| Autor: |
Malgapo MIP; Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA., Linder ME; Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY, USA. |
| Jazyk: |
angličtina |
| Zdroj: |
Open biology [Open Biol] 2021 Apr; Vol. 11 (4), pp. 210026. Date of Electronic Publication: 2021 Apr 21. |
| DOI: |
10.1098/rsob.210026 |
| Abstrakt: |
Protein palmitoylation is the post-translational attachment of fatty acids, most commonly palmitate (C16 : 0), onto a cysteine residue of a protein. This reaction is catalysed by a family of integral membrane proteins, the zDHHC protein acyltransferases (PATs), so-called due to the presence of an invariant Asp-His-His-Cys (DHHC) cysteine-rich domain harbouring the catalytic centre of the enzyme. Conserved throughout eukaryotes, the zDHHC PATs are encoded by multigene families and mediate palmitoylation of thousands of protein substrates. In humans, a number of zDHHC proteins are associated with human diseases, including intellectual disability, Huntington's disease, schizophrenia and cancer. Key to understanding the physiological and pathophysiological importance of individual zDHHC proteins is the identification of their protein substrates. Here, we will describe the approaches and challenges in assigning substrates for individual zDHHCs, highlighting key mechanisms that underlie substrate recruitment. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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