Adler, Jacob J.;
Johnson, Derrick E.;
Heller, Brigitte L.;
Bringman, Lauren R.;
Ranahan, William P.;
Conwell, Michael D.;
Sun, Yang;
Hudmon, Andy;
Wells, Clark D.
Serum deprivation inhibits the transcriptional co-activator YAP and cell growth via phosphorylation of the 130-kDa isoform of Angiomotin by the LATS1/2 protein kinases
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Media type:
E-Article
Title:
Serum deprivation inhibits the transcriptional co-activator YAP and cell growth via phosphorylation of the 130-kDa isoform of Angiomotin by the LATS1/2 protein kinases
Contributor:
Adler, Jacob J.;
Johnson, Derrick E.;
Heller, Brigitte L.;
Bringman, Lauren R.;
Ranahan, William P.;
Conwell, Michael D.;
Sun, Yang;
Hudmon, Andy;
Wells, Clark D.
Published:
Proceedings of the National Academy of Sciences, 2013
Published in:
Proceedings of the National Academy of Sciences, 110 (2013) 43, Seite 17368-17373
Language:
English
DOI:
10.1073/pnas.1308236110
ISSN:
0027-8424;
1091-6490
Origination:
Footnote:
Description:
Significance This study defines a unique mechanism controlling the activation of Hippo signaling and consequent inhibition of cell growth. Specifically, serum starvation is found to induce the large tumor suppressor (LATS)1/2 kinases to phosphorylate and thus stabilize the 130 kDa isoform of the membrane-associated polarity protein angiomotin (Amot130). As a consequence, Amot130 recruits the E3 protein-ubiquitin ligase atrophin-1 interacting protein 4. This multiprotein complex then signals the degradation of Yes-associated protein (YAP) and the inhibition of cell growth. These findings significantly modify our current view that YAP phosphorylation by LATS1/2 is sufficient for its inhibition in mammals and thus for growth arrest.