Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.ccr.2011.02.017
Title: A Tight Junction-Associated Merlin-Angiomotin Complex Mediates Merlin's Regulation of Mitogenic Signaling and Tumor Suppressive Functions
Authors: Yi, C.
Troutman, S.
Fera, D.
Stemmer-Rachamimov, A.
Avila, J.
Christian, N.
Persson, N.
Shimono, A. 
Speicher, D.
Marmorstein, R.
Holmgren, L.
Kissil, J.
Issue Date: 12-Apr-2011
Citation: Yi, C., Troutman, S., Fera, D., Stemmer-Rachamimov, A., Avila, J., Christian, N., Persson, N., Shimono, A., Speicher, D., Marmorstein, R., Holmgren, L., Kissil, J. (2011-04-12). A Tight Junction-Associated Merlin-Angiomotin Complex Mediates Merlin's Regulation of Mitogenic Signaling and Tumor Suppressive Functions. Cancer Cell 19 (4) : 527-540. ScholarBank@NUS Repository. https://doi.org/10.1016/j.ccr.2011.02.017
Abstract: The Merlin/. NF2 tumor suppressor restrains cell growth and tumorigenesis by controlling contact-dependent inhibition of proliferation. We have identified a tight-junction-associated protein complex comprising Merlin, Angiomotin, Patj, and Pals1. We demonstrate that Angiomotin functions downstream of Merlin and upstream of Rich1, a small GTPase Activating Protein, as a positive regulator of Rac1. Merlin, through competitive binding to Angiomotin, releases Rich1 from the Angiomotin-inhibitory complex, allowing Rich1 to inactivate Rac1, ultimately leading to attenuation of Rac1 and Ras-MAPK pathways. Patient-derived Merlin mutants show diminished binding capacities to Angiomotin and are unable to dissociate Rich1 from Angiomotin or inhibit MAPK signaling. Depletion of Angiomotin in Nf2-/- Schwann cells attenuates the Ras-MAPK signaling pathway, impedes cellular proliferation in vitro and tumorigenesis in vivo. © 2011 Elsevier Inc.
Source Title: Cancer Cell
URI: http://scholarbank.nus.edu.sg/handle/10635/116205
ISSN: 15356108
DOI: 10.1016/j.ccr.2011.02.017
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