LATS kinase activity and tumor suppressor function are regulated by a second autophosphorylation site.

Ruxin Jin, Zhenxing Zhong, Rui Zhu, Anlan Zhang, Jian Li, Fa-Xing Yu, Yu Wang

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

7 authors.

Ruxin JinInstitute of Pediatrics, Children's Hospital of Fudan University, Qidong-Fudan Innovative Institution of Medical Sciences, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, China.

Zhenxing ZhongInstitute of Pediatrics, Children's Hospital of Fudan University, Qidong-Fudan Innovative Institution of Medical Sciences, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, China.

Rui ZhuInstitute of Pediatrics, Children's Hospital of Fudan University, Qidong-Fudan Innovative Institution of Medical Sciences, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, China.

Anlan ZhangInstitute of Pediatrics, Children's Hospital of Fudan University, Qidong-Fudan Innovative Institution of Medical Sciences, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, China.

Jian LiInstitute of Pediatrics, Children's Hospital of Fudan University, Qidong-Fudan Innovative Institution of Medical Sciences, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, China.

Fa-Xing YuInstitute of Pediatrics, Children's Hospital of Fudan University, Qidong-Fudan Innovative Institution of Medical Sciences, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, China. Electronic address: fxyu@fudan.edu.cn.

Yu WangInstitute of Pediatrics, Children's Hospital of Fudan University, Qidong-Fudan Innovative Institution of Medical Sciences, and Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, China. Electronic address: fd_wangyu@fudan.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hippo signaling pathway regulates cell proliferation, differentiation, and survival. LATS kinases (LATS1 and LATS2) are central kinases in this pathway, activated by MST/MAP4Ks through phosphorylation at the hydrophobic motif, which primes subsequent autophosphorylation at the activation loop. Here, we identify a conserved autophosphorylation site (Ser872 in LATS1 and Ser835 in LATS2) within a canonical HXRXXS motif of the kinase domain, designated as the canonical LATS1/2 substrate site. Phosphorylation at the canonical LATS1/2 substrate site is required for the full activation of LATS kinases, as substitution of this serine with alanine significantly impairs YAP phosphorylation, thereby enhancing the oncogenic activity of YAP, a key downstream effector of LATS kinases. These results provide new mechanistic insights into the regulation of LATS kinase activity and the biological function of the Hippo pathway.

Indexed as

Protein Serine-Threonine KinasesTumor Suppressor ProteinsAnimalsHumansPhosphorylationSignal TransductionLATS1 protein, humanLATS2 protein, humanProtein Serine-Threonine KinasesTumor Suppressor Proteinsactivation loopautophosphorylationcanonical LATS1/2 substrate siteHippo signaling pathwayhydrophobic motifkinase activityLATS1/2YAP/TAZ

Identifiers

PMID42167578

DOI10.1016/j.jbc.2026.113177

PMCPMC13292594

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.