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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Angiomotin like 1

amotl1, angiomotin-like 1, Angiomotin-Like Protein 1, JEAP
The protein encoded by this gene is a peripheral membrane protein that is a component of tight junctions or TJs. TJs form an apical junctional structure and act to control paracellular permeability and maintain cell polarity. This protein is related to angiomotin, an angiostatin binding protein that regulates endothelial cell migration and capillary formation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: angiomotin, Amotl2, YAP, Actin, ACID
Papers on amotl1
MiR-124 represses vasculogenic mimicry and cell motility by targeting amotL1 in cervical cancer cells.
Tang et al., Tianjin, China. In Cancer Lett, 2015
Furthermore, we reveal that the effect of miR-124 on vasculogenic mimicry, migration and invasion results from its interaction with AmotL1.
Energy stress regulates hippo-YAP signaling involving AMPK-mediated regulation of angiomotin-like 1 protein.
Wu et al., United States. In Cell Rep, 2014
These effects require the central metabolic sensor AMP-activated protein kinase (AMPK) and the upstream Hippo pathway components Lats1/Lats2 and angiomotin-like 1 (AMOTL1).
Angiomotin'g YAP into the nucleus for cell proliferation and cancer development.
Review
Hong, Singapore, Singapore. In Sci Signal, 2013
Scaffold proteins angiomotin (Amot) and angiomotin-related AmotL1 and AmotL2 were recently identified as negative regulators of YAP and TAZ by preventing their nuclear translocation.
The role of tumor necrosis factor-α and interferon-γ in regulating angiomotin-like protein 1 expression in lung microvascular endothelial cells.
Yamauchi et al., Japan. In Allergol Int, 2013
Angiomotin-like protein 1 (AmotL1) is involved in angiogenesis via regulating endothelial cell function.
The Amotl2 gene inhibits Wnt/β-catenin signaling and regulates embryonic development in zebrafish.
Meng et al., Beijing, China. In J Biol Chem, 2012
Overexpression of amotl2 in masterblind (mbl) homozygous embryos, in which canonical Wnt signaling is up-regulated due to an axin1 mutation, transforms eyeless phenotype into smaller eyes, whereas co-knockdown of amot, amotl1, and amotl2 leads to development of smaller eyes in mbl heterozygotes.
Opposing roles of angiomotin-like-1 and zona occludens-2 on pro-apoptotic function of YAP.
GeneRIF
Sudol et al., United States. In Oncogene, 2012
AmotL1 and ZO-2 are two candidates that could be harnessed to control the oncogenic function of YAP.
YAP1 recruits c-Abl to protect angiomotin-like 1 from Nedd4-mediated degradation.
Walz et al., Freiburg, Germany. In Plos One, 2011
METHODOLOGY/PRINCIPAL FINDINGS: The present study demonstrates that the E3 ubiquitin ligase Nedd4.2 targets Angiomotin-like 1 (AMOTL1), a family member that promotes the formation of epithelial tight junctions, for ubiquitin-dependent degradation.
Differential expression of the motin family in the peri-implantation mouse uterus and their hormonal regulation.
Daikoku et al., Utsunomiya, Japan. In J Reprod Dev, 2011
There are two other members of the motin family, angiomotin-like 1 and 2 (Amotl1 and 2), which are also thought to be involved with angiogenesis.
Pdlim2 is a novel actin-regulating protein of podocyte foot processes.
Patrakka et al., Stockholm, Sweden. In Kidney Int, 2011
Mechanistically, pdlim2 interacts with two actin-associated podocyte proteins, α-actinin-4 and angiomotin-like-1, as shown by immunoprecipitation and yeast two-hybrid analyses.
Hippo pathway-independent restriction of TAZ and YAP by angiomotin.
Hong et al., Singapore, Singapore. In J Biol Chem, 2011
In this report, we describe an independent mechanism for the cell to restrict the activity of TAZ and YAP through interaction with angiomotin (Amot) and angiomotin-like 1 (AmotL1).
PIV5 M protein interaction with host protein angiomotin-like 1.
GeneRIF
Schmitt et al., United States. In Virology, 2010
By yeast two-hybrid screening, angiomotin-like 1 (AmotL1) was identified as a host factor that interacts with the M protein of parainfluenza virus 5 (PIV5).
Human angiomotin-like 1 associates with an angiomotin protein complex through its coiled-coil domain and induces the remodeling of the actin cytoskeleton.
GeneRIF
Fernandes et al., Québec, Canada. In Cell Motil Cytoskeleton, 2009
The angiomotin-like 1 is involved in actin-cytoskeleton-based processes, in part, via its interaction with a p80-angiomotin-containing complex and the actin cytoskeleton
Angiomotin-like protein 1 controls endothelial polarity and junction stability during sprouting angiogenesis.
GeneRIF
Holmgren et al., Stockholm, Sweden. In Circ Res, 2009
Amot and AmotL1 have similar effects on endothelial migration and tight junction formation in vitro. In vivo Amot appears to control the cell polarity and AmotL1 affects the stability of cell-cell junctions.
The Amot/Patj/Syx signaling complex spatially controls RhoA GTPase activity in migrating endothelial cells.
Holmgren et al., Stockholm, Sweden. In Blood, 2009
Here we have used peptide pull-down and yeast 2-hybrid (Y2H) screening to identify proteins that interact with the C-terminal PDZ-binding motifs of Amot and its related proteins AmotL1 and 2. We report that Amot and its related proteins bind to the RhoA GTPase exchange factor (RhoGEF) protein Syx.
Molecular characterization of angiomotin/JEAP family proteins: interaction with MUPP1/Patj and their endogenous properties.
GeneRIF
Tsukita et al., Kyoto, Japan. In Genes Cells, 2007
Data show that MUPP1 interacts with angiomotin (Amot), JEAP/Amot-like 1 and MASCOT/Amot-like 2, and that all the Amot/JEAP family proteins also interacted with Patj, a close relative of MUPP1.
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