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Le, Hoang

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Le, Hoang

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Author's Publications: search.filters.isAuthorOfPublication.6fa817ab-9783-40a4-8e7a-536e58da0ec4

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    ARD1-mediated aurora kinase A acetylation promotes cell proliferation and migration
    (Impact Journals LLC, 2017) Vo, Tam Thuy Lu; Park, Ji-Hyeon; Seo, Ji Hae; Lee, Eun Ji; Choi, Hoon; Bae, Sung-Jin; Le, Hoang; An, Sunho; Lee, Hye Shin; Wee, Hee-Jun; Kim, Kyu-Won
    Aurora kinase A (AuA) is a prerequisite for centrosome maturation, separation, and mitotic spindle assembly, thus, it is essential for cell cycle regulation. Overexpression of AuA is implicated in poor prognosis of many types of cancer. However, the regulatory mechanisms underlying the functions of AuA are still not fully understood. Here, we report that AuA colocalizes with arrest defective protein 1 (ARD1) acetyltransferase during cell division and cell migration. Additionally, AuA is acetylated by ARD1 at lysine residues at positions 75 and 125. The double mutations at K75/K125 abolished the kinase activity of AuA. Moreover, the double mutant AuA exhibited diminished ability to promote cell proliferation and cell migration. Mechanistic studies revealed that AuA acetylation at K75/K125 promoted cell proliferation via activation of cyclin E/CDK2 and cyclin B1. In addition, AuA acetylation stimulated cell migration by activating the p38/AKT/MMP-2 pathway. Our findings indicate that ARD1-mediated acetylation of AuA enhances cell proliferation and migration, and probably contributes to cancer development.
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    SAMHD1 acetylation enhances its deoxynucleotide triphosphohydrolase activity and promotes cancer cell proliferation
    (Impact Journals LLC, 2017) Lee, Eun Ji; Seo, Ji Hae; Park, Ji-Hyeon; Vo, Tam Thuy Lu; An, Sunho; Bae, Sung-Jin; Le, Hoang; Lee, Hye Shin; Wee, Hee-Jun; Lee, Danbi; Chung, Young-Hwa; Kim, Jeong A.; Jang, Myoung-Kuk; Ryu, Soo Hyung; Yu, Ensil; Jang, Se Hwan; Park, Zee Yong; Kim, Kyu-Won
    SAM domain and HD domain containing protein 1 (SAMHD1) is a deoxynucleotide triphosphohydrolase (dNTPase) that inhibits retroviruses by depleting intracellular deoxynucleotide triphosphates (dNTPs) in non-cycling myeloid cells. Although SAMHD1 is expressed ubiquitously throughout the human body, the molecular mechanisms regulating its enzymatic activity and function in non-immune cells are relatively unexplored. Here, we demonstrate that the dNTPase activity of SAMHD1 is regulated by acetylation, which promotes cell cycle progression in cancer cells. SAMHD1 is acetylated at residue lysine 405 (K405) in vitro and in vivo by an acetylatransferase, arrest defective protein 1 (ARD1). Acetylated SAMHD1 wildtype proteins have enhanced dNTPase activity in vitro, whereas non-acetylated arginine substituted mutants (K405R) do not. K405R mutant expressing cancer cells have reduced G1/S transition and slower proliferation compared to wildtype. SAMHD1 acetylation levels are strongest during the G1 phase, indicating a role during G1 phase. Collectively, these findings suggest that SAMHD1 acetylation enhances its dNTPase activity and promotes cancer cell proliferation. Therefore, SAMHD1 acetylation may be a potent therapeutic target for cancer treatment.