KSR1 is a scaffold for the Hippo signaling pathway

The evolutionarily conserved Hippo signaling pathway regulates organ size and tissue homeostasis. Yes-associated protein (YAP) functions as a transcriptional co-activator and is a critical downstream effector of the Hippo signaling pathway. Altered crosstalk with oncogenic signaling pathways contributes to YAP dysregulation in cancer. Kinase Suppressor of Ras 1 (KSR1) scaffolds the Ras cascade. Some of the functions of the Ras and Hippo pathways in regulating cellular processes are similar. Nevertheless, the potential intersection of Ras and Hippo signaling has not been explored. Here, we identify KSR1 as a previously unrecognized scaffold of the Hippo pathway. We demonstrate that KSR1 constitutively binds to YAP and MST1 and forms a complex with LATS1. Moreover, KSR1 modulates YAP protein levels and its transcriptional activity, at least in part through the RhoA/actin axis. Our findings provide insight into the role of KSR1 as a scaffold of the Hippo signaling that could yield novel therapeutics.

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Journal
Communications Biology
Published
2025-12-01
DOI
https://doi.org/10.1038/s42003-025-09009-4
Primary Topic
Hippo pathway signaling and YAP/TAZ
Type
article
Field-Weighted Citation Impact
0.00

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article

KSR1 is a scaffold for the Hippo signaling pathway

David B. Sacks, Pooya Borzou, Andy D. Tran, Louise Thines et al.
Communications Biology
Hippo pathway signaling and YAP/TAZ
article

KSR1 is a scaffold for the Hippo signaling pathway

David B. Sacks, Pooya Borzou, Andy D. Tran, Louise Thines, Samar Sayedyahossein, Zhigang Li, Riddhi Banerjee, Mehrnoosh Bahmani, Sergio A. Hassan, Mehdi Karimi, Mohammed Rizwan Babu Sait, Naomi Mishan
article en

Abstract

The evolutionarily conserved Hippo signaling pathway regulates organ size and tissue homeostasis. Yes-associated protein (YAP) functions as a transcriptional co-activator and is a critical downstream effector of the Hippo signaling pathway. Altered crosstalk with oncogenic signaling pathways contributes to YAP dysregulation in cancer. Kinase Suppressor of Ras 1 (KSR1) scaffolds the Ras cascade. Some of the functions of the Ras and Hippo pathways in regulating cellular processes are similar. Nevertheless, the potential intersection of Ras and Hippo signaling has not been explored. Here, we identify KSR1 as a previously unrecognized scaffold of the Hippo pathway. We demonstrate that KSR1 constitutively binds to YAP and MST1 and forms a complex with LATS1. Moreover, KSR1 modulates YAP protein levels and its transcriptional activity, at least in part through the RhoA/actin axis. Our findings provide insight into the role of KSR1 as a scaffold of the Hippo signaling that could yield novel therapeutics.

Communications BiologyVol. 8(1)
Western University (CA), National Institutes of Health (US), Isfahan University of Technology (IR), National Institute of Allergy and Infectious Diseases (US), Illinois State University (US)
U.S. Department of Health and Human Services, National Institutes of Health
Openalex Percentile: Top 61%
Hippo pathway signaling and YAP/TAZ
DOIOpen Access PDFOpenAlex
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