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Characterizations of Protein Arginine Deiminase 1 as a Substrate of NTMT1: Implications of Nα-Methylation in Protein Stability and Interaction.
Meng, Ying; Li, Zhouxian; He, Ming; Zhang, Quanqing; Deng, Youchao; Wang, Yinsheng; Huang, Rong.
Afiliación
  • Meng Y; Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
  • Li Z; Department of Chemistry, University of California Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
  • He M; Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
  • Zhang Q; Department of Chemistry, University of California Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
  • Deng Y; Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
  • Wang Y; Department of Chemistry, University of California Riverside, 501 Big Springs Road, Riverside, California 92521, United States.
  • Huang R; Borch Department of Medicinal Chemistry and Molecular Pharmacology, Purdue Institute for Drug Discovery, Purdue University Center for Cancer Research, Purdue University, 720 Clinic Drive, West Lafayette, Indiana 47907, United States.
J Proteome Res ; 2024 Sep 17.
Article en En | MEDLINE | ID: mdl-39287128
ABSTRACT
α-N-Methylation (Nα-methylation), catalyzed by protein N-terminal methyltransferases (NTMTs), constitutes a crucial post-translational modification involving the transfer of a methyl group from S-adenosyl-l-methionine (SAM) to the Nα-terminal amino group of substrate proteins. NTMT1/2 are known to methylate canonical Nα sequences, such as X-P-K/R. With over 300 potential human protein substrates, only a small fraction has been validated, and even less is known about the functions of Nα-methylation. This study delves into the characterizations of protein arginine deiminase 1 (PAD1) as a substrate of NTMT1. By employing biochemical and cellular assays, we demonstrated NTMT1-mediated Nα-methylation of PAD1, leading to an increase in protein half-life and the modulation of protein-protein interactions in HEK293T cells. The methylation of PAD1 appears nonessential to its enzymatic activity or cellular localization. Proteomic studies revealed differential protein interactions between unmethylated and Nα-methylated PAD1, suggesting a regulatory role for Nα-methylation in modulating PAD1's protein-protein interactions. These findings shed light on the intricate molecular mechanisms governing PAD1 function and expand our knowledge of Nα-methylation in regulating protein function.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Proteome Res Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: J Proteome Res Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos