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Phosphopeptide mass spectrometry analysis of LATS2 identifies a second autophosphorylation site in HEK293A cells

ABSTRACT: This dataset contains phosphopeptide LC-MS/MS data generated from human LATS2 overexpressed in HEK293A cells. The study was designed to identify LATS2 phosphorylation sites and to support phosphopeptide mapping of LATS2 autophosphorylation, with particular attention to the kinase-domain CLS site. Immunoprecipitated LATS2 samples were digested and analyzed by nanoLC-MS/MS.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: 茹炘靳

LAB HEAD: Ruxin Jin

PROVIDER: PXD076693 | Pride | 2026-06-29

REPOSITORIES: Pride

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Publications

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

Jin Ruxin R Zhong Zhenxing Z Zhu Rui R Zhang Anlan A Li Jian J Yu Fa-Xing FX Wang Yu Y

The Journal of biological chemistry 20260520 7

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. Ph ...[more]

PMID: 42167578

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