Please use this identifier to cite or link to this item:
https://doi.org/10.3390/cancers10020045
DC Field | Value | |
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dc.title | Linking extracellular matrix agrin to the hippo pathway in liver cancer and beyond | |
dc.contributor.author | Chakraborty, S | |
dc.contributor.author | Hong, W | |
dc.date.accessioned | 2020-10-20T08:56:54Z | |
dc.date.available | 2020-10-20T08:56:54Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Chakraborty, S, Hong, W (2018). Linking extracellular matrix agrin to the hippo pathway in liver cancer and beyond. Cancers 10 (2) : 45. ScholarBank@NUS Repository. https://doi.org/10.3390/cancers10020045 | |
dc.identifier.issn | 20726694 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/178261 | |
dc.description.abstract | In addition to the structural and scaffolding role, the extracellular matrix (ECM) is emerging as a hub for biomechanical signal transduction that is frequently relayed to intracellular sensors to regulate diverse cellular processes. At a macroscopic scale, matrix rigidity confers long-ranging effects contributing towards tissue fibrosis and cancer. The transcriptional co-activators YAP/TAZ, better known as the converging effectors of the Hippo pathway, are widely recognized for their new role as nuclear mechanosensors during organ homeostasis and cancer. Still, how YAP/TAZ senses these “stiffness cues” from the ECM remains enigmatic. Here, we highlight the recent perspectives on the role of agrin in mechanosignaling from the ECM via antagonizing the Hippo pathway to activate YAP/TAZ in the contexts of cancer, neuromuscular junctions, and cardiac regeneration. © 2018 by the authors. Licensee MDPI, Basel, Switzerland. | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20201031 | |
dc.subject | agrin | |
dc.subject | focal adhesion kinase | |
dc.subject | glypican 3 | |
dc.subject | Hippo protein | |
dc.subject | integrin linked kinase | |
dc.subject | p21 activated kinase 1 | |
dc.subject | protein TAZ | |
dc.subject | protein YAP | |
dc.subject | transcription factor | |
dc.subject | transcription factor Yap1 | |
dc.subject | unclassified drug | |
dc.subject | cancer growth | |
dc.subject | cell spreading | |
dc.subject | extracellular matrix | |
dc.subject | focal adhesion | |
dc.subject | gene deletion | |
dc.subject | hippo signaling | |
dc.subject | human | |
dc.subject | liver cancer | |
dc.subject | liver carcinogenesis | |
dc.subject | liver cell carcinoma | |
dc.subject | mechanotransduction | |
dc.subject | nonhuman | |
dc.subject | pathophysiology | |
dc.subject | protein function | |
dc.subject | protein localization | |
dc.subject | protein stability | |
dc.subject | Review | |
dc.subject | transcription initiation | |
dc.type | Review | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.3390/cancers10020045 | |
dc.description.sourcetitle | Cancers | |
dc.description.volume | 10 | |
dc.description.issue | 2 | |
dc.description.page | 45 | |
Appears in Collections: | Elements Staff Publications |
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