CELL PRESS
DOI: 10.1016/j.immuni.2007.01.008
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资金
- NCI NIH HHS [R01 CA047752, R01-CA47752] Funding Source: Medline
- NIAID NIH HHS [F31-AI068624, R01-AI038474, R01 AI065474-03, F31 AI068624, R01 AI038474, R01-AI031126, R01 AI065474, R01-AI065474, R01 AI031126] Funding Source: Medline
T cell receptor (TCR)-mediated cytoskeletal reorganization is considered to be actin-related protein (Arp) 2/3 complex dependent. We therefore examined the requirement for Arp2/3- and formin-dependent F-actin nucleation during T cell activation. We demonstrated that without Arp2/3-mediated actin nucleation, stimulated T cells could not form an F-actin-rich lamellipod, but instead produced polarized filopodia-like structures. Moreover, the microtubule-organizing center (MTOC, or centrosome), which rapidly reorients to the immunological synapse through an unknown mechanism, polarized in the absence of Arp2/3. Conversely, the actin-nucleating formins, Diaphanous-1 (DIA1) and Formin-like-1 (FMNL1), did not affect TCR-stimulated F-actin-rich structures, but instead displayed unique patterns of centrosome colocalization and controlled TCR-mediated centrosome polarization. Depletion of FMNL1 or DIA1 in cytotoxic lymphocytes abrogated cell-mediated killing. Altogether, our results have identifed Arp2/3 complex-independent cytoskeletal reorganization events in T lymphocytes and indicate that formins are essential cytoskeletal regulators of centrosome polarity in T cells.
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