| First Author | Elbediwy A | Year | 2018 |
| Journal | J Cell Sci | Volume | 131 |
| Issue | 22 | PubMed ID | 30404826 |
| Mgi Jnum | J:267346 | Mgi Id | MGI:6259002 |
| Doi | 10.1242/jcs.221788 | Citation | Elbediwy A, et al. (2018) Enigma proteins regulate YAP mechanotransduction. J Cell Sci 131(22):jcs221788 |
| abstractText | Human cells can sense mechanical stress acting upon integrin adhesions and respond by sending the YAP (also known as YAP1) and TAZ (also known as WWTR1) transcriptional co-activators to the nucleus to drive TEAD-dependent transcription of target genes. How integrin signaling activates YAP remains unclear. Here, we show that integrin-mediated mechanotransduction requires the Enigma and Enigma-like proteins (PDLIM7 and PDLIM5, respectively; denoted for the family of PDZ and LIM domain-containing proteins). YAP binds to PDLIM5 and PDLIM7 (hereafter PDLIM5/7) via its C-terminal PDZ-binding motif (PBM), which is essential for full nuclear localization and activity of YAP. Accordingly, silencing of PDLIM5/7 expression reduces YAP nuclear localization, tyrosine phosphorylation and transcriptional activity. The PDLIM5/7 proteins are recruited from the cytoplasm to integrin adhesions and F-actin stress fibers in response to force by binding directly to the key stress fiber component alpha-actinin. Thus, forces acting on integrins recruit Enigma family proteins to trigger YAP activation during mechanotransduction.This article has an associated First Person interview with the first author of the paper. |
