AMOTL1
- Known as:
- AMOTL1
- Catalog number:
- 001535A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- AMOTL1
Related genes to: AMOTL1
- Gene:
- AMOTL1 NIH gene
- Name:
- angiomotin like 1
- Previous symbol:
- -
- Synonyms:
- JEAP
- Chromosome:
- 11q21
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-24
- Date modifiied:
- 2015-10-15
Related products to: AMOTL1
Related articles to: AMOTL1
- Predicting mortality in sepsis patients remains a challenge in clinical settings. This study aimed to identify genes associated with sepsis-related mortality and determine the predictive value of a model using these death-related genes. - Source: PubMed
Publication date: 2026/08/12
Bai YulongXu YubiaoTan ShihuiHuang YishengHuang XiaoxiangFu Zhaoyin - Severe steroid-resistant asthma (SSRA) is frequently associated with irreversible airway remodeling (AR), which contributes to persistent airflow limitation and poor therapeutic responsiveness. Celastrol (CEL) exhibits anti-inflammatory and tissue-protective properties; however, its role in steroid-resistant AR remains unclear. - Source: PubMed
Publication date: 2026/06/29
Sun JialiangLiu ZiyuZhang YingZhang YanqiuZhao PeiliangLi Yanan - Angiomotin-like 1 (AMOTL1), by regulating cell-cell junctions, cell polarity, and cell migration, plays a critical role in organogenesis and development. Recently, multiple studies have identified two hotspot mutations in AMOTL1, Arg157 (R157) and Pro160 (P160), in more than ten distinct families presenting with a spectrum of congenital defects, including facial dysmorphisms and cardiac abnormalities. However, the underlying pathogenic mechanism remains elusive. R157 and P160 are located in the highly conserved Tankyrase-binding motif (TBM) of AMOTL1. Here, we show that both the R157C and P160L mutants fail to interact with Tankyrase 1/2 and Ring finger protein 146, rendering them unable to undergo poly ADP-ribosylation, ubiquitination, and subsequent proteasomal degradation. As a result, these mutants are significantly stabilized and accumulate in the cytoplasm. Accumulated AMOTL1 mutants, in turn, disrupt cell junctions and focal adhesions, thereby inhibiting both the velocity and persistence of cell migration. Furthermore, during zebrafish embryonic development, expression of the R157C mutant leads to craniofacial malformations and defects in cardiac function and skeletal muscle. Our study confirms the role of AMOTL1 mutations in tissue development and uncovers the pathogenic mechanism at both molecular and cellular levels. - Source: PubMed
Luo JiaqianJin RuxinGeng FangWang YunyingZhu YuwenGao WenqiangGao WeiLi JianJiu YamingZhang RuilinYu Fa-XingWang Yu - Aerobic glycolysis drives cancer progression through phosphofructokinase (PFK)-mediated regulation. The contribution of platelet-type PFK (PFKP) to head and neck squamous cell carcinoma (HNSCC) pathogenesis remains undefined. - Source: PubMed
Publication date: 2026/02/13
Wang LingwaLi HaiyangYang YifanShi QianFeng LingWang RuFang Jugao - The Hippo signaling pathway regulates the homeostatic balance between cell growth and apoptosis through intricate networks of multivalent protein complexes. How multivalency modulates the assembly and stability of these protein complexes remains poorly understood. Here, we show that Angiomotin-like 1 (AMOTL1), a scaffold protein containing three PPxY motifs, employs distinct cooperative binding mechanisms to engage two WW domain-containing partners: NEDD4-1, which promotes AMOTL1 degradation, and KIBRA, which protects AMOTL1 from degradation. Using quantitative molecular biophysical analyses, including isothermal titration calorimetry and nuclear magnetic resonance spectroscopy, we demonstrate that AMOTL1 forms a cooperatively stabilized complex with NEDD4-1 through simultaneous engagement of all three PPxY motifs with three of the four NEDD4-1 WW domains. This cooperative binding mode produces approximately ten-fold enhancement in affinity compared to the primary anchor interaction alone. In contrast, KIBRA engages AMOTL1 primarily through high-affinity binding at the C-terminal PPxY motif, with transient secondary interactions at the other PPxY sites that do not enhance overall binding strength. These contrasting mechanisms demonstrate that multivalency within the Hippo pathway serves as a tunable regulatory feature, where cooperative interactions can either enhance or minimally contribute to binding strength, explaining how a single scaffold protein can be differentially regulated to achieve opposing functional outcomes. - Source: PubMed
Publication date: 2026/01/22
Vogel AmberMcWhorter MatthewKwok EthieneNyarko Afua