期刊
MOLECULAR MEMBRANE BIOLOGY
卷 26, 期 1-2, 页码 32-41出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/09687680802629329
关键词
APT1; palmitoylation; protein acyl thioesterase; protein acyl transferase; S-acylation
资金
- UK Medical Research Council
- Biotechnology and Biological Sciences Research Council
- Medical Research Council [G0400710] Funding Source: researchfish
- MRC [G0400710] Funding Source: UKRI
Many proteins are S-acylated, affecting their localization and function. Dynamic S-acylation in response to various stimuli has been seen for several proteins in vivo. The regulation of S-acylation is beginning to be elucidated. Proteins can autoacylate or be S-acylated by protein acyl transferases (PATs). Deacylation, on the other hand, is an enzymatic process catalyzed by protein thioesterases (APT1 and PPT1) but only APT1 appears to be involved in the regulation of the reversible S-acylation of cytoplasmic proteins seen in vivo. PPT1, on the other hand, is involved in the lysosomal degradation of S-acylated proteins and PPT1 deficiency causes the disease infant neuronal ceroid lipofuscinosis.
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