Regulation of localization and function of the transcriptional co-activator YAP by angiomotin.

Abstract:

:The Hippo-YAP pathway is a central regulator of cell contact inhibition, proliferation and death. There are conflicting reports regarding the role of Angiomotin (Amot) in regulating this pathway. While some studies suggest a YAP-inhibitory function other studies indicate Amot is required for YAP activity. Here, we describe an Amot-dependent complex comprised of Amot, YAP and Merlin. The phosphorylation of Amot at Serine 176 shifts localization of this complex to the plasma membrane, where it associates with the tight-junction proteins Pals1/PATJ and E-cadherin. Conversely, hypophosphorylated Amot shifts localization of the complex to the nucleus, where it facilitates the association of YAP and TEAD, induces transcriptional activation of YAP target genes and promotes YAP-dependent cell proliferation. We propose that phosphorylation of AmotS176 is a critical post-translational modification that suppresses YAP's ability to promote cell proliferation and tumorigenesis by altering the subcellular localization of an essential YAP co-factor.

journal_name

Elife

journal_title

eLife

authors

Moleirinho S,Hoxha S,Mandati V,Curtale G,Troutman S,Ehmer U,Kissil JL

doi

10.7554/eLife.23966

subject

Has Abstract

pub_date

2017-05-03 00:00:00

issn

2050-084X

journal_volume

6

pub_type

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