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The Structure, Activity, and Function of the SETD3 Protein Histidine Methyltransferase
Apolonia Witecka1, Sebastian Kwiatkowski1, Takao Ishikawa2
1Department of Metabolic Regulation, Institute of Biochemistry, Faculty of Biology, University of Warsaw, Miecznikowa 1, 02-096 Warsaw, Poland.
Life (Basel, Switzerland)
|October 23, 2021
Summary
SETD3 is an actin-specific methyltransferase that modifies histidine 73 (H73) in actin, crucial for cytoskeleton integrity. While initially thought to modify histones, SETD3
Area of Science:
- Biochemistry and Molecular Biology
- Cell Biology
- Enzymology
Background:
- SETD3 is identified as a specific histidine methyltransferase targeting actin.
- It catalyzes the Nτ-methylation of histidine 73 (H73) in actin.
- SETD3 possesses a SET domain for catalysis and a RuBisCO LSMT domain for substrate recognition.
Purpose of the Study:
- To review current research on the SETD3 protein.
- To elucidate the biological importance and functions of SETD3.
- To explore the role of SETD3 in various disease pathologies.
Main Methods:
- Literature review of existing studies on SETD3.
- Analysis of biochemical and cellular data related to SETD3 activity.
- Examination of genetic and proteomic information regarding SETD3 interactors.
Main Results:
- SETD3's primary substrate is actin H73, essential for cytoskeleton integrity.
- Previous findings of SETD3 acting on histone H3 are now considered inaccurate.
- Numerous novel interactors suggest broader roles in cell cycle, apoptosis, and disease.
Conclusions:
- SETD3 is a key regulator of actin methylation and cytoskeleton maintenance.
- Emerging evidence points to SETD3's involvement in diverse cellular processes and diseases.
- Further research is warranted to fully understand SETD3's multifaceted biological roles.
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