Proteomics

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Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness


ABSTRACT: O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT). Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharac-terized. Here we report our comparative O-GlcNAc proteome profiling of 2 differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated can-didates in highly invasive cells. Among these differential proteins, a nuclear RNA-binding protein SAM68 (SRC associated in mitosis of 68 kDa) was further investigated. Results showed that SAM68 is O-GlcNAcylated and may interact with OGT in the nucleus. Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion. Analysis of clinical specimens found that high SAM68 ex-pression was associated with late cancer stages, and patients with high-OGT/high-SAM68 ex-pression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression. Our study has revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Lung

SUBMITTER: Chen-Chung Liao  

LAB HEAD: Chen-Chung Liao

PROVIDER: PXD029627 | Pride | 2022-02-17

REPOSITORIES: Pride

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Comparative <i>O</i>-GlcNAc Proteomic Analysis Reveals a Role of <i>O</i>-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.

Lin Chia-Hung CH   Liao Chen-Chung CC   Wang Shu-Ying SY   Peng Chia-Yi CY   Yeh Yi-Chen YC   Chen Mei-Yu MY   Chou Teh-Ying TY  

Cancers 20220104 1


<i>O</i>-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by <i>O</i>-GlcNAc transferase (OGT). Despite the reported association of <i>O</i>-GlcNAcylation with cancer metastasis, the <i>O</i>-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized. Here, we report our comparative <i>O</i>-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regul  ...[more]

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