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Angiomotin family proteins are novel activators of the LATS2 kinase tumor suppressor

Academic Article
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Overview

authors

  • Paramasivam, M.
  • Sarkeshik, A.
  • Yates III, John
  • Fernandes, M. J. G.
  • McCollum, D.

publication date

  • 2011

journal

  • Molecular Biology of the Cell  Journal

abstract

  • LATS2 kinase functions as part of the Hippo pathway to promote contact inhibition of growth and tumor suppression by phosphorylating and inhibiting the transcriptional coactivator YAP. LATS2 is activated by the MST2 kinase. How LATS2 is activated by MST2 in response to changes in cell density is unknown. Here we identify the angiomotin-family tight junction protein AMOTL2 as a novel activator of LATS2. Like AMOTL2, the other angiomotin-family proteins AMOT and AMOTL1 also activate LATS2 through a novel conserved domain that binds and activates LATS2. AMOTL2 binds MST2, LATS2, and YAP, suggesting that AMOTL2 might serve as a scaffold protein. We show that LATS2, AMOTL2, and YAP all localize to tight junctions, raising the possibility that clustering of Hippo pathway components at tight junctions might function to trigger LATS2 activation and growth inhibition in response to increased cell density.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Cell Line, Tumor
  • Contact Inhibition
  • HEK293 Cells
  • Humans
  • Intercellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Phosphoproteins
  • Phosphorylation
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • RNA, Small Interfering
  • Signal Transduction
  • Tight Junctions
  • Tumor Suppressor Proteins
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Identity

PubMed Central ID

  • PMC3183025

International Standard Serial Number (ISSN)

  • 1059-1524

Digital Object Identifier (DOI)

  • 10.1091/mbc.E11-04-0300

PubMed ID

  • 21832154
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Additional Document Info

start page

  • 3725

end page

  • 3733

volume

  • 22

issue

  • 19

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