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Published online 25 July 2005. doi:10.1083/jcb.200411106
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 3, 379-389
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Article

Identification of FIP200 interaction with the TSC1–TSC2 complex and its role in regulation of cell size control



Boyi Gan1, Zara K. Melkoumian1, Xiaoyang Wu1, Kun-Liang Guan2, and Jun-Lin Guan1

1 Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853
2 Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109

Correspondence to J.-L. Guan: jg19{at}cornell.edu

FIP200 (focal adhesion kinase [FAK] family interacting protein of 200 kD) is a newly identified protein that binds to the kinase domain of FAK and inhibits its kinase activity and associated cellular functions. Here, we identify an interaction between FIP200 and the TSC1–TSC2 complex through FIP200 binding to TSC1. We found that association of FIP200 with the TSC1–TSC2 complex correlated with its ability to increase cell size and up-regulate S6 kinase phosphorylation but was not involved in the regulation of cell cycle progression. Conversely, knockdown of endogenous FIP200 by RNA interference reduced S6 kinase phosphorylation and cell size, which required TSC1 but was independent of FAK. Furthermore, overexpression of FIP200 reduced TSC1–TSC2 complex formation, although knockdown of endogenous FIP200 by RNA interference did not affect TSC1–TSC2 complex formation. Lastly, we showed that FIP200 is important in nutrient stimulation-induced, but not energy- or serum-induced, S6 kinase activation. Together, these results suggest a cellular function of FIP200 in the regulation of cell size by interaction with the TSC1–TSC2 complex.

Abbreviations used in this paper: FSC-H, forward scatter; MEF, mouse embryonic fibroblast; RNAi, RNA interference; S6K, S6 kinase; TSC, tuberous sclerosis.


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